|
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: 1145.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 22 VVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFYRQLS 101
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 102 RQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTQISWQLTVLALIPMPLMAIAIKYYGDQ 181
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 182 LHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNLLAIG 261
Cdd:PRK10789 161 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 262 GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSLLNEAPAVQDGPQALPAGRGVLEVDIRA 341
Cdd:PRK10789 241 GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFL 421
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 502 AVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQQLEAALDEAP 581
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDAP 560
|
....*....
gi 1574033397 582 ENGEEALAD 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: 610.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 1 MRLFAQIGWYFRREWRRYLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYLLRYVWRVL 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 81 LFGASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTqISWQL 160
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV-IDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 161 TVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARV 240
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 241 DARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSLLNEAPA 320
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 321 VQDGPQA--LPAGRGVLEVDIRAFHYPENpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGL 398
Cdd:COG1132 324 IPDPPGAvpLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 399 PLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQK 478
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 479 QRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALA 558
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
570
....*....|....*..
gi 1574033397 559 AQPGWYRDMYRYQQLEA 575
Cdd:COG1132 563 ARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
10-572 |
1.23e-136 |
|
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: 414.23 E-value: 1.23e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 10 YFRREWRRYLGAVVLLIVIAILQLLPPKLVGIIVDGV-TEKQMSTGVLLAwlGLMIGTAIVVYLLRYVWRVLLFGASYQL 88
Cdd:COG2274 150 LLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVlPNQDLSTLWVLA--IGLLLALLFEGLLRLLRSYLLLRLGQRI 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 89 AVELRENFYRQLSRQNPAFYLRHRTGDLMARAtNDVDRVV-FAAGEGVLTLVDSLVMGLVVLVVMStqISWQLTVLALIP 167
Cdd:COG2274 228 DLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIReFLTGSLLTALLDLLFVLIFLIVLFF--YSPPLALVVLLL 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 168 MPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPT 247
Cdd:COG2274 305 IPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 248 IYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSLLNEAPAVQDG--P 325
Cdd:COG2274 385 SGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGrsK 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 326 QALPAGRGVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRL 405
Cdd:COG2274 465 LSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 406 DDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIAR 485
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIAR 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 486 ALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYR 565
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
....*..
gi 1574033397 566 DMYRYQQ 572
Cdd:COG2274 705 ELVQQQL 711
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
18-311 |
1.63e-123 |
|
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: 365.58 E-value: 1.63e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 18 YLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFY 97
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 98 RQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVmSTQISWQLTVLALIPMPLMAIAIKY 177
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVM-MFTISPKLTLIALLPLPLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 178 YGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNL 257
Cdd:cd18541 160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 258 LAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 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 |
2.77e-106 |
|
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: 331.30 E-value: 2.77e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 1 MRLFAqigwYFRREWRRYLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQmsTGVLLAWLGLM-IGTAIVVYLLRYVWRV 79
Cdd:TIGR02203 3 RRLWS----YVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGR--DRSVLWWVPLVvIGLAVLRGICSFVSTY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 80 LLFGASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAgEGVLTLVDSLVMGLVVLVVMSTQISWQ 159
Cdd:TIGR02203 77 LLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAA-TDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 160 LTVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVAR 239
Cdd:TIGR02203 156 LTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 240 VDARFDPTI--YIAIGASNLLAIGGgsWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSLLNE 317
Cdd:TIGR02203 236 AGSISSPITqlIASLALAVVLFIAL--FQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 318 APAVQDGPQALPAGRGVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG 397
Cdd:TIGR02203 314 PPEKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 398 LPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPG-ATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGG 476
Cdd:TIGR02203 394 HDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 477 QKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAA 556
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
570
....*....|....*
gi 1574033397 557 LAAQPGWYRDMYRYQ 571
Cdd:TIGR02203 554 LLARNGLYAQLHNMQ 568
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
9-571 |
1.04e-101 |
|
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: 319.72 E-value: 1.04e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 9 WYFRREWR-RYLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMS-------TGVLLAWLGLMIGTAIVVYLlryvwrVL 80
Cdd:TIGR02204 10 WPFVRPYRgRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSgllnryfAFLLVVALVLALGTAARFYL------VT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 81 LFGAsyQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGV-------LTLVDSLVMGLVvlvvms 153
Cdd:TIGR02204 84 WLGE--RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLsmalrnaLMCIGGLIMMFI------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 154 tqISWQLTVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQtgAK 233
Cdd:TIGR02204 156 --TSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEK--AY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 234 NMHVARVDARFDPT---IYIAIGASNLLAIGGGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSR 310
Cdd:TIGR02204 232 EAARQRIRTRALLTaivIVLVFGAIVGVLWVGAH-DVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 311 IRSLLNEAPAVQ--DGPQALPA-GRGVLEVDIRAFHYPENP-HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQF 386
Cdd:TIGR02204 311 LIELLQAEPDIKapAHPKTLPVpLRGEIEFEQVNFAYPARPdQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 387 DVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEV 466
Cdd:TIGR02204 391 DPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 467 GERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHG 546
Cdd:TIGR02204 471 GERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQG 550
|
570 580
....*....|....*....|....*
gi 1574033397 547 GVAQRGDPAALAAQPGWYRDMYRYQ 571
Cdd:TIGR02204 551 RIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
9-569 |
3.86e-100 |
|
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: 315.17 E-value: 3.86e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 9 WYFRREWRRYLGAVVLLIVIAILQLLppklvgiivdgvtekqMSTGvLLA---WL---------GLMIGTAIVVY----- 71
Cdd:COG4987 4 LRLLRLLRPHRGRLLLGVLLGLLTLL----------------AGIG-LLAlsgWLiaaaalappILNLFVPIVGVrafai 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 72 ---LLRYVWRVLLFGASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVD-------RVVFAAGEGVLTLVds 141
Cdd:COG4987 67 grtVFRYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDaldnlylRVLLPLLVALLVIL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 142 lvmglvVLVVMSTQISWQLTVLALIPMPLMAIAIKYYGDQLHQRF-KSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQS 220
Cdd:COG4987 145 ------AAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRRAgRRLAAARAALRARLTDLLQGAAELAAYGALDRAL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 221 NRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMY-LGLM-IWPMLALAWMF 298
Cdd:COG4987 219 ARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAaLALFeALAPLPAAAQH 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 299 niVERGSAAYSRIRSLLNEAPAVQDGPQALPA-GRGVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKST 377
Cdd:COG4987 299 --LGRVRAAARRLNELLDAPPAVTEPAEPAPApGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKST 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 378 LLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILR 457
Cdd:COG4987 377 LLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 458 LPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEA 537
Cdd:COG4987 457 LPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM 536
|
570 580 590
....*....|....*....|....*....|..
gi 1574033397 538 SEILVMQHGGVAQRGDPAALAAQPGWYRDMYR 569
Cdd:COG4987 537 DRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
16-562 |
1.50e-98 |
|
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: 310.92 E-value: 1.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLLIVIA----ILQLLppkLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVE 91
Cdd:COG4988 16 RRWLALAVLLGLLSglliIAQAW---LLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 92 LRENFYRQLSRQNPAFYLRHRTGDLMARATNDVD-----------RVVFAAGEGVLTLVdslvmglvvlvvMSTQISWQL 160
Cdd:COG4988 93 LRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEaldgyfarylpQLFLAALVPLLILV------------AVFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 161 TVLALIPMPL----MAIAIKYYGDQLHQRFksaqAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMH 236
Cdd:COG4988 161 GLILLVTAPLiplfMILVGKGAAKASRRQW----RALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 237 VARV--------DarFDPTIYIAIGAsnlLAIGggsWMVVNGSLTLGQltsfvmylGLMIW--------PMLALAWMFNI 300
Cdd:COG4988 237 VLRVaflssavlE--FFASLSIALVA---VYIG---FRLLGGSLTLFA--------ALFVLllapefflPLRDLGSFYHA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 301 VERGSAAYSRIRSLLN-EAPAVQDGPQALPAGRGVlevDIRA----FHYPENPhPALHDLALTLKPGQMLGLCGPTGAGK 375
Cdd:COG4988 301 RANGIAAAEKIFALLDaPEPAAPAGTAPLPAAGPP---SIELedvsFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 376 STLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDI 455
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 456 LRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALT 535
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
570 580
....*....|....*....|....*..
gi 1574033397 536 EASEILVMQHGGVAQRGDPAALAAQPG 562
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
9-582 |
1.08e-93 |
|
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: 299.43 E-value: 1.08e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 9 WYFRREWRRYLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLglmigtaIVVY-LLRYV------WRVLL 81
Cdd:COG5265 29 PPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGL-------LLAYgLLRLLsvlfgeLRDAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 82 FG-----ASYQLAVELrenfYRQLSRQNPAFYLRHRTGDL---MARATNDVD----RVVFAAG----EGVLTLVdslvmg 145
Cdd:COG5265 102 FArvtqrAVRRLALEV----FRHLHALSLRFHLERQTGGLsrdIERGTKGIEfllrFLLFNILptllEIALVAG------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 146 lvvlvVMSTQISWQLTVLALIpMPLMAIAIKYYGDQLHQRF-KSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRF- 223
Cdd:COG5265 172 -----ILLVKYDWWFALITLV-TVVLYIAFTVVVTEWRTKFrREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYd 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 224 --------ADVAAQT--GAKNMHVARVdarfdptIYIAIGASNLLAIGGgswmVVNGSLTLGQltsFVMYLGLMIW---P 290
Cdd:COG5265 246 ealaryerAAVKSQTslALLNFGQALI-------IALGLTAMMLMAAQG----VVAGTMTVGD---FVLVNAYLIQlyiP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 291 MLALAWMFNIVERGSAAYSRIRSLLNEAPAVQDGPQA--LPAGRGVLEVDIRAFHY-PEnpHPALHDLALTLKPGQMLGL 367
Cdd:COG5265 312 LNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAppLVVGGGEVRFENVSFGYdPE--RPILKGVSFEVPAGKTVAI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 368 CGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAAR 447
Cdd:COG5265 390 VGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAAR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 448 LASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIIS 527
Cdd:COG5265 470 AAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVI 549
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 528 AHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQQLEAALDEAPE 582
Cdd:COG5265 550 AHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALA 604
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
342-568 |
1.84e-91 |
|
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: 281.43 E-value: 1.84e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFL 421
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:cd03251 88 FNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 502 AVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMY 568
Cdd:cd03251 168 ALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
10-567 |
2.02e-86 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 283.15 E-value: 2.02e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 10 YFRREWRRYLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQ----MSTGVLLAWLgLMIGTAIVVYLLryvwrvllfGAS 85
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKgppaLASAIFFMCL-LSIASSVSAGLR---------GGS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 86 YQLAVE-----LRENFYRQLSRQNPAFYLRHRTGDLMARATNDV----DRVVFAAGEGVLTLVdslvmGLVVLVVMSTQI 156
Cdd:TIGR00958 225 FNYTMArinlrIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTqtmsRSLSLNVNVLLRNLV-----MLLGLLGFMLWL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 157 SWQLTVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMH 236
Cdd:TIGR00958 300 SPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKR 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 237 VARVDARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSLLN 316
Cdd:TIGR00958 380 KALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLD 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 317 EAPAVQ-DGPQALPAGRGVLEVDIRAFHYPENPH-PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIR 394
Cdd:TIGR00958 460 RKPNIPlTGTLAPLNLEGLIEFQDVSFSYPNRPDvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 395 YHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLS 474
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 475 GGQKQRISIARALLLDAEILILDDALSAVDGRTEhQILHNLRSWGqDRTVIISAHRLSALTEASEILVMQHGGVAQRGDP 554
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECE-QLLQESRSRA-SRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
570
....*....|...
gi 1574033397 555 AALAAQPGWYRDM 567
Cdd:TIGR00958 698 KQLMEDQGCYKHL 710
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
11-571 |
1.59e-85 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 277.67 E-value: 1.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 11 FRREW---RRY----LGAVVLLIVIA-----ILQLLPPKLVgiivDGVTEKQMStgvLLAWLGLMIgtaIVVYLLRYVWR 78
Cdd:PRK11176 13 FRRLWptiAPFkaglIVAGVALILNAasdtfMLSLLKPLLD----DGFGKADRS---VLKWMPLVV---IGLMILRGITS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 79 vllFGASYQLA-------VELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVdslvmglvvlvV 151
Cdd:PRK11176 83 ---FISSYCISwvsgkvvMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVV-----------R 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 152 MSTQI----------SWQLTVLALIPMPLMAIAIKyygdQLHQRF----KSAQAAFSSLNDQAQESMTSIRMIKAFGLED 217
Cdd:PRK11176 149 EGASIiglfimmfyySWQLSLILIVIAPIVSIAIR----VVSKRFrnisKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 218 HQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAigASNLLA--IGGGSWMVVNGSLTLGQLTS-FVMYLGLMiWPMLAL 294
Cdd:PRK11176 225 VETKRFDKVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAfvLYAASFPSVMDTLTAGTITVvFSSMIALM-RPLKSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 295 AWMFNIVERGSAAYSRIRSLLNEAPAVQDGPQALPAGRGVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAG 374
Cdd:PRK11176 302 TNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 375 KSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGA-TQAQIEQAARLASVHE 453
Cdd:PRK11176 382 KSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 454 DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSA 533
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541
|
570 580 590
....*....|....*....|....*....|....*...
gi 1574033397 534 LTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQ 571
Cdd:PRK11176 542 IEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
342-571 |
1.67e-84 |
|
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: 263.25 E-value: 1.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENP-HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPF 420
Cdd:cd03249 8 FRYPSRPdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 LFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:cd03249 88 LFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 501 SAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQ 571
Cdd:cd03249 168 SALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
11-571 |
1.12e-83 |
|
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: 275.47 E-value: 1.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 11 FRREWRRYLGAVVLLIVIAilqLLPPKLVGIIVDGV-TEKQMSTGVLLAwlGLMIGTAIVVYLLRYVWRVLLFGASYQLA 89
Cdd:TIGR01846 137 YRKQFREVLLISLALQLFA---LVTPLLFQVVIDKVlVHRGLSTLSVLA--LAMLAVAIFEPALGGLRTYLFAHLTSRID 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 90 VELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMstQISWQLTVLALIPMP 169
Cdd:TIGR01846 212 VELGARLYRHLLGLPLGYFESRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMF--FYSPTLTGVVIGSLV 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 170 LMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIY 249
Cdd:TIGR01846 290 CYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 250 IAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSLLNE-APAVQDGPQAL 328
Cdd:TIGR01846 370 LIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSpTEPRSAGLAAL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 329 PAGRGVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDW 408
Cdd:TIGR01846 450 PELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 409 RSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALL 488
Cdd:TIGR01846 530 RRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALV 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 489 LDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMY 568
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLW 689
|
...
gi 1574033397 569 RYQ 571
Cdd:TIGR01846 690 QQQ 692
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-571 |
3.95e-82 |
|
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: 257.16 E-value: 3.95e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYpeNPH-PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPF 420
Cdd:cd03253 8 FAY--DPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 LFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:cd03253 86 LFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 501 SAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQ 571
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-587 |
2.91e-75 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 250.65 E-value: 2.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 1 MRLFAQIGWYFRREWRRYLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIV-VYLLRYVWRV 79
Cdd:PRK13657 4 FRLYARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDIFPLLAAWAGFGLFNIIAgVLVARHADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 80 llfgASYQLAVELRENFYRQLsrQNP-AFYLRHRTGDL---MARATN-------DVDRVVFAAGEGVLTLVDslvmglvv 148
Cdd:PRK13657 84 ----AHRRRLAVLTEYFERII--QLPlAWHSQRGSGRAlhtLLRGTDalfglwlEFMREHLATLVALVVLLP-------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 149 lvvMSTQISWQLTVLalipmpLMAIAIKYY--GDQLHQRFKSAQAA----FSSLNDQAQESMTSIRMIKAFGLEDHQSNR 222
Cdd:PRK13657 150 ---LALFMNWRLSLV------LVVLGIVYTliTTLVMRKTKDGQAAveehYHDLFAHVSDAIGNVSVVQSYNRIEAETQA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 223 FADVAAQTGAKNMHV------ARVDARFDPTIYIAIgasnLLAIGggSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAW 296
Cdd:PRK13657 221 LRDIADNLLAAQMPVlswwalASVLNRAASTITMLA----ILVLG--AALVQKGQLRVGEVVAFVGFATLLIGRLDQVVA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 297 MFNIVERGSAAYSRIRSLLNEAPAVQDGPQALPAGR--GVLEVDIRAFHYPeNPHPALHDLALTLKPGQMLGLCGPTGAG 374
Cdd:PRK13657 295 FINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRvkGAVEFDDVSFSYD-NSRQGVEDVSFEAKPGQTVAIVGPTGAG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 375 KSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHED 454
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDF 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 455 ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSAL 534
Cdd:PRK13657 454 IERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTV 533
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 535 TEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQQL--EAALDEAPENGEEA 587
Cdd:PRK13657 534 RNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQGMlqEDERRKQPAAEGAN 588
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
342-562 |
5.74e-73 |
|
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: 233.27 E-value: 5.74e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYpENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFL 421
Cdd:cd03254 10 FSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:cd03254 89 FSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 502 AVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPG 562
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-546 |
1.86e-68 |
|
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: 219.18 E-value: 1.86e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 335 LEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSV 414
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 415 VSQTPFLFSDTVANNIalgqpgatqaqieqaarlasvhedilrlpqgydtevgergvmLSGGQKQRISIARALLLDAEIL 494
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 495 ILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHG 546
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
18-311 |
1.54e-66 |
|
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: 218.45 E-value: 1.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 18 YLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMsTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFY 97
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGL-RELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 98 RQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTqISWQLTVLALIPMPLMAIAIKY 177
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFS-INWKLTLISLAIIPFIALFSYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 178 YGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNL 257
Cdd:cd18542 159 FFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 258 LAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 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 |
5.57e-66 |
|
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: 215.04 E-value: 5.57e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFL 421
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:cd03252 88 FNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 502 AVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQ 571
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-543 |
3.33e-65 |
|
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: 222.16 E-value: 3.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLLIVI-AILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRE 94
Cdd:TIGR02857 2 RRALALLALLGVLgALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 95 NFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTQiSWQLTVLALIPMPLMAIA 174
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQ-DWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 175 IKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVD------ARFDPTI 248
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAflssavLELFATL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 249 YIAIGAsnlLAIGGGswmVVNGSLTLgqLTSFVM-------YLglmiwPMLALAWMFNIVERGSAAYSRIRSLLNEAPAV 321
Cdd:TIGR02857 241 SVALVA---VYIGFR---LLAGDLDL--ATGLFVlllapefYL-----PLRQLGAQYHARADGVAAAEALFAVLDAAPRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 322 -QDGPQALPAGRGVLEVDIRAFHYPENPhPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL 400
Cdd:TIGR02857 308 lAGKAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 401 PQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQR 480
Cdd:TIGR02857 387 ADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQR 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 481 ISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVM 543
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-548 |
1.27e-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: 210.91 E-value: 1.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 333 GVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRL 412
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAE 492
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 493 ILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGV 548
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-568 |
9.17e-63 |
|
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: 219.61 E-value: 9.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 22 VVLLIVIA-----ILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLmIGTAIVVYLLRYVWRVLLFGASYQLAVELRENF 96
Cdd:TIGR01193 157 LIVNIVIAaiivtLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGL-IIAYIIQQILSYIQIFLLNVLGQRLSIDIILSY 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 97 YRQLSRQNPAFYLRHRTGDLMARATnDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTQISwQLTVLALIPMPLMAIAIK 176
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNM-LLFLLSLLSIPVYAVIII 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 177 YYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDArfdptIYIAIGAS- 255
Cdd:TIGR01193 314 LFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQ-----GQQAIKAVt 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 256 ----NLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRirslLNEAPAV----QDGPQ- 326
Cdd:TIGR01193 389 klilNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNR----LNEVYLVdsefINKKKr 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 327 -ALPAGRGVLEVDIRAFHYPENpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRL 405
Cdd:TIGR01193 465 tELNNLNGDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDR 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 406 DDWRSRLSVVSQTPFLFSDTVANNIALG-QPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIA 484
Cdd:TIGR01193 544 HTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALA 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 485 RALLLDAEILILDDALSAVDGRTEHQILHNLRSWgQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWY 564
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFY 702
|
....
gi 1574033397 565 RDMY 568
Cdd:TIGR01193 703 ASLI 706
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
332-548 |
8.06e-61 |
|
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: 201.16 E-value: 8.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 332 RGVLEVDIRAFHYPENP-HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRS 410
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 411 RLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLD 490
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 491 AEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGV 548
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-569 |
1.16e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.22 E-value: 1.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 306 AAYSRIRSLLNEAPAVQ-DGPQALPAGRGVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQR 384
Cdd:PRK11160 309 ASARRINEITEQKPEVTfPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 385 QFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAarLASVH-EDILRLPQGYD 463
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEV--LQQVGlEKLLEDDKGLN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 464 TEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVM 543
Cdd:PRK11160 467 AWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVM 546
|
250 260
....*....|....*....|....*.
gi 1574033397 544 QHGGVAQRGDPAALAAQPGWYRDMYR 569
Cdd:PRK11160 547 DNGQIIEQGTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
344-554 |
1.09e-55 |
|
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: 187.32 E-value: 1.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 344 YPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFS 423
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 DTVANNIA-LGQpgATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:cd03244 92 GTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 503 VDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDP 554
Cdd:cd03244 170 VDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-311 |
2.41e-55 |
|
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: 188.91 E-value: 2.41e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFYR 98
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAG-DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 99 QLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVdSLVMGLVVLVVMSTQISWQLTVLALIPMPLMAIAIKYY 178
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLL-SDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 179 GDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNLL 258
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 259 AIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
2-569 |
4.15e-55 |
|
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: 196.26 E-value: 4.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 2 RLFAQIGWYFRREWRRYLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYL-------LR 74
Cdd:TIGR01192 5 QVYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLvareadrLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 75 YVWRVLLFGASYQLAVELRENFYRQLSRQNpAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlvmglvvlvvmST 154
Cdd:TIGR01192 85 HGRRATLLTEAFGRIISMPLSWHQQRGTSN-ALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPT-----------AF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 155 QISWQLTVLalipmpLMAIAIKYY--GDQLHQRFKSAQAA----FSSLNDQAQESMTSIRMIkafgledHQSNRfadVAA 228
Cdd:TIGR01192 153 AMDWRLSIV------LMVLGILYIliAKLVMQRTKNGQAAvehhYHNVFKHVSDSISNVSVV-------HSYNR---IEA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 229 QTGAKNMHVARVDARFDPTIYIAIGASNLLAIGG----------GSWMVVNGSLTLGQLTSFVMYLGLMIWpmlALAWMF 298
Cdd:TIGR01192 217 ETSALKQFTNNLLSAQYPVLDWWALASGLNRMAStismmcilviGTVLVIKGELSVGEVIAFIGFANLLIG---RLDQMS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 299 NIVERGSAAYSRIRSLLNEAPAVQDGPQ-----ALPAGRGVLEVDIRAFHYPeNPHPALHDLALTLKPGQMLGLCGPTGA 373
Cdd:TIGR01192 294 GFITQIFEARAKLEDFFDLEDSVFQREEpadapELPNVKGAVEFRHITFEFA-NSSQGVFDVSFEAKAGQTVAIVGPTGA 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 374 GKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHE 453
Cdd:TIGR01192 373 GKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 454 DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSA 533
Cdd:TIGR01192 453 FILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLST 532
|
570 580 590
....*....|....*....|....*....|....*.
gi 1574033397 534 LTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYR 569
Cdd:TIGR01192 533 VRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLR 568
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
15-589 |
5.83e-55 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 196.09 E-value: 5.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 15 WRRYLG-AVVLLIVIAILQLLPPKLVGIIVDGVTEK-----QMSTGVLLAWLGLMIGTAivvyLLRYvWRVLLFG-ASYQ 87
Cdd:PRK10790 21 WRKPLGlAVLMLWVAAAAEVSGPLLISYFIDNMVAKgnlplGLVAGLAAAYVGLQLLAA----GLHY-AQSLLFNrAAVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 88 LAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRV------VFAAGEGVLTLVDSLVMGLVVlvvmstqISWQLT 161
Cdd:PRK10790 96 VVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIrdlyvtVVATVLRSAALIGAMLVAMFS-------LDWRMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 162 VLALIPMPLMAIAIKYYgdqlhQRF-----KSAQAAFSSLNDQAQESMTSIRMIKAFgledHQSNRFADVAAQTgAKNMH 236
Cdd:PRK10790 169 LVAIMIFPAVLVVMVIY-----QRYstpivRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMGEA-SRSHY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 237 VARVDA-RFD-----P--TIYIAIGASNLLAIGGGSwmvVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAY 308
Cdd:PRK10790 239 MARMQTlRLDgfllrPllSLFSALILCGLLMLFGFS---ASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 309 SRIRSLLnEAPAVQDGPQALPAGRGVLEVDIRAFHYPENpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDV 388
Cdd:PRK10790 316 ERVFELM-DGPRQQYGNDDRPLQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 389 DQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPgATQAQIEQAARLASVHEDILRLPQGYDTEVGE 468
Cdd:PRK10790 394 TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 469 RGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGV 548
Cdd:PRK10790 473 QGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQA 552
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1574033397 549 AQRGDPAALAAQPGWYRDMYRYQQLEAALdEAPENGEEALA 589
Cdd:PRK10790 553 VEQGTHQQLLAAQGRYWQMYQLQLAGEEL-AASVREEESLS 592
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
72-531 |
6.50e-55 |
|
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: 194.50 E-value: 6.50e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 72 LLRYVWRVLLFGASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVD-------RVVFAAGEGVLTLVDSLVM 144
Cdd:TIGR02868 68 VFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDalqdlyvRVIVPAGVALVVGAAAVAA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 145 glvvlvvmSTQISWQLT-------VLALIPMPLMAIAIKYYGDQlhqrfkSAQAAFSSLNDQAQESMTSIRMIKAFGLED 217
Cdd:TIGR02868 148 --------IAVLSVPAAlilaaglLLAGFVAPLVSLRAARAAEQ------ALARLRGELAAQLTDALDGAAELVASGALP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 218 HQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWM 297
Cdd:TIGR02868 214 AALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 298 FNIVERGSAAYSRIRSLLNEAPAVQDGPQALPAGRGVLEVDIRA----FHYPENPhPALHDLALTLKPGQMLGLCGPTGA 373
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELrdlsAGYPGAP-PVLDGVSLDLPPGERVAILGPSGS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 374 GKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQAQIEQAARLASVHE 453
Cdd:TIGR02868 373 GKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLAD 452
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 454 DILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRL 531
Cdd:TIGR02868 453 WLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-546 |
3.19e-54 |
|
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: 183.05 E-value: 3.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 345 PENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlddwrsRLSVVSQTPFLFSD 424
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQEPWIQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALGQPgATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:cd03250 81 TIRENILFGKP-FDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1574033397 505 GRTEHQILHN--LRSWGQDRTVIISAHRLSALTEASEILVMQHG 546
Cdd:cd03250 160 AHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
183-553 |
8.18e-54 |
|
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: 192.27 E-value: 8.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 183 HQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNLLAIGG 262
Cdd:COG4618 180 RKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 263 GSWMVVNGSLTLGQL--TSFVMYLGL-----MI--WPMLALAWmfnivergsAAYSRIRSLLNEAPAVQDGPqALPAGRG 333
Cdd:COG4618 260 GAYLVIQGEITPGAMiaASILMGRALapieqAIggWKQFVSAR---------QAYRRLNELLAAVPAEPERM-PLPRPKG 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLS 413
Cdd:COG4618 330 RLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQTPFLFSDTVANNIA-LGQPgaTQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAE 492
Cdd:COG4618 410 YLPQDVELFDGTIAENIArFGDA--DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 493 ILILDDALSAVDGRTE---HQILHNLRSWGqdRTVIISAHRLSALTEASEILVMQHGGVAQRGD 553
Cdd:COG4618 488 LVVLDEPNSNLDDEGEaalAAAIRALKARG--ATVVVITHRPSLLAAVDKLLVLRDGRVQAFGP 549
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
355-574 |
1.07e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 186.97 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 355 LALTLKPGQMLGLCGPTGAGKSTLLSLIQrQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQ 434
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 435 PGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHN 514
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 515 LRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYRYQQLE 574
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
5.97e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 171.95 E-value: 5.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFYR 98
Cdd:cd18778 2 ILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 99 QLSRQNPAFYLRHRTGDLMARATNDVD---RVVFAAGEG----VLTLVDSLVMGLvvlvvmstQISWQLTVLALIPMPLM 171
Cdd:cd18778 82 KLQRLSLRYFDDRQTGDLMSRVINDVAnveRLIADGIPQgitnVLTLVGVAIILF--------SINPKLALLTLIPIPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 172 AIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIA 251
Cdd:cd18778 154 ALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 252 IGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18778 234 TSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
258-552 |
9.95e-49 |
|
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: 177.93 E-value: 9.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 258 LAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSLLNEAPAvQDGPQALPAGRGVLEV 337
Cdd:TIGR01842 241 LVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPS-RDPAMPLPEPEGHLSV 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 338 DIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQ 417
Cdd:TIGR01842 320 ENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 418 TPFLFSDTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILD 497
Cdd:TIGR01842 400 DVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLD 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 498 DALSAVDGRTEHQILHNLRSW-GQDRTVIISAHRLSALTEASEILVMQHGGVAQRG 552
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
1.76e-47 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 168.46 E-value: 1.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDGVT-------------EKQMSTGVLLAWLGL-MIGTAIVVYLLRYVWRVLLFGA 84
Cdd:cd18564 2 ALALLALLLETALRLLEPWPLKVVIDDVLgdkplpgllglapLLGPDPLALLLLAAAaLVGIALLRGLASYAGTYLTALV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 85 SYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMStQISWQLTVLA 164
Cdd:cd18564 82 GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMF-WLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 165 LIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARF 244
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 245 DPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-311 |
2.39e-47 |
|
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: 167.60 E-value: 2.39e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 18 YLGAVVLLIVIAILQLLPPKLVGIIVDGV-TEKQMStgvLLAWLGLMIgtaIVVYLLR----YVWRVLLFGASYQLAVEL 92
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIfVEKDLE---ALLLVPLAI---IGLFLLRglasYLQTYLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 93 RENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlvmglvvlvvmSTQI----------SWQLTV 162
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRD-----------PLTVigllgvlfylDWKLTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 163 LALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDA 242
Cdd:cd18552 144 IALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 243 RFDPTIYI--AIGASNLLAIGGgsWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18552 224 LSSPLMELlgAIAIALVLWYGG--YQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
1.59e-46 |
|
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: 165.38 E-value: 1.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDGV---TEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELREN 95
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIDDVliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 96 FYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTqISWQLTVLALIPMPLMAIAI 175
Cdd:cd18563 82 LYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFS-LNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 176 KYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGAS 255
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 256 NLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
19-311 |
3.21e-46 |
|
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: 164.58 E-value: 3.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFYR 98
Cdd:cd18543 2 ILALLAALLATLAGLAIPLLTRRAIDGPIAHG-DRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 99 QLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMStqISWQLTVLALIPMPLMAIAIKYY 178
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLTLVVGLVVMLV--LSPPLALVALASLPPLVLVARRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 179 GDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNLL 258
Cdd:cd18543 159 RRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 259 AIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18543 239 VLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-311 |
1.85e-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: 152.34 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 18 YLGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLA------------WL--GLMIGTAIVVYLLRYVWRVLLFG 83
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLPLVPaslgpadprgqlWLlgGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 84 ASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDR---------------VVFAAGEGVLTLVdslvmglvv 148
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQlerflddgansiirvVVTVLGIGAILFY--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 149 lvvmstqISWQLTVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAA 228
Cdd:cd18565 152 -------LNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 229 QTGAKNMHVARVDARFDPTIYIAIGASNLLAIGGGSWMVVNG------SLTLGQLTSFVMYLGLMIWPMLALAWMFNIVE 302
Cdd:cd18565 225 EYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQ 304
|
....*....
gi 1574033397 303 RGSAAYSRI 311
Cdd:cd18565 305 RAMASAKRV 313
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-552 |
5.71e-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: 143.61 E-value: 5.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSVVSQTPFL 421
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTVANNIalgqpgatqaqieqaarlasvhedilrlpqgydtevGERgvmLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:cd03247 87 FDTTLRNNL------------------------------------GRR---FSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 502 AVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRG 552
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-501 |
6.10e-39 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.09 E-value: 6.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSD-TVANNI 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 431 ALGQPGATQAQIEQAARLASVHEDiLRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
7-562 |
3.68e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 151.28 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 7 IGWYFRREWRRYLGAV-VLLIVIA------ILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWrv 79
Cdd:PLN03232 896 ISWNVLMRYNKAVGGLwVVMILLVcyltteVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFW-- 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 80 lLFGASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDV---DRVVFAAGEGVLTLVDSLVMGLVVLVVMSTQI 156
Cdd:PLN03232 974 -LISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIgdiDRNVANLMNMFMNQLWQLLSTFALIGTVSTIS 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 157 SWQLtvlalipMPLMAI---AIKYYGDQLHQ--RFKS-AQAAFSSLNDQAQESMTSIRMIKAFgledhqsNRFADVAAQT 230
Cdd:PLN03232 1053 LWAI-------MPLLILfyaAYLYYQSTSREvrRLDSvTRSPIYAQFGEALNGLSSIRAYKAY-------DRMAKINGKS 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 231 GAKNMHVARVDARFDPTIYIaigasNLLAIGG------GSWMVVNGSLTLGQlTSFVMYLGLMIWPMLALAWMF-NIVER 303
Cdd:PLN03232 1119 MDNNIRFTLANTSSNRWLTI-----RLETLGGvmiwltATFAVLRNGNAENQ-AGFASTMGLLLSYTLNITTLLsGVLRQ 1192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 304 GSAAYSRIRS---------LLNEAPAVQDG---PQALPAGRGVLEVDIRAFHYPENPhPALHDLALTLKPGQMLGLCGPT 371
Cdd:PLN03232 1193 ASKAENSLNSvervgnyidLPSEATAIIENnrpVSGWPSRGSIKFEDVHLRYRPGLP-PVLHGLSFFVSPSEKVGVVGRT 1271
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 372 GAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIalgQPGA--TQAQIEQAARLA 449
Cdd:PLN03232 1272 GAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSehNDADLWEALERA 1348
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 450 SVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAH 529
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
|
570 580 590
....*....|....*....|....*....|...
gi 1574033397 530 RLSALTEASEILVMQHGGVAQRGDPAALAAQPG 562
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
21-311 |
5.06e-37 |
|
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: 139.23 E-value: 5.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKqmSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFG-ASYQLAVELRENFYRQ 99
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKG--GDLDVLNELALILLAIYLLQSVFTFVRYYLFNiAGERIVARLRRDLFSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 100 LSRQNPAFYLRHRTGDLMARATNDV--------------DRVVFAAGEGVLTLVdslvmglvvlvvmstQISWQLTVLAL 165
Cdd:cd18557 79 LLRQEIAFFDKHKTGELTSRLSSDTsvlqsavtdnlsqlLRNILQVIGGLIILF---------------ILSWKLTLVLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 166 IPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFD 245
Cdd:cd18557 144 LVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQ 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 246 PTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18557 224 GITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
42-569 |
7.03e-37 |
|
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: 147.40 E-value: 7.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 42 IVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLfgASYQLAVELRENFYRqlsrqNP-AFYLRHRTGDLMARA 120
Cdd:TIGR00957 996 MVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQ--ASRVLHQDLLHNKLR-----SPmSFFERTPSGNLVNRF 1068
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 121 TNDVDRVVFAAGEGVLTLVDSLVMGlvvlvvmstqISWQLTVLALIPMPLMAI---AIKYYgdqLHQRFKSAQA------ 191
Cdd:TIGR00957 1069 SKELDTVDSMIPPVIKMFMGSLFNV----------IGALIVILLATPIAAVIIpplGLLYF---FVQRFYVASSrqlkrl 1135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 192 ---AFSSLNDQAQESMTSIRMIKAFgledHQSNRF---ADVAAQTGAKNMHVARVDARfdptiYIAIG---ASNLLAIGG 262
Cdd:TIGR00957 1136 esvSRSPVYSHFNETLLGVSVIRAF----EEQERFihqSDLKVDENQKAYYPSIVANR-----WLAVRlecVGNCIVLFA 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 263 GSWMVVN-GSLTLGQLTSFVMYlGLMIwpMLALAWMFNI---VERGSAAYSRIRSLL---NEAPAVQDG---PQALPAgR 332
Cdd:TIGR00957 1207 ALFAVISrHSLSAGLVGLSVSY-SLQV--TFYLNWLVRMsseMETNIVAVERLKEYSeteKEAPWQIQEtapPSGWPP-R 1282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 333 GVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRL 412
Cdd:TIGR00957 1283 GRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKI 1362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTPFLFSDTVANNI-ALGQpgATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDA 491
Cdd:TIGR00957 1363 TIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 492 EILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYR 569
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
26-310 |
8.36e-37 |
|
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: 138.74 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 26 IVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYLLRYVwrVLLFGASYQLAVE--LRENFYRQLSRQ 103
Cdd:cd18549 12 VLIAALDLVFPLIVRYIIDDLLPSK-NLRLILIIGAILLALYILRTLLNYF--VTYWGHVMGARIEtdMRRDLFEHLQKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 104 NPAFYLRHRTGDLMARATNDVDRVVFAAGEG-------VLTLVDSLVMGLvvlvvmstQISWQLTVLALIPMPLMAIAIK 176
Cdd:cd18549 89 SFSFFDNNKTGQLMSRITNDLFDISELAHHGpedlfisIITIIGSFIILL--------TINVPLTLIVFALLPLMIIFTI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 177 YYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADV------AAQTGAKNMhvarvdARFDPTIYI 250
Cdd:cd18549 161 YFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGndrfleSKKKAYKAM------AYFFSGMNF 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 251 AIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSR 310
Cdd:cd18549 235 FTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
19-311 |
1.30e-36 |
|
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: 138.37 E-value: 1.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVD-GVTEKQMStgVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFY 97
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAIDeYIPNGDLS--GLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 98 RQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV-DSLVMGLVVLVVMStqISWQLTVLALIPMPLMAIAIK 176
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIpDLLTLVGIVIIMFS--LNVRLALVTLAVLPLLVLVVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 177 YYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASN 256
Cdd:cd18545 159 LLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 257 LLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18545 239 ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
339-548 |
2.27e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 134.94 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 339 IRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQT 418
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 PFLFSDTVANNIALGQPGATQAQIEQAAR--LASVH--EDILrlpqgyDTEVGErgvmLSGGQKQRISIARALLLDAEIL 494
Cdd:COG4619 83 PALWGGTVRDNLPFPFQLRERKFDRERALelLERLGlpPDIL------DKPVER----LSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 495 ILDDALSAVDGRTEHQILHNLRSW--GQDRTVIISAH-RLSALTEASEILVMQHGGV 548
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-561 |
2.85e-36 |
|
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: 135.15 E-value: 2.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPF- 420
Cdd:COG1122 8 FSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 -LFSDTVANNIALG--QPGATQAQIEQAAR--LASVH-EDIL-RLPQgydtevgergvMLSGGQKQRISIARALLLDAEI 493
Cdd:COG1122 87 qLFAPTVEEDVAFGpeNLGLPREEIRERVEeaLELVGlEHLAdRPPH-----------ELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 494 LILDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
19-311 |
9.98e-36 |
|
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: 135.59 E-value: 9.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDG-VTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFY 97
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDyIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 98 RQLSRQNPAFYLRHRTGDLMARATNDVDRV--VFAAG-----EGVLTLVdslvmglvVLVVMSTQISWQLTVLALIPMPL 170
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALneLFTSGlvtliGDLLLLI--------GILIAMFLLNWRLALISLLVLPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 171 MAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYI 250
Cdd:cd18544 154 LLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVEL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 251 AIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18544 234 LSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
19-311 |
3.07e-35 |
|
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: 134.15 E-value: 3.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVD-GVTEKqmSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFY 97
Cdd:cd18546 2 ALALLLVVVDTAASLAGPLLVRYGIDsGVRAG--DLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 98 RQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTqISWQLTVLALIPMPLMAIAIKY 177
Cdd:cd18546 80 AHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLV-LDPRLALVALAALPPLALATRW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 178 YGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNL 257
Cdd:cd18546 159 FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 258 LAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18546 239 AVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
342-546 |
6.16e-35 |
|
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: 131.05 E-value: 6.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPF- 420
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 -LFSDTVANNIALG--QPGATQAQIEQAAR--LASVHEDIL--RLPQgydtevgergvMLSGGQKQRISIARALLLDAEI 493
Cdd:cd03225 87 qFFGPTVEEEVAFGleNLGLPEEEIEERVEeaLELVGLEGLrdRSPF-----------TLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 494 LILDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLS-ALTEASEILVMQHG 546
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-554 |
9.01e-35 |
|
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: 130.61 E-value: 9.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 333 GVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRL 412
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTPFLFSDTVANNIalgQP--GATQAQIEQAARlasvhedilrlpqgydteVGERGVMLSGGQKQRISIARALLLD 490
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNL---DPfdEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 491 AEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDP 554
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
19-311 |
1.36e-34 |
|
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: 132.56 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIV----VYLLRYVwrvllfgaSYQLAVELRE 94
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLsalsSYLLGRT--------GERVVLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 95 NFYRQLSRQNPAFYLRHRTGDLMARATND-------VDRVVFAAGEGVLTLVDSLVMGLVvlvvmstqISWQLTVLALIP 167
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTNDttllrelITSGLPQLVTGVLTVVGAVVLMFL--------LDWVLTLVTLAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 168 MPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPT 247
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 248 IYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
349-560 |
2.00e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.18 E-value: 2.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVPQEPALYPDlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIAL-----GQPGATQAqiEQAARLAsvheDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:COG1131 92 ENLRFfarlyGLPRKEAR--ERIDELL----ELFGLTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 503 VD--GRTE-HQILHNLRSwgQDRTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:COG1131 162 LDpeARRElWELLRELAA--EGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
273-557 |
3.18e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 139.10 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 273 TLGQLTSFVMYLGLMIWPMLALAWM----FNIVERgSAAYSRIRSllnEAPAVQDG---PQALPAGRGVLEVDIRAFHYP 345
Cdd:PLN03130 1174 TMGLLLSYALNITSLLTAVLRLASLaensLNAVER-VGTYIDLPS---EAPLVIENnrpPPGWPSSGSIKFEDVVLRYRP 1249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 346 ENPhPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDT 425
Cdd:PLN03130 1250 ELP-PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGT 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIalgQPGA--TQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:PLN03130 1329 VRFNL---DPFNehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 504 DGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:PLN03130 1406 DVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENL 1459
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
19-311 |
4.80e-34 |
|
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: 130.98 E-value: 4.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVD-GVTEKQMStgVLLAWLGLMIGTAIVVYLLRYVwrVLLFGA--SYQLAVELREN 95
Cdd:cd18548 2 ILAPLFKLLEVLLELLLPTLMADIIDeGIANGDLS--YILRTGLLMLLLALLGLIAGIL--AGYFAAkaSQGFGRDLRKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 96 FYRQLSRQNPAFYLRHRTGDLMARATNDVDRV---------------VFAAGEGVLTLVdslvmglvvlvvmstqISWQL 160
Cdd:cd18548 78 LFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVqnfvmmllrmlvrapIMLIGAIIMAFR----------------INPKL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 161 TVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARV 240
Cdd:cd18548 142 ALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 241 DARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18548 222 MALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
271-561 |
7.91e-34 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 137.85 E-value: 7.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 271 SLTLGQLTSfvMYLGLMIWPmlalawmfNIVE--RGSAAYSRIRSLLNEAPAV---QDGpQALPAGRGVLEVDIRaFHYP 345
Cdd:PTZ00265 326 SILLGVLIS--MFMLTIILP--------NITEymKSLEATNSLYEIINRKPLVennDDG-KKLKDIKKIQFKNVR-FHYD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 346 ENPHPALH-DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQI---RYHGLPlpQVRLDDWRSRLSVVSQTPFL 421
Cdd:PTZ00265 394 TRKDVEIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiinDSHNLK--DINLKWWRSKIGVVSQDPLL 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTVANNI-----ALGQPGATQAQIEQ---------------------------------------------------- 444
Cdd:PTZ00265 472 FSNSIKNNIkyslySLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsevvd 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 445 AARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH---QILHNLRSwGQD 521
Cdd:PTZ00265 552 VSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYlvqKTINNLKG-NEN 630
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1574033397 522 RTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PTZ00265 631 RITIIIAHRLSTIRYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
300-561 |
8.11e-34 |
|
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: 135.03 E-value: 8.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 300 IVERGS-----AAYSRIRSLLNEAPAVQDGPQALPAGRGVLEVDIRAFHYPE---NPHPALHDLALTLKPGQMLGLCGPT 371
Cdd:COG1123 221 IVEDGPpeeilAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVrgkGGVRAVDDVSLTLRRGETLGLVGES 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 372 GAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQV---RLDDWRSRLSVVSQTPF--LF-SDTVANNIALG---QPGATQAQI 442
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELRRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAER 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 443 EQAAR--LASVH--EDIL-RLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRS 517
Cdd:COG1123 381 RERVAelLERVGlpPDLAdRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRD 449
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1574033397 518 WgQDR---TVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG1123 450 L-QRElglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFANP 496
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-548 |
8.41e-34 |
|
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: 126.56 E-value: 8.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 335 LEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSV 414
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 415 VSQTPFLFSDTVANNIalgqpgatqaqieqaarlasvhedilrlpqgydtevgergvmLSGGQKQRISIARALLLDAEIL 494
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 495 ILDDALSAVDGRTEHQILHNLRSW-GQDRTVIISAHRLSALTEASEILVMQHGGV 548
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
19-311 |
1.72e-33 |
|
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: 129.45 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTG-----VLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18547 2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGgvdfsGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 94 ENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlvmglvvlvvmSTQI----------SWQLTVL 163
Cdd:cd18547 82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISS-----------ILTIvgtlimmlyiSPLLTLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 164 ALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVaaqtgAKNMHVARVDAR 243
Cdd:cd18547 151 VLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEI-----NEELYKASFKAQ 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 244 F-----DPTIyIAIGASNLLAIGG-GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18547 226 FysgllMPIM-NFINNLGYVLVAVvGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-311 |
2.81e-33 |
|
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: 128.76 E-value: 2.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQMST---GVLLAWLGLMIGTAIVVYllryvWRVLLFG-ASYQLAVELRENF 96
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTAslnQIALLLLGLFLLQAVFSF-----FRIYLFArVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 97 YRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEG-------VLTLVDSLVMGLVvlvvmstqISWQLTVLALIPMP 169
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTlaeflrqILTLIGGVVLLFF--------ISWKLTLLMLATVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 170 LMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIY 249
Cdd:cd18576 148 VVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFII 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 250 IAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18576 228 FLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
344-560 |
4.45e-33 |
|
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: 127.33 E-value: 4.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 344 YPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFS 423
Cdd:cd03288 29 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 DTVANNIAlGQPGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:cd03288 109 GSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 504 DGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:cd03288 188 DMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-588 |
1.78e-32 |
|
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: 131.18 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLS----LIQRQFDVdQGQIRYHGLPLPQVRLDDWR 409
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALalmgLLPHGGRI-SGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 410 SRLSVVSQTPF--LFSDTVANNIA--LGQPGATQAQIEQAAR--LASVHedILRLPQGYDTEvgergvmLSGGQKQRISI 483
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAeaLENLGLSRAEARARVLelLEAVG--LERRLDRYPHQ-------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 484 ARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
250 260
....*....|....*....|....*...
gi 1574033397 561 PGWYRDMYRYQQLEAALDEAPENGEEAL 588
Cdd:COG1123 234 PQALAAVPRLGAARGRAAPAAAAAEPLL 261
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
336-546 |
1.81e-32 |
|
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: 122.35 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 336 EVDIRAFHYPEnpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVV 415
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 416 SQtpflfsdtvannialgqpgatqaqieqaarlasvhedilrlpqgydtevgergvmLSGGQKQRISIARALLLDAEILI 495
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 496 LDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLSALTEAS-EILVMQHG 546
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAAdRVIVLKDG 156
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
349-561 |
3.61e-32 |
|
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: 124.53 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSD---T 425
Cdd:COG1124 18 VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYASLHprhT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANniALGQP------GATQAQIEQAARLASVHEDIL-RLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDD 498
Cdd:COG1124 98 VDR--ILAEPlrihglPDREERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVAIARALILEPELLLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 499 ALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG1124 165 PTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDrVAVMQNGRIVEELTVADLLAGP 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
349-550 |
4.60e-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: 123.03 E-value: 4.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP----------LPQVRLDDWRSRLSVvsqt 418
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPlekerkrigyVPQRRSIDRDFPISV---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 pflfSDTVANNI-----ALGQPGATQAQIEQAArLASVheDIlrlpqgydTEVGERGV-MLSGGQKQRISIARALLLDAE 492
Cdd:cd03235 88 ----RDVVLMGLyghkgLFRRLSKADKAKVDEA-LERV--GL--------SELADRQIgELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 493 ILILDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLSALTE-ASEILVMQHGGVAQ 550
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVAS 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
342-586 |
5.39e-32 |
|
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: 123.81 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPhpALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPlPQVRLDDWRSRLSVVSQTPFL 421
Cdd:COG4555 9 KKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-VRKEPREARRQIGVLPDERGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSD-TVANNIAL-----GQPG-ATQAQIEQAARLasvhediLRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEIL 494
Cdd:COG4555 86 YDRlTVRENIRYfaelyGLFDeELKKRIEELIEL-------LGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 495 ILDDALSAVDGRTEHQILHNLRSWG-QDRTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQpgwyrdmYRYQQ 572
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE-------IGEEN 227
|
250
....*....|....
gi 1574033397 573 LEAALDEAPENGEE 586
Cdd:COG4555 228 LEDAFVALIGSEEG 241
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
332-545 |
1.46e-31 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 130.92 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 332 RGVLEVDIRAFHYPENPH-PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDV---------------------- 388
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdy 1242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 389 --------------------------------DQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIALGQPG 436
Cdd:PTZ00265 1243 qgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED 1322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 437 ATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLR 516
Cdd:PTZ00265 1323 ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402
|
250 260 270
....*....|....*....|....*....|.
gi 1574033397 517 SWGQ--DRTVIISAHRLSALTEASEILVMQH 545
Cdd:PTZ00265 1403 DIKDkaDKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
334-546 |
1.66e-31 |
|
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: 121.84 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEV-DIRAfHYPEN--PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG---LPLPQVRLDD 407
Cdd:cd03257 1 LLEVkNLSV-SFPTGggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 408 WRSRLSVVSQTPFL---FSDTVANNIA----LGQPGATQAQIEQAARLASVH----EDIL-RLPQgydtevgergvMLSG 475
Cdd:cd03257 80 RRKEIQMVFQDPMSslnPRMTIGEQIAeplrIHGKLSKKEARKEAVLLLLVGvglpEEVLnRYPH-----------ELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 476 GQKQRISIARALLLDAEILILDDALSAVDGRTEHQI---LHNLRSwGQDRTVIISAHRLSALTE-ASEILVMQHG 546
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQIldlLKKLQE-ELGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
341-557 |
4.29e-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: 121.69 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 341 AFHYPEnpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPF 420
Cdd:COG1120 8 SVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 L-FSDTVANNIALG---------QPGAT-QAQIEQAARLASVHEDILRLpqgYDTevgergvmLSGGQKQRISIARALLL 489
Cdd:COG1120 86 ApFGLTVRELVALGryphlglfgRPSAEdREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 490 DAEILILDDALSAVDGRTEHQILHNLRSW--GQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-555 |
9.37e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.19 E-value: 9.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPEnpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP----------LPQV 403
Cdd:COG1121 6 AIELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPprrarrrigyVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 404 RLDDWRSRLSVvsqtpflfSDTVANNI-----ALGQPGATQ-AQIEQAarLASVH-EDILRLPqgydteVGErgvmLSGG 476
Cdd:COG1121 84 AEVDWDFPITV--------RDVVLMGRygrrgLFRRPSRADrEAVDEA--LERVGlEDLADRP------IGE----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 477 QKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSW-GQDRTVIISAHRLSALTE-ASEILVMQHGGVAQrGDP 554
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPP 222
|
.
gi 1574033397 555 A 555
Cdd:COG1121 223 E 223
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
21-307 |
6.00e-30 |
|
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: 119.19 E-value: 6.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIvvYLLRYVWRVLLFGASYQ-LAVELRENFYRQ 99
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVL--SGLFSGLRGGCFSYAGTrLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 100 LSRQNPAFYLRHRTGDLMARATNDVDRV---------VFAagEGVLTLVDSLVMGLVvlvvmstqISWQLTVLALIPMPL 170
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSDCQKVsdplstnlnVFL--RNLVQLVGGLAFMFS--------LSWRLTLLAFITVPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 171 MAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYI 250
Cdd:cd18572 149 IALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 251 AIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAA 307
Cdd:cd18572 229 LQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGA 285
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
350-546 |
6.46e-30 |
|
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: 117.43 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG--LPLPQVRLDDWRSRLSVV--SQTPFLFSDT 425
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNknESEPSFEATRSRNRYSVAyaAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQPGATQaQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDG 505
Cdd:cd03290 95 VEENITFGSPFNKQ-RYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1574033397 506 R-TEHQILHNLRSWGQD--RTVIISAHRLSALTEASEILVMQHG 546
Cdd:cd03290 174 HlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
281-569 |
7.47e-30 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 125.83 E-value: 7.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 281 VMYLGLMIWPMLalawMFNIVErGSAAYSRIRSLLN----EAPAVQDGPQAlPAGRGVLEVDIRAFHYPENPHPALHDLA 356
Cdd:TIGR00957 585 ILRFPLNILPMV----ISSIVQ-ASVSLKRLRIFLSheelEPDSIERRTIK-PGEGNSITVHNATFTWARDLPPTLNGIT 658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 357 LTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlddwrsRLSVVSQTPFLFSDTVANNIALG--- 433
Cdd:TIGR00957 659 FSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGkal 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 434 QPGATQAQIEQAARLAsvheDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILH 513
Cdd:TIGR00957 726 NEKYYQQVLEACALLP----DLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 514 NL---RSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDMYR 569
Cdd:TIGR00957 802 HVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLR 860
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-562 |
1.13e-29 |
|
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: 116.91 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVR---LDDWRSRLSVVSQT 418
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 PFLFSD-TVANNIALGQPGATQAQIEQAARLasvhEDILRL------PQGYDTEvgergvmLSGGQKQRISIARALLLDA 491
Cdd:cd03258 91 FNLLSSrTVFENVALPLEIAGVPKAEIEERV----LELLELvgledkADAYPAQ-------LSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 492 EILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQPG 562
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
347-552 |
1.18e-29 |
|
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: 116.46 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpqVRLDDWRSRLSVVSQTPFLFSD-T 425
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMVFQDYALFPHlT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALG--QPGATQAQIEQAARLASVHEDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:cd03259 89 VAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALAREPSLLLLDEPLSAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 504 DGRTEHQILHNLRSW--GQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRG 552
Cdd:cd03259 162 DAKLREELREELKELqrELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
349-546 |
3.35e-29 |
|
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: 113.65 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQvRLDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIalgqpgatqaqieqaarlasvhedilrlpqgydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSAVD--G 505
Cdd:cd03230 92 ENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDpeS 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1574033397 506 RTE-HQILHNLRSWGqdRTVIISAHRLSALTE-ASEILVMQHG 546
Cdd:cd03230 131 RREfWELLRELKKEG--KTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-543 |
3.62e-29 |
|
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: 115.26 E-value: 3.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 335 LEVDIRAFHYPEN--PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVrlddwRSRL 412
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTPFLFS-DTVANNIALG--QPGATQAQIEQAAR--LASVH----EDilRLPQgydtevgergvMLSGGQKQRISI 483
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGleLQGVPKAEARERAEelLELVGlsgfEN--AYPH-----------QLSGGMRQRVAL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 484 ARALLLDAEILILDDALSAVDGRTEHQiLHN--LRSWGQDR-TVIISAHRLS-ALTEASEILVM 543
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQ-LQEelLDIWRETGkTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
21-311 |
5.89e-29 |
|
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: 116.46 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLL----RYVwRVLLFG-ASYQLAVELREN 95
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALALLGVFVVgaaaNFG-RVYLLRiAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 96 FYRQLSRQNPAFYLRHRTGDLMARATNDVD--------------RVVFAAGEGVLTLVdslvmglvvlvvmstQISWQLT 161
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSvvgksltqnlsdglRSLVSGVGGIGMML---------------YISPKLT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 162 VLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVD 241
Cdd:cd18573 145 LVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALAS 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 242 ARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18573 225 GLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
21-291 |
6.71e-29 |
|
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: 115.82 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVT-----EKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVllfgASYQLAVELREN 95
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLpdgdpETQALNVYSLALLLLGLAQFILSFLQSYLLNH----TGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 96 FYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGLVVLVVMSTQiSWQLTVLALIPMPLMAIAI 175
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 176 KYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGAS 255
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1574033397 256 NLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPM 291
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
341-552 |
5.73e-28 |
|
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: 110.60 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 341 AFHYPEnpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQtpf 420
Cdd:cd03214 6 SVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 lfsdtvanniALGQPGATQaqieqaarLAsvhedilrlpqgydtevgERGVM-LSGGQKQRISIARALLLDAEILILDDA 499
Cdd:cd03214 81 ----------ALELLGLAH--------LA------------------DRPFNeLSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 500 LSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRG 552
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
337-546 |
8.64e-28 |
|
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: 109.97 E-value: 8.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 337 VDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLD--DWRSRLSV 414
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 415 VSQTPFLFSD-TVANNIALGqpgatqaqieqaarlasvhedilrlpqgydtevgergvmLSGGQKQRISIARALLLDAEI 493
Cdd:cd03229 81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 494 LILDDALSAVDGRTEHQILHNLRS-WGQD-RTVIISAHRLS-ALTEASEILVMQHG 546
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSlQAQLgITVVLVTHDLDeAARLADRVVVLRDG 177
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-295 |
3.92e-27 |
|
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: 111.42 E-value: 3.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 19 LGAVVLLIVI-AILQLLPPKLVGIIVD-GVTEKQMStgvLLAWL-GLMIGTAIVVYLLRYVWRVLLFGASYQLAVELREN 95
Cdd:cd18550 1 LALVLLLILLsALLGLLPPLLLREIIDdALPQGDLG---LLVLLaLGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 96 FYRQLSRQNPAFYLRHRTGDLMARATNDVDRVvfaagEGVL--TLVDSLVMGLVVLVVMST--QISWQLTVLALIPMPLM 171
Cdd:cd18550 78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGA-----QSVVtgTLTSVVSNVVTLVATLVAmlALDWRLALLSLVLLPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 172 AIAIKYYGDQLHQRFKSAQAAFSSLNDQAQE--SMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIY 249
Cdd:cd18550 153 VLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1574033397 250 IAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALA 295
Cdd:cd18550 233 LFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLL 278
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
348-585 |
5.24e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 116.80 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 348 PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIryhglplpqvrlddWRSR-LSVVSQTPFLFSDTV 426
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------WAERsIAYVPQQAWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 427 ANNIALGQPGATqAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGR 506
Cdd:PTZ00243 738 RGNILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 507 TEHQILHNL---RSWGQDRtvIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPgwyrdmyRYQQLEAALDEAPEN 583
Cdd:PTZ00243 817 VGERVVEECflgALAGKTR--VLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-------LYATLAAELKENKDS 887
|
..
gi 1574033397 584 GE 585
Cdd:PTZ00243 888 KE 889
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
349-561 |
1.16e-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: 108.54 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFPHmTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALgQP---GATQAQIEQAAR--LASVHEDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:cd03295 94 ENIAL-VPkllKWPKEKIRERADelLALVGLDPAEFADRYPHE-------LSGGQQQRVGVARALAADPPLLLMDEPFGA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 503 VDGRTEHQILHNLRSWGQD--RTVIISAHRL-SALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:cd03295 166 LDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
349-569 |
1.18e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 108.99 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVR---LDDWRSRLSVVSQTPFLFSD- 424
Cdd:COG3638 16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRIGMIFQQFNLVPRl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNI---ALGQPGA--------TQAQIEQAAR-LASVheDILRLpqgydteVGERGVMLSGGQKQRISIARALLLDAE 492
Cdd:COG3638 96 SVLTNVlagRLGRTSTwrsllglfPPEDRERALEaLERV--GLADK-------AYQRADQLSGGQQQRVAIARALVQEPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 493 ILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALaaQPGWYRDMYR 569
Cdd:COG3638 167 LILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDlARRYADRIIGLRDGRVVFDGPPAEL--TDAVLREIYG 244
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
161-550 |
1.34e-26 |
|
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: 115.78 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 161 TVLALIPMPLMAIAIKYYGDQLHQRFKSAQA-AFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADvaaqtgAKNMHVA- 238
Cdd:TIGR01271 1027 IFIAAIPVAVIFIMLRAYFLRTSQQLKQLESeARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHK------ALNLHTAn 1100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 239 -------------RVDA----RFDPTIYIAIGASN-------------LLAIGGGSWmVVNGSLTLGQLtsfvmylglmi 288
Cdd:TIGR01271 1101 wflylstlrwfqmRIDIifvfFFIAVTFIAIGTNQdgegevgiiltlaMNILSTLQW-AVNSSIDVDGL----------- 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 289 wpMLALAWMFNIVE---------RGSAAYSRIRSLLNEAPAVQDgpqALPAGrGVLEVDIRAFHYPENPHPALHDLALTL 359
Cdd:TIGR01271 1169 --MRSVSRVFKFIDlpqeeprpsGGGGKYQLSTVLVIENPHAQK---CWPSG-GQMDVQGLTAKYTEAGRAVLQDLSFSV 1242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 360 KPGQMLGLCGPTGAGKSTLLSLIQRQFDVDqGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSDTVANNIalgQPGA-- 437
Cdd:TIGR01271 1243 EGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEqw 1318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 438 TQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRS 517
Cdd:TIGR01271 1319 SDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
410 420 430
....*....|....*....|....*....|...
gi 1574033397 518 WGQDRTVIISAHRLSALTEASEILVMQHGGVAQ 550
Cdd:TIGR01271 1399 SFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ 1431
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
343-546 |
1.54e-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: 109.56 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 343 HYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlddwrsRLSVVSQTPFLF 422
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDTVANNIALGQpGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:cd03291 111 PGTIKENIIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1574033397 503 VDGRTEHQILHN-LRSWGQDRTVIISAHRLSALTEASEILVMQHG 546
Cdd:cd03291 190 LDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
324-561 |
3.49e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 114.49 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 324 GPQALPAGRGVLE-VDIRafhYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQ 402
Cdd:PTZ00243 1300 APHPVQAGSLVFEgVQMR---YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 403 VRLDDWRSRLSVVSQTPFLFSDTVANNIalgQP--GATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQR 480
Cdd:PTZ00243 1377 YGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQL 1453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 481 ISIARALLLDAEILIL-DDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAA 559
Cdd:PTZ00243 1454 MCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
..
gi 1574033397 560 QP 561
Cdd:PTZ00243 1534 NR 1535
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
329-543 |
5.26e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.10 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 329 PAGRGVLEVDI--RAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLD 406
Cdd:COG1116 2 SAAAPALELRGvsKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 407 dwrsrLSVVSQTPFLFS-DTVANNIALGQP--GATQAQIEQAAR--LASV----HEDilRLPQgydtevgergvMLSGGQ 477
Cdd:COG1116 82 -----RGVVFQEPALLPwLTVLDNVALGLElrGVPKAERRERARelLELVglagFED--AYPH-----------QLSGGM 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 478 KQRISIARALLLDAEILILDDALSAVDGRTEHQiLHN--LRSWGQDR-TVIISAHRLS-ALTEASEILVM 543
Cdd:COG1116 144 RQRVAIARALANDPEVLLMDEPFGALDALTRER-LQDelLRLWQETGkTVLFVTHDVDeAVFLADRVVVL 212
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
300-578 |
5.87e-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: 111.70 E-value: 5.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 300 IVERGSAA---------YSRirSLLNEAPAVQDGPQAlPAGRGVLEVDIRAFHYP---------ENPHPALHDLALTLKP 361
Cdd:COG4172 235 IVEQGPTAelfaapqhpYTR--KLLAAEPRGDPRPVP-PDAPPLLEARDLKVWFPikrglfrrtVGHVKAVDGVSLTLRR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 362 GQMLGLCGPTGAGKSTL----LSLIQRQfdvdqGQIRYHGLPLPQVR---LDDWRSRLSVVSQTPF-------LFSDTVA 427
Cdd:COG4172 312 GETLGLVGESGSGKSTLglalLRLIPSE-----GEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPFgslsprmTVGQIIA 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQPGATQAQIEQAARlasvheDILRlpqgydtEVG-ERGVM------LSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:COG4172 387 EGLRVHGPGLSAAERRARVA------EALE-------EVGlDPAARhrypheFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 501 SAVDGRTEHQILHNLRSWgQDRT----VIISaHRLS---ALteASEILVMQHGGVAQRGDPAALAAQPgwyRDMYRYQQL 573
Cdd:COG4172 454 SALDVSVQAQILDLLRDL-QREHglayLFIS-HDLAvvrAL--AHRVMVMKDGKVVEQGPTEQVFDAP---QHPYTRALL 526
|
....*
gi 1574033397 574 EAALD 578
Cdd:COG4172 527 AAAPL 531
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
333-550 |
7.13e-26 |
|
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: 107.25 E-value: 7.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 333 GVLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDqGQIRYHGLPLPQVRLDDWRSRL 412
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTPFLFSDTVANNI-ALGQpgATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDA 491
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 492 EILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQ 550
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
352-554 |
1.58e-25 |
|
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: 105.11 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG-----LPlPQVRlddwrsRLSVVSQTPFLFSD-T 425
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnLP-PEKR------DISYVPQNYALFPHmT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQPGATQAQIEQAARLASVHEDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDG 505
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 506 RTEHQILHNLRSWGQ--DRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDP 554
Cdd:cd03299 163 RTKEKLREELKKIRKefGVTVLHVTHDFEeAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
347-557 |
2.25e-25 |
|
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: 104.57 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDV-----DQGQIRYHGLPLPQVRLDDWRSRLSV--VSQTP 419
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLELRRRVgmVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 FLFSDTVANNIALGQP-------GATQAQIEQAARLASVHEDILRLPQGYDtevgergvmLSGGQKQRISIARALLLDAE 492
Cdd:cd03260 91 NPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 493 ILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
348-561 |
2.56e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.79 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 348 PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL--PQVRLDDWRSRLSVVSQTPFLFSDT 425
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VA-NNIALGqP----GATQAQIEQAAR--LASVhedilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDD 498
Cdd:PRK09493 93 TAlENVMFG-PlrvrGASKEEAEKQARelLAKV---------GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 499 ALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
349-540 |
2.84e-25 |
|
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: 103.71 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNI----ALGQPGATQAQIEQAArlasvheDILRLPQGYDTEVGergvMLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:COG4133 94 ENLrfwaALYGLRADREAIDEAL-------EAVGLAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1574033397 504 DGRTEHQILHNLRSW-GQDRTVIISAHRLSALTEASEI 540
Cdd:COG4133 163 DAAGVALLAELIAAHlARGGAVLLTTHQPLELAAARVL 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
349-561 |
3.98e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.72 E-value: 3.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI---QRqfdVDQGQIRYHG-----LPlPQVRlddwrsRLSVVSQTPF 420
Cdd:COG3842 18 VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagfET---PDSGRILLDGrdvtgLP-PEKR------NVGMVFQDYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 LFSD-TVANNIA--LGQPGATQAQIEQAAR--LASVH----EDilRLPQgydtevgergvMLSGGQKQRISIARALLLDA 491
Cdd:COG3842 88 LFPHlTVAENVAfgLRMRGVPKAEIRARVAelLELVGleglAD--RYPH-----------QLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 492 EILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEeALALADRIAVMNDGRIEQVGTPEEIYERP 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
334-554 |
4.48e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.07 E-value: 4.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLS 413
Cdd:PRK13632 7 MIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQTP---FLFSdTVANNIALG------QPGATQAQIEQAARLASVHEDILRLPQGydtevgergvmLSGGQKQRISIA 484
Cdd:PRK13632 87 IIFQNPdnqFIGA-TVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 485 RALLLDAEILILDDALSAVDGRTEH---QILHNLRSWGqDRTVIISAHRLSALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKReikKIMVDLRKTR-KKTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
350-546 |
7.07e-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: 110.39 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlddwrsRLSVVSQTPFLFSDTVANN 429
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 IALGQpGATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH 509
Cdd:TIGR01271 507 IIFGL-SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190
....*....|....*....|....*....|....*...
gi 1574033397 510 QILHN-LRSWGQDRTVIISAHRLSALTEASEILVMQHG 546
Cdd:TIGR01271 586 EIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
350-561 |
7.22e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 106.00 E-value: 7.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI---QRQfdvDQGQIRYHGlplpqvrlDDWRSRLSV-------VSQTP 419
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglETP---DSGRIVLNG--------RDLFTNLPPrerrvgfVFQHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 FLFSD-TVANNIA--LGQPGATQAQIEQAAR--LASVH----EDilRLP-QgydtevgergvmLSGGQKQRISIARALLL 489
Cdd:COG1118 85 ALFPHmTVAENIAfgLRVRPPSKAEIRARVEelLELVQleglAD--RYPsQ------------LSGGQRQRVALARALAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 490 DAEILILDDALSAVDG--RTEhqilhnLRSW------GQDRTVIISAH-RLSALTEASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:COG1118 151 EPEVLLLDEPFGALDAkvRKE------LRRWlrrlhdELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
.
gi 1574033397 561 P 561
Cdd:COG1118 225 P 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
350-561 |
7.92e-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: 103.09 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpqVRLDDWRSRLSVVSQTPFLFSD-TVAN 428
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALGqpgATQAQIEQAARLASVHEdILRLPQGYDTEvGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDG--R 506
Cdd:cd03300 92 NIAFG---LRLKKLPKAEIKERVAE-ALDLVQLEGYA-NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLklR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 507 TEHQI-LHNLrswgQDR---TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:cd03300 167 KDMQLeLKRL----QKElgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
340-546 |
1.27e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.43 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 340 RAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI---QRqfdVDQGQIRYHGLP---LPQVRLDDWRSR-L 412
Cdd:COG1136 12 KSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDissLSERELARLRRRhI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTPFLFSD-TVANNIALgqP----GATQAQIEQAAR--LASVH-EDIL-RLPQgydtevgergvMLSGGQKQRISI 483
Cdd:COG1136 89 GFVFQFFNLLPElTALENVAL--PlllaGVSRKERRERARelLERVGlGDRLdHRPS-----------QLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 484 ARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQD--RTVIISAHRLSALTEASEILVMQHG 546
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-557 |
2.29e-24 |
|
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: 101.88 E-value: 2.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 335 LEVDIRAFHYPeNPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVR---LDDWRSR 411
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 412 LSVVSQTPFLFSD-TVANNIALGQPGA-----------TQAQIEQAAR-LASVhedilrlpqGYDTEVGERGVMLSGGQK 478
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALAaLERV---------GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 479 QRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPA 555
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPA 230
|
..
gi 1574033397 556 AL 557
Cdd:cd03256 231 EL 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-562 |
2.35e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.39 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP---LPQVRLDDWRSRLSVVSQT 418
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 PFLF-SDTVANNIAL-----GQPGAtqaqiEQAARlasVHEdILRLpqgydteVG--ERGVM----LSGGQKQRISIARA 486
Cdd:COG1135 91 FNLLsSRTVAENVALpleiaGVPKA-----EIRKR---VAE-LLEL-------VGlsDKADAypsqLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 487 LLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQPG 562
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVFANPQ 233
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
263-558 |
2.54e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 108.52 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 263 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRSL-------LNEAPAVQDGPQALPAGRGVL 335
Cdd:PLN03232 543 GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseeriLAQNPPLQPGAPAISIKNGYF 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 336 EVDIRAfhypenPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQfdvdqgqiryhgLPLPQVRLDDWRSRLSVV 415
Cdd:PLN03232 623 SWDSKT------SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGE------------LSHAETSSVVIRGSVAYV 684
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 416 SQTPFLFSDTVANNIALGQPGATQaQIEQAARLASVHEDILRLPqGYD-TEVGERGVMLSGGQKQRISIARALLLDAEIL 494
Cdd:PLN03232 685 PQVSWIFNATVRENILFGSDFESE-RYWRAIDVTALQHDLDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIY 762
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 495 ILDDALSAVDGRTEHQILHN-LRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALA 558
Cdd:PLN03232 763 IFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
343-497 |
4.97e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.51 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 343 HYPENpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDD---WRSRLSVVSQTP 419
Cdd:COG2884 10 RYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRIGVVFQDF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 FLFSD-TVANNIALgqP----GATQAQIEQAARlasvheDILRLpqgydteVGERGVM------LSGGQKQRISIARALL 488
Cdd:COG2884 89 RLLPDrTVYENVAL--PlrvtGKSRKEIRRRVR------EVLDL-------VGLSDKAkalpheLSGGEQQRVAIARALV 153
|
....*....
gi 1574033397 489 LDAEILILD 497
Cdd:COG2884 154 NRPELLLAD 162
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
346-546 |
5.61e-24 |
|
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: 100.26 E-value: 5.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 346 ENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP---LPQVRLDDWRSR-LSVVSQTPFL 421
Cdd:cd03255 14 GEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKELAAFRRRhIGFVFQSFNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSD-TVANNIALGQPGATQAQIEQAARLASVHEdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:cd03255 94 LPDlTALENVELPLLLAGVPKKERRERAEELLE-RVGLGDRLNHYPSE----LSGGQQQRVAIARALANDPKIILADEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1574033397 501 SAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTEASEILVMQHG 546
Cdd:cd03255 169 GNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
341-543 |
6.42e-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: 99.64 E-value: 6.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 341 AFHYPENPHpALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLddwRSRLSVVSQTP- 419
Cdd:cd03226 6 SFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 -FLFSDTVANNIALG--QPGATQAQIEQAARLASVHEDILRLPQGydtevgergvmLSGGQKQRISIARALLLDAEILIL 496
Cdd:cd03226 82 yQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1574033397 497 DDALSAVDGRTEHQILHNLRS-WGQDRTVIISAHRLSALTEASEILVM 543
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLL 198
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
350-562 |
1.09e-23 |
|
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: 100.11 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwrSRLSVVSQTPFLFSD-TVAN 428
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALGQPGATQAQIEQAARLASVHEDILRLPQ------GYDTEvgergvmLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEIRAKVHELLKLVQldwladRYPAQ-------LSGGQRQRVALARALAVEPKVLLLDEPFGA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 503 VDGrtehQILHNLRSWGQ---DR----TVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQPG 562
Cdd:cd03296 167 LDA----KVRKELRRWLRrlhDElhvtTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
352-552 |
1.63e-23 |
|
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: 98.39 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLI--QRQFDVDQGQIRYHGLPLPqvrLDDWRSRLSVVSQTPFLFSD-TVAN 428
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPTlTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALgqpgatqaqieqAARLasvhedilrlpqgydtevgeRGvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTE 508
Cdd:cd03213 102 TLMF------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1574033397 509 HQILHNLRSWGQD-RTVIISAHRLSALTEAS--EILVMQHGGVAQRG 552
Cdd:cd03213 148 LQVMSLLRRLADTgRTIICSIHQPSSEIFELfdKLLLLSQGRVIYFG 194
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-555 |
2.41e-23 |
|
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: 99.81 E-value: 2.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGL-PLPQVRLDDWRSRLSVVSQTPf 420
Cdd:TIGR04520 8 FSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdTLDEENLWEIRKKVGMVFQNP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 lfsD------TVANNIALG------QPGATQAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALL 488
Cdd:TIGR04520 87 ---DnqfvgaTVEDDVAFGlenlgvPREEMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIAGVLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 489 LDAEILILDDALSAVD--GRTE-HQILHNLRSwGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPA 555
Cdd:TIGR04520 153 MRPDIIILDEATSMLDpkGRKEvLETIRKLNK-EEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-552 |
2.54e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 105.21 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 345 PENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQfdvdqgqiryhgLPLPQVRLDDWRSRLSVVSQTPFLFSD 424
Cdd:PLN03130 626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGE------------LPPRSDASVVIRGTVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALGQPgATQAQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:PLN03130 694 TVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1574033397 505 GRTEHQILHN-LRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRG 552
Cdd:PLN03130 773 AHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
334-555 |
3.57e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 99.70 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLS 413
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQTP---FLFSdTVANNIALG--QPGATQAQ----IEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIA 484
Cdd:PRK13635 85 MVFQNPdnqFVGA-TVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 485 RALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTEASEILVMQHGGVAQRGDPA 555
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
357-561 |
8.03e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 97.52 E-value: 8.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 357 LTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwrsR-LSVVSQTPFLFSD-TVANNIALG- 433
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSMLFQENNLFPHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 434 QPG-----ATQAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTE 508
Cdd:COG3840 97 RPGlkltaEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 509 HQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG3840 166 QEMLDLVDELCRERglTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
349-561 |
8.38e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.37 E-value: 8.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL--PQVRLDDWRSRLSVVSQTPFLFSD-T 425
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFPHlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQ---PGATQAQIEQAAR--LASV----HEDilRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILIL 496
Cdd:COG1126 94 VLENVTLAPikvKKMSKAEAEERAMelLERVgladKAD--AYPA-----------QLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 497 DDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGfAREVADRVVFMDGGRIVEEGPPEEFFENP 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
305-561 |
8.85e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.09 E-value: 8.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 305 SAAYSRIRSLLNEAPavQDGPQALPAGRG-VLEVDIRAFHYP---------ENPHPALHDLALTLKPGQMLGLCGPTGAG 374
Cdd:PRK15134 247 APTHPYTQKLLNSEP--SGDPVPLPEPASpLLDVEQLQVAFPirkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 375 KST----LLSLIQrqfdvDQGQIRYHGLPLPQV---RLDDWRSRLSVVSQTPFLFSD---TVANNIALG----QPGATQA 440
Cdd:PRK15134 325 KSTtglaLLRLIN-----SQGEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPNSSLNprlNVLQIIEEGlrvhQPTLSAA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 441 QIEQaaRLASVHEDIlrlpqGYDTEVGER-GVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWG 519
Cdd:PRK15134 400 QREQ--QVIAVMEEV-----GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQ 472
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1574033397 520 QDRTV--IISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK15134 473 QKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAP 517
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
351-561 |
1.01e-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: 97.12 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwRSRLSVVS--QTPFLFSD-TVA 427
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQPGATQAQIEQAARLASVHE---------DILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDD 498
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREareraeellERVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 499 ALSAVDGRTEHQILHNLRSW-GQDRTVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAAQP 561
Cdd:cd03219 170 PAAGLNPEETEELAELIRELrERGITVLLVEHDMDVVMSLADrVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
347-559 |
1.15e-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: 96.97 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG---LPLPQVRLDDWRSRLSVVSQTPFLFS 423
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSEKELYELRRRIGMLFQGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 D-TVANNIALG---QPGATQAQIEQAARLAsvhediLRLpqgydteVGERGVM------LSGGQKQRISIARALLLDAEI 493
Cdd:COG1127 96 SlTVFENVAFPlreHTDLSEAEIRELVLEK------LEL-------VGLPGAAdkmpseLSGGMRKRVALARALALDPEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 494 LILD------DALSAvdGRTEHQILhNLRswgqDR---TVIISAHRL-SALTEASEILVMQHGGVAQRGDPAALAA 559
Cdd:COG1127 163 LLYDeptaglDPITS--AVIDELIR-ELR----DElglTSVVVTHDLdSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-552 |
1.24e-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: 96.21 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLkPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL----PQVRLDDWRSRLSVVSQTPFLFSD-TVAN 428
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALGQPGATQAQIEQAAR--LASVHEDilrlpqgydtEVGERGVM-LSGGQKQRISIARALLLDAEILILDDALSAVDG 505
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDelLDLLGLD----------HLLNRYPAqLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1574033397 506 RTEHQILHNLRSWGQD--RTVIISAHRLS-ALTEASEILVMQHGGVAQRG 552
Cdd:cd03297 165 ALRLQLLPELKQIKKNlnIPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
343-550 |
1.26e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 343 HYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLF 422
Cdd:PRK10247 14 GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDTVANNIALgqPGATQAQIEQAARLAsvhEDILRLpqGYDTEVGERGVM-LSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:PRK10247 94 GDTVYDNLIF--PWQIRNQQPDPAIFL---DDLERF--ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 502 AVD---GRTEHQILHNLRSwGQDRTVIISAHRLSALTEASEILVMQ-HGGVAQ 550
Cdd:PRK10247 167 ALDesnKHNVNEIIHRYVR-EQNIAVLWVTHDKDEINHADKVITLQpHAGEMQ 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
352-561 |
1.68e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.39 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwrSRLSVVSQTPFLFSD-TVANNI 430
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 431 ALG--------QPGAtqAQIEQ-AARLASVHEdILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:PRK10851 96 AFGltvlprreRPNA--AAIKAkVTQLLEMVQ-LAHLADRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 502 AVDGrtehQILHNLRSWGQD-------RTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK10851 166 ALDA----QVRKELRRWLRQlheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
349-561 |
3.79e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.22 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG-----LPlPQVRlddwrsRLSVVSQTPFLF- 422
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGrdvtdLP-PKDR------NIAMVFQSYALYp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDTVANNIALG-----QPGATQAQ-IEQAARLasVH-EDIL-RLPQGydtevgergvmLSGGQKQRISIARALLLDAEIL 494
Cdd:COG3839 89 HMTVYENIAFPlklrkVPKAEIDRrVREAAEL--LGlEDLLdRKPKQ-----------LSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 495 ILD------DALSAVDGRTE-HQILHNLRSwgqdrTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG3839 156 LLDeplsnlDAKLRVEMRAEiKRLHRRLGT-----TTIYVTHDQVeAMTLADRIAVMNDGRIQQVGTPEELYDRP 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
351-552 |
9.61e-22 |
|
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: 93.80 E-value: 9.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGqMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSVVSQ--------TPFLF 422
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQefgvypnfTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDTVAnnIALGQPGATQ-AQIEQAarLASVHedilrLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:cd03264 93 LDYIA--WLKGIPSKEVkARVDEV--LELVN-----LGDRAKKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 502 AVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTE-ASEILVMQHGGVAQRG 552
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
348-546 |
1.13e-21 |
|
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: 93.36 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 348 PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQ--VRLDDWRSRLSVVSQTPFLFSD- 424
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALGQ---PGATQAQIEQAAR--LASVhedilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDA 499
Cdd:cd03262 92 TVLENITLAPikvKGMSKAEAEERALelLEKV---------GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1574033397 500 LSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLS-ALTEASEILVMQHG 546
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGfAREVADRVIFMDDG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
350-531 |
2.07e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTL---LSLIQRQfdvDQGQIRYHGLPlpqVRLDD----WRSRLSVVSQTPFLF 422
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLmkiLSGVYQP---DSGEILLDGEP---VRFRSprdaQAAGIAIIHQELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SD-TVANNIALGQPGAT------QAQIEQAAR-LASVHEDIlrLPqgyDTEVGErgvmLSGGQKQRISIARALLLDAEIL 494
Cdd:COG1129 92 PNlSVAENIFLGREPRRgglidwRAMRRRARElLARLGLDI--DP---DTPVGD----LSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1574033397 495 ILD---DALSAVDgrTEH--QILHNLRSwgQDRTVI-ISaHRL 531
Cdd:COG1129 163 ILDeptASLTERE--VERlfRIIRRLKA--QGVAIIyIS-HRL 200
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
357-560 |
8.27e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 91.57 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 357 LTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlpLPQVRLDDWRSRLSVVSQTPFLFSD-TVANNIALG-Q 434
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--QDHTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLGlN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 435 PG-----ATQAQIEQAARLASVHEDILRLPqgydtevGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH 509
Cdd:PRK10771 98 PGlklnaAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 510 QILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:PRK10771 167 EMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
349-552 |
8.61e-21 |
|
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: 91.16 E-value: 8.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqVRLDDWRSR---LSVVSQTPFLFSD- 424
Cdd:cd03301 13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-----RDVTDLPPKdrdIAMVFQNYALYPHm 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALG------QPGATQAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDD 498
Cdd:cd03301 88 TVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 499 ALSAVDGRTEHQILHNLRSWGQ--DRTVIISAH-RLSALTEASEILVMQHGGVAQRG 552
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-311 |
1.01e-20 |
|
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: 92.55 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYL---LRYVWrVLLFGAsyQLAVELRENFY 97
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAG-NTALLNRAFLLLLAVALVLALasaLRFYL-VSWLGE--RVVADLRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 98 RQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGV-------LTLVDSLVMGLVVlvvmstqiSWQLTVLALIPMPL 170
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLsialrnlLLLIGGLVMLFIT--------SPKLTLLVLLVIPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 171 MAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFAdvAAQTGAKNMHVARVDAR-FDPTIY 249
Cdd:cd18575 149 VVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFA--TAVEAAFAAALRRIRARaLLTALV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 250 IAIGASnllAIGGGSWM----VVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18575 227 IFLVFG---AIVFVLWLgahdVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
350-557 |
1.43e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.36 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLP-QVRLDdwRSRLSVVSQTPFLFSD-TVA 427
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPaRARLA--RARIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NN-IALGQP-GATQAQIEqaARLASVHEdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVDG 505
Cdd:PRK13536 133 ENlLVFGRYfGMSTREIE--AVIPSLLE-FARLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 506 RTEHQILHNLRS-WGQDRTVIISAHrlsaLTEASEIL-----VMQHGGVAQRGDPAAL 557
Cdd:PRK13536 206 HARHLIWERLRSlLARGKTILLTTH----FMEEAERLcdrlcVLEAGRKIAEGRPHAL 259
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
16-311 |
1.45e-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: 92.12 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGVTEKQMSTgvllaWLGLMIGTAIVVYLLR----YVWRVLLFGASYQLAV 90
Cdd:cd18570 1 KKLLILILLLsLLITLLGIAGSFFFQILIDDIIPSGDIN-----LLNIISIGLILLYLFQsllsYIRSYLLLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 91 ELRENFYRQLSRQNPAFYLRHRTGDLMARaTNDVDRVVFAAGEGVLTL-VDSLVMGLVVLVVMStqISWQLTVLALIPMP 169
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFETRKTGEIISR-FNDANKIREAISSTTISLfLDLLMVIISGIILFF--YNWKLFLITLLIIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 170 LMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDpTIY 249
Cdd:cd18570 153 LYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQS-SIK 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 250 IAI-GASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18570 232 GLIsLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
352-555 |
1.71e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.33 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQ-TPFLFSDTVANNI 430
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQhSSLAFPFTVEEVV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 431 ALG-QPGAT-QAQIEQAARLASVHEDILRLPQG-YDTevgergvmLSGGQKQRISIARAL--LLDAE-----ILILDDAL 500
Cdd:COG4559 97 ALGrAPHGSsAAQDRQIVREALALVGLAHLAGRsYQT--------LSGGEQQRVQLARVLaqLWEPVdggprWLFLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 501 SAVDGRTEHQILHNLRSWGQDR-TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPA 555
Cdd:COG4559 169 SALDLAHQHAVLRLARQLARRGgGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPE 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
16-295 |
1.80e-20 |
|
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: 91.89 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRE 94
Cdd:cd18782 1 RRALIEVLALsFVVQLLGLANPLLFQVIIDKVLVQQ-DLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 95 NFYRQLSRQNPAFYLRHRTGDLMARaTNDVDRV-VFAAGEGVLTLVDSLVMGLVVLVVMStqISWQLTVLALIPMPLMAI 173
Cdd:cd18782 80 TIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIrGFLTGTALTTLLDVLFSVIYIAVLFS--YSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 174 AIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIG 253
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNK 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1574033397 254 ASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALA 295
Cdd:cd18782 237 LSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLS 278
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
351-555 |
2.50e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.65 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL--PQVRLDDWRSRLSVVSQTP--FLFSDTV 426
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 427 ANNIALGqP---GATQAQIEQAARLASvheDILRLPqgYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:PRK13637 102 EKDIAFG-PinlGLSEEEIENRVKRAM---NIVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 504 DGRTEHQILHNLRSWGQDR--TVIISAHRLSALTE-ASEILVMQHGGVAQRGDPA 555
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPR 230
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
18-311 |
2.63e-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: 91.71 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 18 YLGAVVLLIVIAILQLLPPKLVGIIVDGVTE-KQMSTGVLLAWLGLMIGTAIVVYL-----LRYVWRVLLFGASYQLAVE 91
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQgSSLTLDEKVYKLFTIIGIMFFIFLilrppVEYYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 92 LRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVvfaaGEGVLTLVDSLVMGLVVLVVMSTQISW---QLTVLALIPM 168
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQT----KDFITTGLMNIWLDMITIIIAICIMLVlnpKLTFVSLVIF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 169 PLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTI 248
Cdd:cd18554 157 PFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAV 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 249 YIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18554 237 NTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
21-283 |
3.40e-20 |
|
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: 91.16 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTG---------VLLAWLGLMIGTAIVVYLlryvwRVLLFG-ASYQLAV 90
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGeealralnqAVLILLGVVLIGSIATFL-----RSWLFTlAGERVVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 91 ELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVdRVVFAAG--------EGVLTLVDSLVMGLvvlvvmstQISWQLTV 162
Cdd:cd18780 76 RLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDT-QVLQNAVtvnlsmllRYLVQIIGGLVFMF--------TTSWKLTL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 163 LALIPMPLMAIAIKYYGD---QLHQRFKSAQAAFSSLndqAQESMTSIRMIKAFGLEDHQSNRFA---DVAAQTGAKnmh 236
Cdd:cd18780 147 VMLSVVPPLSIGAVIYGKyvrKLSKKFQDALAAASTV---AEESISNIRTVRSFAKETKEVSRYSekiNESYLLGKK--- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1574033397 237 VARVDARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMY 283
Cdd:cd18780 221 LARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLY 267
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
334-554 |
3.58e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 90.58 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLS 413
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQTP---FLFSdTVANNIALGQPGATQAQIEQAARLASVHEDILRLPQGyDTEVGErgvmLSGGQKQRISIARALLLD 490
Cdd:PRK13648 87 IVFQNPdnqFVGS-IVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERA-DYEPNA----LSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 491 AEILILDDALSAVDGRTEHQILHNLRSWGQDRTV-IIS-AHRLSALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNItIISiTHDLSEAMEADHVIVMNKGTVYKEGTP 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
343-548 |
6.75e-20 |
|
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: 88.72 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 343 HYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpQVRLDDWRSRLSVVSQTPFLF 422
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SD-TVANNIALgqpgatQAQI-----EQAARLASVHEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILIL 496
Cdd:cd03263 88 DElTVREHLRF------YARLkglpkSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 497 DDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRL---SALteASEILVMQHGGV 548
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKL 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
352-559 |
6.76e-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: 89.10 E-value: 6.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLP---QVRLDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRRRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIA--LGQPGA-TQAQIEQAAR--LASV--HEDILRLPqgydtevGErgvmLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:cd03261 96 ENVAfpLREHTRlSEEEIREIVLekLEAVglRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 501 SAVDGRTEHQILHNLRSWGQ--DRTVIISAHRL-SALTEASEILVMQHGGVAQRGDPAALAA 559
Cdd:cd03261 165 AGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
350-559 |
8.06e-20 |
|
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: 88.26 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwRSRLSV--VSQTPFLFSD-TV 426
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGIgyVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 427 ANNIALGqpGATQAQIEQAARLASVHEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDA---LSAV 503
Cdd:cd03224 93 EENLLLG--AYARRRAKRKARLERVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPsegLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 504 DGRTEHQILHNLRSWGQdrTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAA 559
Cdd:cd03224 167 IVEEIFEAIRELRDEGV--TILLVEQNARfALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-576 |
1.09e-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: 90.93 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLI---QRqfdVDQGQIRYHGLPL----PQVRLDDWRSRLSVVSQTPFLFSD-T 425
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEARLFPHlS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQPGATQAQieQAARLASVHE-----DIL-RLPQGydtevgergvmLSGGQKQRISIARALLLDAEILILDDA 499
Cdd:COG4148 94 VRGNLLYGRKRAPRAE--RRISFDEVVEllgigHLLdRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 500 LSAVDGRTEHQILHNLRSWgQDRT---VIISAHrlsALTE----ASEILVMQHGGVAQRGDPAALAAQPgwyrDMYRYQQ 572
Cdd:COG4148 161 LAALDLARKAEILPYLERL-RDELdipILYVSH---SLDEvarlADHVVLLEQGRVVASGPLAEVLSRP----DLLPLAG 232
|
....
gi 1574033397 573 LEAA 576
Cdd:COG4148 233 GEEA 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
354-557 |
1.19e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.86 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQvRLDDWRSRLSVVSQTPFLFSD-TVANNI-A 431
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQFDNLDPDfTVRENLlV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 LGQP-GATQAQIEqaARLASVHEdILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQ 510
Cdd:PRK13537 104 FGRYfGLSAAAAR--ALVPPLLE-FAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1574033397 511 ILHNLRS-WGQDRTVIISAHRL-SALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:PRK13537 177 MWERLRSlLARGKTILLTTHFMeEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
352-555 |
1.42e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPlpqvrLDDWRS-----RLSVVSQTPFL-FSDT 425
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-----LADWSPaelarRRAVLPQHSSLsFPFT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALG----QPGATQAQIEQAARLASVheDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAE------ILI 495
Cdd:PRK13548 93 VEEVVAMGraphGLSRAEDDALVAAALAQV--DLAHLAGRDYPQ-------LSGGEQQRVQLARVLAQLWEpdgpprWLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 496 LDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRGDPA 555
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
60-311 |
1.42e-19 |
|
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: 89.46 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 60 LGLMIGTAIVVYLLRYVWRVllfgASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 139
Cdd:cd18577 54 VYLGIGSFVLSYIQTACWTI----TGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 140 DSlvmglvvlvvmSTQI----------SWQLTVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRM 209
Cdd:cd18577 130 QS-----------LSTFiagfiiafiySWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 210 IKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQ-LTSF--VMYLGL 286
Cdd:cd18577 199 VKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDvLTVFfaVLIGAF 278
|
250 260
....*....|....*....|....*
gi 1574033397 287 MIwpmLALAWMFNIVERGSAAYSRI 311
Cdd:cd18577 279 SL---GQIAPNLQAFAKARAAAAKI 300
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-531 |
1.70e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.17 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYpeNPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFD-VDQ----GQIRYHGLPL--PQVRLDDWRSRLSV 414
Cdd:COG1117 19 VYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEDIydPDVDVVELRRRVGM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 415 VSQTPFLFSDTVANNIALGqpgATQAQIEQAARLASVHEDILR---LpqgYDtEVGER----GVMLSGGQKQRISIARAL 487
Cdd:COG1117 97 VFQKPNPFPKSIYDNVAYG---LRLHGIKSKSELDEIVEESLRkaaL---WD-EVKDRlkksALGLSGGQQQRLCIARAL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1574033397 488 LLDAEILILDDALSAVD----GRTEhQILHNLRswgQDRTVIISAHRL 531
Cdd:COG1117 170 AVEPEVLLMDEPTSALDpistAKIE-ELILELK---KDYTIVIVTHNM 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
334-540 |
2.11e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.91 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYpeNPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVD-----QGQIRYHGLPLPQVRLD-- 406
Cdd:PRK14239 5 ILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 407 DWRSRLSVVSQTPFLFSDTVANNIALGqpgATQAQIEQAARLASVHEDILRLPQGYDtEVGER----GVMLSGGQKQRIS 482
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSIYENVVYG---LRLKGIKDKQVLDEAVEKSLKGASIWD-EVKDRlhdsALGLSGGQQQRVC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 483 IARALLLDAEILILDDALSAVD----GRTEhQILHNLRswgQDRTVIISAHrlsALTEASEI 540
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDpisaGKIE-ETLLGLK---DDYTMLLVTR---SMQQASRI 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
349-540 |
2.36e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.30 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDV-----DQGQIRYHGLPL--PQVRLDDWRSRLSVVSQTPFL 421
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTVANNIA-----LGQPGATQAQIEQAARLASVHEDIlrlpqgyDTEVGERGVMLSGGQKQRISIARALLLDAEILIL 496
Cdd:PRK14243 103 FPKSIYDNIAygariNGYKGDMDELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1574033397 497 DDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEI 540
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDM 219
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
15-295 |
2.56e-19 |
|
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: 88.69 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 15 WRRYLGAVVLLIVIAILQLLPPKLVGIIVD-GVTEKQMST--GVLLAWLGLMIGTAIVVYLL-RYVWRVllfgaSYQLAV 90
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDhFITPGTLDGltGFILLYLGLILIQALSVFLFiRLAGKI-----EMGVSY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 91 ELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVvfaaGE----GVLTLVDSLVMGLVVLVVMSTqISWQLTVLALI 166
Cdd:cd18540 76 DLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRL----GEiiswGLVDLVWGITYMIGILIVMLI-LNWKLALIVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 167 PMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDP 246
Cdd:cd18540 151 VVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 247 TI----YIAIGasnlLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALA 295
Cdd:cd18540 231 IVlflgSIATA----LVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLA 279
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
350-561 |
4.17e-19 |
|
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: 87.31 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDW----RSRLSVVSQTPFLFSD- 424
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIAL-----GQPGAT-QAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDD 498
Cdd:cd03294 118 TVLENVAFglevqGVPRAErEERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 499 ALSAVDG--RTEHQ-ILHNLRSwGQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:cd03294 187 AFSALDPliRREMQdELLRLQA-ELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
351-561 |
5.75e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 86.63 E-value: 5.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwRSRLSVVS--QTPFLFSD-TVA 427
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIARtfQNPRLFPElTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQPGATQAQI------------EQAARLASVHE--DILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEI 493
Cdd:COG0411 98 ENVLVAAHARLGRGLlaallrlprarrEEREARERAEEllERVGLADRADEPAGN----LSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 494 LILDDALSAVdGRTE-HQILHNLRSW--GQDRTVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG0411 174 LLLDEPAAGL-NPEEtEELAELIRRLrdERGITILLIEHDMDLVMGLADrIVVLDFGRVIAEGTPAEVRADP 244
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
334-554 |
6.95e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.16 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQF---DVDQGQIRYHGLPLPQVRLDDWRS 410
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 411 RLSVVSQTP---FLFSdTVANNIALGQPGATQAQIEQAARLASVHEDILRLpQGYDTEVGErgvmLSGGQKQRISIARAL 487
Cdd:PRK13640 85 KVGIVFQNPdnqFVGA-TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGML-DYIDSEPAN----LSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 488 LLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
351-591 |
7.14e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.38 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL-PQVR---LDDWRSRLSVVSQTP--FLFSD 424
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKnkkLKPLRKKVGIVFQFPehQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALGqP---GATQAQIEQAAR----LASVHEDIL-RLPqgYDtevgergvmLSGGQKQRISIARALLLDAEILIL 496
Cdd:PRK13634 102 TVEKDICFG-PmnfGVSEEDAKQKARemieLVGLPEELLaRSP--FE---------LSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 497 DDALSAVDGRTEHQI------LHNlrswGQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQPGWYRDM-- 567
Cdd:PRK13634 170 DEPTAGLDPKGRKEMmemfykLHK----EKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIgl 245
|
250 260 270
....*....|....*....|....*....|...
gi 1574033397 568 -----YRYQQ-LEAALD---EAPENGEEALADE 591
Cdd:PRK13634 246 dlpetVKFKRaLEEKFGisfPKPCLTLEELAHE 278
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
346-554 |
8.87e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 346 ENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLS-----LIQRQFDV---------DQGQIRYHGLPLPQV--RLDDWR 409
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIqvgdiyigdKKNNHELITNPYSKKikNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 410 SRLSVVSQTP--FLFSDTVANNIALGqPGATQAQIEQAARLASVHEDILrlpqGYDTEVGERGVM-LSGGQKQRISIARA 486
Cdd:PRK13631 116 RRVSMVFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKM----GLDDSYLERSPFgLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 487 LLLDAEILILDDALSAVDGRTEHQILH-NLRSWGQDRTVIISAHRLSALTE-ASEILVMQHGGVAQRGDP 554
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTP 260
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
352-529 |
8.92e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 85.40 E-value: 8.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVD---QGQIRYHGLPLpqvRLDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQPGATQAQIEQAARLASVheDILRLPQGYDTEVGERGVM-LSGGQKQRISIARALLLDAEILILDDALSAVDGR 506
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKRV--EDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....
gi 1574033397 507 TEHQILHNLRSWGQ-DRTVIISAH 529
Cdd:cd03234 178 TALNLVSTLSQLARrNRIVILTIH 201
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
335-552 |
1.33e-18 |
|
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: 84.47 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 335 LEVDIRAFHYPENPHpalhDLALTLKPGQMLGLCGPTGAGKSTLLSLIQrQFDVDQ-GQIRYHGLPLpqVRLDDWRSRLS 413
Cdd:cd03298 1 VRLDKIRFSYGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIA-GFETPQsGRVLINGVDV--TAAPPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQTPFLFSD-TVANNIALG-QPG-----ATQAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARA 486
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGlSPGlkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 487 LLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRG 552
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-555 |
1.81e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.55 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI---QRQfdvDQGQIRYHGLPL----PQVRLddwRSRLSVVSQTPFLFS 423
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILyglYQP---DSGEILIDGKPVrirsPRDAI---ALGIGMVHQHFMLVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 D-TVANNIALGQPGATQAQIeqaaRLASVHEDILRLPQGY------DTEVGErgvmLSGGQKQRISIARALLLDAEILIL 496
Cdd:COG3845 94 NlTVAENIVLGLEPTKGGRL----DRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 497 DDAlSAV--DGRTEH--QILHNLRSwgQDRTVIISAHRLSALTEAS-EILVMQHGGVAQRGDPA 555
Cdd:COG3845 166 DEP-TAVltPQEADElfEILRRLAA--EGKSIIFITHKLREVMAIAdRVTVLRRGKVVGTVDTA 226
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
21-283 |
2.03e-18 |
|
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: 85.83 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVT----EKQMSTGVLLAWLgLMIGTAIVVYLlryvwRVLLFG-ASYQLAVELREN 95
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVieksQDKFSRAIIIMGL-LAIASSVAAGI-----RGGLFTlAMARLNIRIRNL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 96 FYRQLSRQNPAFYLRHRTGDLMARATNDVDRV---------VFAA----GEGVLTLVDSlvmglvvlvvmstqISWQLTV 162
Cdd:cd18784 75 LFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMsdtvslnlnIFLRslvkAIGVIVFMFK--------------LSWQLSL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 163 LALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDA 242
Cdd:cd18784 141 VTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1574033397 243 RFDPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMY 283
Cdd:cd18784 221 GYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILY 261
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
334-561 |
2.45e-18 |
|
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: 86.26 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEV-DIR-AFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTL-LSLIQ--RQFDVDQGQIRYHG---LPLPQVRL 405
Cdd:COG0444 1 LLEVrNLKvYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGllPPPGITSGEILFDGedlLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 406 DDWR-SRLSVVSQTPF-----LFS--DTVANNIALGQpGATQAQIEQAAR--LASVH----EDILRLpqgYDTEvgergv 471
Cdd:COG0444 81 RKIRgREIQMIFQDPMtslnpVMTvgDQIAEPLRIHG-GLSKAEARERAIelLERVGlpdpERRLDR---YPHE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 472 mLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTE-ASEILVMQHGGV 548
Cdd:COG0444 151 -LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEiADRVAVMYAGRI 229
|
250
....*....|...
gi 1574033397 549 AQRGDPAALAAQP 561
Cdd:COG0444 230 VEEGPVEELFENP 242
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
349-554 |
2.65e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.92 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDdwRSRLSVVSQTPFLFSD-TVA 427
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPHmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQPGATQAQIEQAARLasvhEDILRLPQgyDTEVGERGV-MLSGGQKQRISIARALLLDAEILILDDALSAVDGR 506
Cdd:PRK09452 105 ENVAFGLRMQKTPAAEITPRV----MEALRMVQ--LEEFAQRKPhQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 507 TEHQILHNL----RSWGQdrTVIISAH-RLSALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK09452 179 LRKQMQNELkalqRKLGI--TFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
351-561 |
2.94e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.89 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpQVRLDDWRSRL-SVVSQTPflfsdtvanN 429
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYKYRCKHiRMIFQDP---------N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 IALgQPGATQAQI-EQAARLASVHEDILRLPQGYDT--EVGERG-------VMLSGGQKQRISIARALLLDAEILILDDA 499
Cdd:COG4167 98 TSL-NPRLNIGQIlEEPLRLNTDLTAEEREERIFATlrLVGLLPehanfypHMLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 500 LSAVDGRTEHQILhNLRSWGQDR---TVIISAHRLSALTEAS-EILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG4167 177 LAALDMSVRSQII-NLMLELQEKlgiSYIYVSQHLGIVKHISdKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
21-311 |
3.70e-18 |
|
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: 85.29 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVllAWLGLMIGTA---IVVYLLR----YVWRVLLFGASYQLAVELR 93
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSLKETNG--DFIEDLKKPAlklLGLYLLQslltFAYISLLSVVGERVAARLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 94 ENFYRQLSRQNPAFYLRHRTGDLMARATNDVD--------------RVVFAAGEGVLTLVdslvmglvvlvvmstQISWQ 159
Cdd:cd18574 79 NDLFSSLLRQDIAFFDTHRTGELVNRLTADVQefkssfkqcvsqglRSVTQTVGCVVSLY---------------LISPK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 160 LTVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFAdvaaqtgAKNMHVAR 239
Cdd:cd18574 144 LTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYE-------EEVEKAAK 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 240 VDARFDPTIYIAIGASNlLAIGG--------GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18574 217 LNEKLGLGIGIFQGLSN-LALNGivlgvlyyGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
351-561 |
4.78e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 85.40 E-value: 4.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTL---LSLIQRQfdvDQGQIRYHGLPL---PQVRLDDWRSRLSVVSQTPF--LF 422
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIETP---TGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPYgsLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDTVANNIaLGQPGATQAQIEQAARLASVHEDILRLpqGYDTEVGER-GVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:PRK11308 107 PRKKVGQI-LEEPLLINTSLSAAERREKALAMMAKV--GLRPEHYDRyPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 502 AVDGRTEHQILhNLRSWGQDRT----VIISaHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK11308 184 ALDVSVQAQVL-NLMMDLQQELglsyVFIS-HDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
349-560 |
6.57e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 6.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDW----RSRLSVVSQTP--FLF 422
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpvRKRIGMVFQFPesQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDTVANNIALGqPGATQAQIEQAARLAsvHEDILRLpqGYdtevgERGVM------LSGGQKQRISIARALLLDAEILIL 496
Cdd:PRK13646 100 EDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDL--GF-----SRDVMsqspfqMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 497 DDALSAVDGRTEHQILHNLRSWG--QDRTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
352-561 |
6.89e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 83.65 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRY------HGLPLPQVR--LDDWRSRLSVVSQTPFLFS 423
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKglIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 D-TVANNIALGQ---PGATQAQIEQAAR--LASVHEdilrlpQGYDTEVGERgvmLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK11264 99 HrTVLENIIEGPvivKGEPKEEATARARelLAKVGL------AGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 498 DALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
344-529 |
7.28e-18 |
|
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: 82.46 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 344 YPENpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP---LPQVRLDDWRSRLSVVSQTPF 420
Cdd:cd03292 10 YPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRKIGVVFQDFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 LFSD-TVANNIALG------QPGATQAQIEQAARLASVHEDILRLPQGydtevgergvmLSGGQKQRISIARALLLDAEI 493
Cdd:cd03292 89 LLPDrNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTI 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1574033397 494 LILDDALSAVDGRTEHQILHNLRSWGQ-DRTVIISAH 529
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATH 194
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
334-558 |
8.87e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 83.63 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHpALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLS 413
Cdd:PRK13647 4 IIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQTP--FLFSDTVANNIALG--QPGATQAQIEQAAR--LASVHEDILRLPQGYDtevgergvmLSGGQKQRISIARAL 487
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEeaLKAVRMWDFRDKPPYH---------LSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 488 LLDAEILILDDALSAVDGR---TEHQILHNLRSWGqdRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALA 558
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRgqeTLMEILDRLHNQG--KTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLT 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
350-547 |
1.00e-17 |
|
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: 83.32 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVrldDWRSRLSVVSQTPFLFSDTVAN- 428
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL---DRKQRRAFRRDVQLVFQDSPSAv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 ------NIALGQPGATQAQIEQAARLASVHEdILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:TIGR02769 102 nprmtvRQIIGEPLRHLTSLDESEQKARIAE-LLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1574033397 503 VDGRTEHQILHNLRSWGQD--RTVIISAHRLSALTEASEILVMQHGG 547
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQAfgTAYLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
350-561 |
1.15e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.89 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVrlDDWRSRLSVVSQTPFLFSD-TVAN 428
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALGQPGATQAQIEQAAR----LASVH--EDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRvnemLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 503 VD----GRTEHQILHNLRSWGQDrTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK11607 180 LDkklrDRMQLEVVDILERVGVT-CVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHP 241
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
349-555 |
1.58e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 82.44 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:COG4604 14 KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRlTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALG-------QPGAT-QAQIEQA-ARLasvheDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAEILILDD 498
Cdd:COG4604 94 ELVAFGrfpyskgRLTAEdREIIDEAiAYL-----DLEDLADRYLDE-------LSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 499 ALSAVDGRTEHQILHNLRSW--GQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPA 555
Cdd:COG4604 162 PLNNLDMKHSVQMMKLLRRLadELGKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTPE 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
334-560 |
1.59e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.24 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENP-HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRL 412
Cdd:PRK13650 4 IIEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTP---FLFSdTVANNIALGQPGA------TQAQIEQAARLASVHEDILRLPqgydtevgergVMLSGGQKQRISI 483
Cdd:PRK13650 84 GMVFQNPdnqFVGA-TVEDDVAFGLENKgipheeMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 484 ARALLLDAEILILDDALSAVD--GRTEH-QILHNLRSWGQdRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDpeGRLELiKTIKGIRDDYQ-MTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
340-552 |
1.90e-17 |
|
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: 81.26 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 340 RAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwRSRLSVVSQTP 419
Cdd:cd03266 9 KRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA-RRRLGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 FLFSD-TVANNIAL--GQPGATQAQIEqaARLASVhEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILIL 496
Cdd:cd03266 88 GLYDRlTARENLEYfaGLYGLKGDELT--ARLEEL-ADRLGMEELLDRRVGG----FSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 497 DDALSAVD---GRTEHQILHNLRSWGqdRTVIISAHRLSALTE-ASEILVMQHGGVAQRG 552
Cdd:cd03266 161 DEPTTGLDvmaTRALREFIRQLRALG--KCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
351-572 |
3.05e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQ--IRYHGLP--LPQVR-LDDWRSRLSVVSQTP--FLFS 423
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtiVGDYAIPanLKKIKeVKRLRKEIGLVFQFPeyQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 DTVANNIALGqPGATQAQIEQAARLASVHEDILRLPQGYdteVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:PRK13645 106 ETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 504 DGRTEHQILH---NLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQ-----------PGWYRDMYR 569
Cdd:PRK13645 182 DPKGEEDFINlfeRLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNqelltkieidpPKLYQLMYK 261
|
...
gi 1574033397 570 YQQ 572
Cdd:PRK13645 262 LKN 264
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-561 |
5.51e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.47 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP---LPQVRLDDWRSRLSVVSQTPFLFSD--- 424
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDPYASLNprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANniALGQPGATQAQIEQAARLASVHEdILRLpQGYDTEVGER-GVMLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:COG4608 113 TVGD--IIAEPLRIHGLASKAERRERVAE-LLEL-VGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 504 DGRTEHQILhNLRSWGQDR---TVIISAHRLSALTEAS-EILVMQHGGVAQRGDPAALAAQP 561
Cdd:COG4608 189 DVSIQAQVL-NLLEDLQDElglTYLFISHDLSVVRHISdRVAVMYLGKIVEIAPRDELYARP 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
347-552 |
5.96e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.08 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP------------LPQVRLDDWrsrlsv 414
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPtrqalqknlvayVPQSEEVDW------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 415 vsQTPFLFSDTV-----ANNIALGQPGATQAQIEQAArLASVHEDILRLPQgydteVGErgvmLSGGQKQRISIARALLL 489
Cdd:PRK15056 92 --SFPVLVEDVVmmgryGHMGWLRRAKKRDRQIVTAA-LARVDMVEFRHRQ-----IGE----LSGGQKKRVFLARAIAQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 490 DAEILILDDALSAVDGRTEHQILHNLRSW-GQDRTVIISAHRLSALTEASEILVMQHGGVAQRG 552
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-543 |
6.29e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.06 E-value: 6.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 335 LEVDIRAFHYPEN--PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL--PQVRlddwrs 410
Cdd:COG4525 4 LTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgPGAD------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 411 RlSVVSQT----PFLfsdTVANNIALGQ--PGATQAQIEQAArlasvhEDILRLpqgydteVGERGV------MLSGGQK 478
Cdd:COG4525 78 R-GVVFQKdallPWL---NVLDNVAFGLrlRGVPKAERRARA------EELLAL-------VGLADFarrriwQLSGGMR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 479 QRISIARALLLDAEILILDDALSAVDGRTEHQI-LHNLRSWGQ-DRTVIISAHRL-SALTEASEILVM 543
Cdd:COG4525 141 QRVGIARALAADPRFLLMDEPFGALDALTREQMqELLLDVWQRtGKGVFLITHSVeEALFLATRLVVM 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
349-561 |
6.35e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.44 E-value: 6.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG--------LPLPQVRLddWRSRLSVVSQT-- 418
Cdd:COG4161 15 HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIRL--LRQKVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 --PFLfsdTVANNI------ALGQpgATQAQIEQAARLASVhediLRLpqgydTEVGERGVM-LSGGQKQRISIARALLL 489
Cdd:COG4161 93 lwPHL---TVMENLieapckVLGL--SKEQAREKAMKLLAR----LRL-----TDKADRFPLhLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 490 DAEILILDDALSAVDGRTEHQILHNLRSWGQDR-TVIISAHRLS-ALTEASEILVMQHGGVAQRGDpAALAAQP 561
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEfARKVASQVVYMEKGRIIEQGD-ASHFTQP 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-559 |
7.20e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.82 E-value: 7.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPEnpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVR--LDDWRSRLSVVSQTP 419
Cdd:PRK13638 9 FRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 --FLFSDTVANNIALGQPGATQAQIEQAARLasvhEDILRL--PQGYDTEVGErgvMLSGGQKQRISIARALLLDAEILI 495
Cdd:PRK13638 87 eqQIFYTDIDSDIAFSLRNLGVPEAEITRRV----DEALTLvdAQHFRHQPIQ---CLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 496 LDDALSAVDGRTEHQILHNLRSW-GQDRTVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAA 559
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEISDaVYVLRQGQILTHGAPGEVFA 225
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
349-547 |
9.48e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 79.18 E-value: 9.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpqVRLDDWRSRLSVVSQTPFLFSD-TVA 427
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIGALIEAPGFYPNlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQ--PGATQAQIEQAarlasvhEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVD- 504
Cdd:cd03268 91 ENLRLLArlLGIRKKRIDEV-------LDVVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDEPTNGLDp 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1574033397 505 -GRTE-HQILHNLRSWGqdRTVIISAHRLSALTEASEILVMQHGG 547
Cdd:cd03268 160 dGIKElRELILSLRDQG--ITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
334-561 |
9.81e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHpALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLP--QVRLDDWRSR 411
Cdd:PRK13639 1 ILETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 412 LSVVSQTP--FLFSDTVANNIALGqP---GATQAQIEQaarlaSVHEDILRLP-QGYDTEVGERgvmLSGGQKQRISIAR 485
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFG-PlnlGLSKEEVEK-----RVKEALKAVGmEGFENKPPHH---LSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 486 ALLLDAEILILDDALSAVDGRTEHQI---LHNLRSWGQdrTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQImklLYDLNKEGI--TIIISTHDVDlVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
352-497 |
1.30e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.81 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrldDWrsRLSVVSQTPFLFSD-TVANNI 430
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---------GL--RIGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 431 --ALGQPGATQAQIEQA-----------ARLASVHEDI------------------LRLPQG-YDTEVGErgvmLSGGQK 478
Cdd:COG0488 83 ldGDAELRALEAELEELeaklaepdedlERLAELQEEFealggweaearaeeilsgLGFPEEdLDRPVSE----LSGGWR 158
|
170
....*....|....*....
gi 1574033397 479 QRISIARALLLDAEILILD 497
Cdd:COG0488 159 RRVALARALLSEPDLLLLD 177
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
350-511 |
1.31e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.74 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqVRLDDWRSRLSVVSQTPFLFS-DTVAN 428
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQNEGLLPwRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALG--QPGATQAQIEQAAR--LASVHEDilrlpqgydtEVGERGV-MLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:PRK11248 90 NVAFGlqLAGVEKMQRLEIAHqmLKKVGLE----------GAEKRYIwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
....*...
gi 1574033397 504 DGRTEHQI 511
Cdd:PRK11248 160 DAFTREQM 167
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
343-555 |
1.63e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.16 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 343 HYPENPHP--ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL----PQVRLDDWRSRLSVVS 416
Cdd:PRK13643 11 YQPNSPFAsrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPVRKKVGVVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 417 QTP--FLFSDTVANNIALGqPGATQAQIEQAARLASVHEDILrlpqGYDTEVGERGVM-LSGGQKQRISIARALLLDAEI 493
Cdd:PRK13643 91 QFPesQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAEKLEMV----GLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 494 LILDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPA 555
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
334-561 |
1.75e-16 |
|
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: 78.87 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEV-DIRAfHYPENPhpALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwRSRL 412
Cdd:COG0410 3 MLEVeNLHA-GYGGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHR-IARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SV--VSQTPFLFSD-TVANNIALGQPGATQAQiEQAARLASVHEdilRLPqgydtEVGER----GVMLSGGQKQRISIAR 485
Cdd:COG0410 79 GIgyVPEGRRIFPSlTVEENLLLGAYARRDRA-EVRADLERVYE---LFP-----RLKERrrqrAGTLSGGEQQMLAIGR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 486 ALLLDAEILILDDAlsavdgrTE----------HQILHNLRSwgQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDP 554
Cdd:COG0410 150 ALMSRPKLLLLDEP-------SLglapliveeiFEIIRRLNR--EGVTILLVEQNARfALEIADRAYVLERGRIVLEGTA 220
|
....*..
gi 1574033397 555 AALAAQP 561
Cdd:COG0410 221 AELLADP 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
342-516 |
1.93e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG-----LPLPQVRLDdwRSRLSVVS 416
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltaLSEKELRKA--RRQIGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 417 QTpF--LFSDTVANNIALgqP----GATQAQIEqaarlASVHE--DILRLPQGYDTEVGErgvmLSGGQKQRISIARALL 488
Cdd:PRK11153 89 QH-FnlLSSRTVFDNVAL--PlelaGTPKAEIK-----ARVTEllELVGLSDKADRYPAQ----LSGGQKQRVAIARALA 156
|
170 180
....*....|....*....|....*...
gi 1574033397 489 LDAEILILDDALSAVDGRTEHQILHNLR 516
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLK 184
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-559 |
2.49e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.37 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHY-PENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRL 412
Cdd:PRK13642 4 ILEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTP--FLFSDTVANNIALGQPGATQAQIEQAARlasVHEDILRLPQ-GYDTEVGERgvmLSGGQKQRISIARALLL 489
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKR---VDEALLAVNMlDFKTREPAR---LSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 490 DAEILILDDALSAVD--GRTE-HQILHNLRSwGQDRTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAA 559
Cdd:PRK13642 158 RPEIIILDESTSMLDptGRQEiMRVIHEIKE-KYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
351-569 |
2.54e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 81.23 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRS----RLSVVSQTPFLFSD-T 425
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQ--PGATQAQIEQAARLASVHEDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:PRK10070 123 VLDNTAFGMelAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 504 DG--RTEHQI-LHNLRSWGQdRTVIISAHRL-SALTEASEILVMQHGGVAQRGDPAALAAQPG--WYRDMYR 569
Cdd:PRK10070 196 DPliRTEMQDeLVKLQAKHQ-RTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndYVRTFFR 266
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
343-561 |
2.71e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.86 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 343 HYPEnpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDD-------------WR 409
Cdd:PRK10619 14 RYGE--HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 410 SRLSVVSQTPFLFSD-TVANNIaLGQP----GATQAQI-EQAAR-LASVHEDilrlpqgyDTEVGERGVMLSGGQKQRIS 482
Cdd:PRK10619 92 TRLTMVFQHFNLWSHmTVLENV-MEAPiqvlGLSKQEArERAVKyLAKVGID--------ERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 483 IARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAALAAQ 560
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGfARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
.
gi 1574033397 561 P 561
Cdd:PRK10619 243 P 243
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
354-557 |
4.94e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 4.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQiryhgLPLPQVRLDDW----RSrLSVVSQTPFLFSD-TVAN 428
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD-----LFIGEKRMNDVppaeRG-VGMVFQSYALYPHlSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALGQ--PGATQAQIEQaaRLASVHEdILRLPQGYDtevgERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDG- 505
Cdd:PRK11000 95 NMSFGLklAGAKKEEINQ--RVNQVAE-VLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAa 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 506 -----RTEHQILHN-LRswgqdRTVIISAH-RLSALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:PRK11000 168 lrvqmRIEISRLHKrLG-----RTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
347-561 |
5.24e-16 |
|
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: 77.58 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDwRSRLSV--VSQTPFLFSD 424
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyLPQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 -TVANNIALGQPGATQAQIEQAARLASVHED--ILRLPQgydtevgERGVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:cd03218 90 lTVEENILAVLEIRGLSKKEREEKLEELLEEfhITHLRK-------SKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 502 AVDGRTEH---QILHNLRSWGQdrTVIISAHrlsaltEASEIL-------VMQHGGVAQRGDPAALAAQP 561
Cdd:cd03218 163 GVDPIAVQdiqKIIKILKDRGI--GVLITDH------NVRETLsitdrayIIYEGKVLAEGTPEEIAANE 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
343-546 |
5.50e-16 |
|
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: 75.54 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 343 HYPenPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlddwrsrlsvvsqTPFLF 422
Cdd:cd03216 9 RFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDtvannialgqpgATQAQieqAARLASVHEdilrlpqgydtevgergvmLSGGQKQRISIARALLLDAEILILDD---A 499
Cdd:cd03216 67 AS------------PRDAR---RAGIAMVYQ-------------------LSVGERQMVEIARALARNARLLILDEptaA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1574033397 500 LSAVDGRTEHQILHNLRSwgQDRTVIISAHRLSALTE-ASEILVMQHG 546
Cdd:cd03216 113 LTPAEVERLFKVIRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
349-553 |
8.08e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 77.36 E-value: 8.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTL--------------LSLIQRQFD----VDQGQIRyhglplpqvrldDWRS 410
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLlrvlnllemprsgtLNIAGNHFDfsktPSDKAIR------------ELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 411 RLSVVSQT----PFLfsdTVANNI------ALGQpgATQAQIEQAARLAsvheDILRLpqgydTEVGERGVM-LSGGQKQ 479
Cdd:PRK11124 83 NVGMVFQQynlwPHL---TVQQNLieapcrVLGL--SKDQALARAEKLL----ERLRL-----KPYADRFPLhLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 480 RISIARALLLDAEILILDDALSAVDGRTEHQ---ILHNLRSWGQdrTVIISAHRLS-ALTEASEILVMQHGGVAQRGD 553
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQivsIIRELAETGI--TQVIVTHEVEvARKTASRVVYMENGHIVEQGD 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
347-534 |
8.69e-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: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLP---LPQVRlddwRSRL-SVVSQTPFL- 421
Cdd:COG1101 17 NEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK----RAKYiGRVFQDPMMg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 --FSDTVANNIAL----GQ-----PGATQAQIEQ-AARLASVH---EDilRLpqgyDTEVGergvMLSGGQKQRISIARA 486
Cdd:COG1101 93 taPSMTIEENLALayrrGKrrglrRGLTKKRRELfRELLATLGlglEN--RL----DTKVG----LLSGGQRQALSLLMA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1574033397 487 LLLDAEILILDDALSAVDGRTEHQILhnlrswgqDRTV-IISAHRLSAL 534
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVL--------ELTEkIVEENNLTTL 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
341-561 |
1.32e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 77.33 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 341 AFHYPENPhPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQV-RLDDWRSRLSVVSQTP 419
Cdd:PRK13644 8 SYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 --FLFSDTVANNIALGQPGATQAQIEQAARLASVHEDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK13644 87 etQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 498 DALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLSALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
345-568 |
1.35e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 1.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 345 PENPHPA--LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL-PQV---RLDDWRSRLSVVSQT 418
Cdd:PRK13641 14 PGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETgnkNLKKLRKKVSLVFQF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 P--FLFSDTVANNIALGQP--GATqaqiEQAARLASVhEDILRLpqGYDTEVGERGVM-LSGGQKQRISIARALLLDAEI 493
Cdd:PRK13641 94 PeaQLFENTVLKDVEFGPKnfGFS----EDEAKEKAL-KWLKKV--GLSEDLISKSPFeLSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 494 LILDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQPGWYRDMY 568
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWLKKHY 243
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
92-298 |
1.42e-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: 77.38 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 92 LRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRV--VFAAGEGVL--TLVDSLVMGLVVLVvmstqISWQLTVLALIP 167
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMsrSVALNANVLlrSLVKTLGMLGFMLS-----LSWQLTLLTLIE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 168 MPLMAIAIKYYgDQLHQRFKSA-QAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTgaknmhvARVDARFDP 246
Cdd:cd18590 146 MPLTAIAQKVY-NTYHQKLSQAvQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERT-------YNLKDRRDT 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 247 TIYIAIGASNLLAIG-------GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMF 298
Cdd:cd18590 218 VRAVYLLVRRVLQLGvqvlmlyCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIY 276
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-546 |
1.54e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 337 VDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVD-----QGQIRYHGLPLPQ--VRLDDWR 409
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 410 SRLSVVSQTPFLFSDTVANNIALG------QPGATQAQI-EQAARLASVHEDIlrlpqgyDTEVGERGVMLSGGQKQRIS 482
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEI-------KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 483 IARALLLDAEILILDDALSAVDG----RTEHqILHNLRsWGQDRTVIISAHRLSALTEASEILVMQHG 546
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPiasmKVES-LIQSLR-LRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
347-587 |
1.85e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQrqfdvdqGQIRYHGLPLPQVRL-------------DDWRSRls 413
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS-------GLITGDKSAGSHIELlgrtvqregrlarDIRKSR-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 vvSQTPFLFSD-------TVANNIALGQPGAT-----------QAQIEQAARLAsvhedilrlpqgydTEVG------ER 469
Cdd:PRK09984 86 --ANTGYIFQQfnlvnrlSVLENVLIGALGSTpfwrtcfswftREQKQRALQAL--------------TRVGmvhfahQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 470 GVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHG 546
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1574033397 547 GVAQRGDPAALaaqpgwyrDMYRYQQLEAALDEAPENGEEA 587
Cdd:PRK09984 230 HVFYDGSSQQF--------DNERFDHLYRSINRVEENAKAA 262
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
334-573 |
3.00e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.43 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHpALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVR--LDDWRSR 411
Cdd:PRK13636 5 ILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkgLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 412 LSVVSQTP--FLFSDTVANNIALG--QPGATQAQIEQAARLASVHEDILRLPQgydtevgERGVMLSGGQKQRISIARAL 487
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 488 LLDAEILILDDALSAVDGRTEHQILHNLRSW--GQDRTVIISAHRLSALT-EASEILVMQHGGVAQRGDPAALAAQpgwy 564
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqkELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE---- 232
|
....*....
gi 1574033397 565 RDMYRYQQL 573
Cdd:PRK13636 233 KEMLRKVNL 241
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-561 |
3.09e-15 |
|
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: 77.46 E-value: 3.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVR----LDDWRSRLSVVSQTPFLFSD-TVAN 428
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALG----QPGATQAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:TIGR02142 95 NLRYGmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 505 GRTEHQILHNLRSWGQ--DRTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
352-557 |
3.71e-15 |
|
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: 75.51 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQ-FDVDQGQIRYHGLPLPQVRLDDWRSRLSVVS---QTPFLFSDTVA 427
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGLVSpalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 N--------NIALGQPgATQAQIEQAARLAsvheDILRLpqgydTEVGERGV-MLSGGQKQRISIARALLLDAEILILDD 498
Cdd:COG1119 99 DvvlsgffdSIGLYRE-PTDEQRERARELL----ELLGL-----AHLADRPFgTLSQGEQRRVLIARALVKDPELLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 499 ALSAVDGRTEHQILHNLRSWGQD--RTVIISAHRLSALTEA-SEILVMQHGGVAQRGDPAAL 557
Cdd:COG1119 169 PTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEV 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
352-548 |
4.01e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.88 E-value: 4.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRS-RLSVvsQTPFLFSDTVAN-- 428
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfRRDI--QMVFQDSISAVNpr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 ---NIALGQPGATQAQIEQAARLASVHEdILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDG 505
Cdd:PRK10419 106 ktvREIIREPLRHLLSLDKAERLARASE-MLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1574033397 506 RTEHQILHNLRSWGQDR---TVIISaHRLSaLTE--ASEILVMQHGGV 548
Cdd:PRK10419 185 VLQAGVIRLLKKLQQQFgtaCLFIT-HDLR-LVErfCQRVMVMDNGQI 230
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
352-551 |
4.41e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRyhglpLPQvrlddwRSRLSVVSQTPFLFSDTVANNIA 431
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-----RPA------GARVLFLPQRPYLPLGTLREALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 LGQPGA--TQAQIEQAARLASVHEDILRLpqgyDTEVgERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH 509
Cdd:COG4178 448 YPATAEafSDAELREALEAVGLGHLAERL----DEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEA 522
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1574033397 510 QILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGGVAQR 551
Cdd:COG4178 523 ALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
9-321 |
5.15e-15 |
|
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: 76.34 E-value: 5.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 9 WYFRREWRRYLGAVVLLIVIAILQllpP-------KLVGIIVDGVTEKQMSTGVL--LAWLGLMIGTAIVVYLLRYvwrv 79
Cdd:cd18578 2 KLNKPEWPLLLLGLIGAIIAGAVF---PvfailfsKLISVFSLPDDDELRSEANFwaLMFLVLAIVAGIAYFLQGY---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 80 lLFG-ASYQLAVELRENFYRQLSRQNPAFYLR--HRTGDLMARATNDVDRVVFAAGEGVLTLVDSLvmglvvlvvmSTQI 156
Cdd:cd18578 75 -LFGiAGERLTRRLRKLAFRAILRQDIAWFDDpeNSTGALTSRLSTDASDVRGLVGDRLGLILQAI----------VTLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 157 ---------SWQLTVLALIPMPLMAIAIKYYGdQLHQRF-KSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADV 226
Cdd:cd18578 144 agliiafvyGWKLALVGLATVPLLLLAGYLRM-RLLSGFeEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 227 AAQTGAKNMHVARVDArfdptiyIAIGASNLLAIGG-------GSWMVVNGSLTLGQL--TSFVMYLGLMIWpMLALAWM 297
Cdd:cd18578 223 LEEPLKKGLRRALISG-------LGFGLSQSLTFFAyalafwyGGRLVANGEYTFEQFfiVFMALIFGAQSA-GQAFSFA 294
|
330 340
....*....|....*....|....
gi 1574033397 298 FNIVeRGSAAYSRIRSLLNEAPAV 321
Cdd:cd18578 295 PDIA-KAKAAAARIFRLLDRKPEI 317
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
352-552 |
9.92e-15 |
|
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: 73.65 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDdwrsRLSVVSQTPFLFSDTVANNIA 431
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD----RMVVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 LGQpGATQAQIEQAARLASV--HEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH 509
Cdd:TIGR01184 77 LAV-DRVLPDLSKSERRAIVeeHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1574033397 510 QILHNL-RSWGQDR-TVIISAHRL-SALTEASEILVMQHGGVAQRG 552
Cdd:TIGR01184 152 NLQEELmQIWEEHRvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
350-497 |
1.07e-14 |
|
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: 73.62 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYH--GLPLPQVRLDDW------RSRLSVVSQtpFL 421
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdGGWVDLAQASPReilalrRRTIGYVSQ--FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FS-------DTVANN-IALGQPGATqAQiEQAARLASVhediLRLPqgydtevgERgvmL--------SGGQKQRISIAR 485
Cdd:COG4778 103 RViprvsalDVVAEPlLERGVDREE-AR-ARARELLAR----LNLP--------ER---LwdlppatfSGGEQQRVNIAR 165
|
170
....*....|..
gi 1574033397 486 ALLLDAEILILD 497
Cdd:COG4778 166 GFIADPPLLLLD 177
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
354-561 |
1.22e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.53 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplPQVRLDDWRSR-LSVVSQTPFLFSD-TVANNIA 431
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQQRdICMVFQSYALFPHmSLGENVG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 LG--QPGATQAQIEQAARLASVHEDIlrlpQGYdtevGERGV-MLSGGQKQRISIARALLLDAEILILDDALSAVDGRTE 508
Cdd:PRK11432 101 YGlkMLGVPKEERKQRVKEALELVDL----AGF----EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 509 HQILHNLRSWgQDRTVIISAHRLSALTEA----SEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK11432 173 RSMREKIREL-QQQFNITSLYVTHDQSEAfavsDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
16-311 |
1.36e-14 |
|
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: 74.52 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRE 94
Cdd:cd18568 1 RKLLAEILLAsLLLQLLGLALPLFTQIILDRVLVHK-NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 95 NFYRQLSRQNPAFYLRHRTGDLMARAT-NDVDRVvFAAGEGVLTLVDSLVMGLVVLVVMStqISWQLTVLALIPMPLMAI 173
Cdd:cd18568 80 DFYKHLLSLPLSFFASRKVGDIITRFQeNQKIRR-FLTRSALTTILDLLMVFIYLGLMFY--YNLQLTLIVLAFIPLYVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 174 AIKYYGDQLHqrfKSAQAAFSSLNDQAQ---ESMTSIRMIKAFGLED----HQSNRFAdvaaqtgaKNMHVARVDARFDP 246
Cdd:cd18568 157 LTLLSSPKLK---RNSREIFQANAEQQSflvEALTGIATIKALAAERpirwRWENKFA--------KALNTRFRGQKLSI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1574033397 247 TIYIAIGA----SNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18568 226 VLQLISSLinhlGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
351-561 |
1.53e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTP--FLFSDTVAN 428
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALG------QPGATQAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:PRK13652 99 DIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 503 VD--GRTEHQILHNLRSWGQDRTVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK13652 168 LDpqGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADyIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
328-547 |
2.00e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 328 LPAGRGVLEV-DIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQ------GQIRYHGLPL 400
Cdd:PRK14246 1 MEAGKSAEDVfNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 401 PQVRLDDWRSRLSVVSQTPFLFSD-TVANNIALgqPGATQAqIEQAARLASVHEDILRlPQGYDTEVGER----GVMLSG 475
Cdd:PRK14246 81 FQIDAIKLRKEVGMVFQQPNPFPHlSIYDNIAY--PLKSHG-IKEKREIKKIVEECLR-KVGLWKEVYDRlnspASQLSG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 476 GQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSALTEASEILVMQHGG 547
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
351-557 |
2.94e-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: 72.56 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL----PQVRLddwRSRLSVVSQTPFLFSD-T 425
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklpPHERA---RAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALG---QPGATQAQIEQAARLASVHEDILrlpqgydtevGERGVMLSGGQKQRISIARALLLDAEILILDDAlsa 502
Cdd:TIGR03410 92 VEENLLTGlaaLPRRSRKIPDEIYELFPVLKEML----------GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP--- 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 503 vdgrTE----------HQILHNLRSWGqDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:TIGR03410 159 ----TEgiqpsiikdiGRVIRRLRAEG-GMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
352-554 |
3.31e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.74 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSD-TVANNI 430
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRELV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 431 ALGQP----------GATQAQIEQAarlasvhedilrLPQGYDTEVGERGVM-LSGGQKQRISIARALLLDAEILILDDA 499
Cdd:PRK11231 98 AYGRSpwlslwgrlsAEDNARVNQA------------MEQTRINHLADRRLTdLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 500 LSAVDgrTEHQI-----LHNLRSWGqdRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK11231 166 TTYLD--INHQVelmrlMRELNTQG--KTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTP 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
352-548 |
3.56e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.79 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDdwrsrlsvvsqTPFLFSD------- 424
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----------TRLMFQDarllpwk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALGQPGATQAQIEQAarLASVhedilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:PRK11247 97 KVIDNVGLGLKGQWRDAALQA--LAAV---------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1574033397 505 G--RTEHQILHNlRSWGQDR-TVIISAHRLS-ALTEASEILVMQHGGV 548
Cdd:PRK11247 166 AltRIEMQDLIE-SLWQQHGfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
350-546 |
3.78e-14 |
|
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: 72.37 E-value: 3.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLpLPQVRLDDWRSRLSVV-SQTPFLFSD-TVA 427
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfGQKTQLWWDlPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQ------PGATQAQIEQAARLASVhEDILrlpqgyDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:cd03267 114 DSFYLLAaiydlpPARFKKRLDELSELLDL-EELL------DTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1574033397 502 AVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTE-ASEILVMQHG 546
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKG 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
351-546 |
4.33e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTL---LSLIQRQFDVDqGQIRYHGLPL--PQVRlDDWRSRLSVVSQTPFLFSD- 424
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTYE-GEIIFEGEELqaSNIR-DTERAGIAIIHQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALGQ---PGAT---QAQIEQAAR-LASVHEDIlrlpqGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK13549 98 SVLENIFLGNeitPGGImdyDAMYLRAQKlLAQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 498 D---ALSAVDGRTEHQILHNLRSwgQDRTVIISAHRLSALTEASE-ILVMQHG 546
Cdd:PRK13549 169 EptaSLTESETAVLLDIIRDLKA--HGIACIYISHKLNEVKAISDtICVIRDG 219
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
352-554 |
4.60e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.02 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLI--QRQFDVDQGQIRYHGLPLpqvrLD---DWRSRLSV------------ 414
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDI----LElspDERARAGIflafqypveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 415 VSQTPFLfsDTVANNIALGQPGATQ--AQIEQAARLASVHEDILrlpqgydtevgERGVM--LSGGQKQRISIARALLLD 490
Cdd:COG0396 92 VSVSNFL--RTALNARRGEELSAREflKLLKEKMKELGLDEDFL-----------DRYVNegFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 491 AEILILD--------DALSAV-DGrtehqiLHNLRSwgQDRTVIISAH--RLSALTEASEILVMQHGGVAQRGDP 554
Cdd:COG0396 159 PKLAILDetdsgldiDALRIVaEG------VNKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
351-555 |
6.45e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlddwrsrlSVVS----QTPFLFSDTV 426
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------------RVSAllelGAGFHPELTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 427 ANNIALGqpGA----TQAQIEqaARLASVHE--DIlrlpQGY-DTEVGergvMLSGGQKQRISIARALLLDAEILILDDA 499
Cdd:COG1134 106 RENIYLN--GRllglSRKEID--EKFDEIVEfaEL----GDFiDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 500 LSAVDGR-TE--HQILHNLRSwgQDRTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPA 555
Cdd:COG1134 174 LAVGDAAfQKkcLARIRELRE--SGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPE 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
351-515 |
1.01e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTL---LSLIQRQFDVDqGQIRYHGLPLPQVRLDDW-RSRLSVVSQTPFLFSD-T 425
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWD-GEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQ----PGATQAQIEQAARLASVHEDiLRLPQGYDT-EVGERGvmlsGGQKQRISIARALLLDAEILILDDAL 500
Cdd:TIGR02633 95 VAENIFLGNeitlPGGRMAYNAMYLRAKNLLRE-LQLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEPS 169
|
170
....*....|....*
gi 1574033397 501 SAVDgRTEHQILHNL 515
Cdd:TIGR02633 170 SSLT-EKETEILLDI 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
349-547 |
1.08e-13 |
|
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: 69.10 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHglplpqvrlddWRSRLSVVSQTPFLfsdtvan 428
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-----------EGEDLLFLPQRPYL------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 nialgqPGATqaqieqaarLAsvheDILRLPqgYDTEvgergvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTE 508
Cdd:cd03223 76 ------PLGT---------LR----EQLIYP--WDDV-------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1574033397 509 HQILHNLRswgQDRTVIIS-AHRLSALTEASEILVMQHGG 547
Cdd:cd03223 128 DRLYQLLK---ELGITVISvGHRPSLWKFHDRVLDLDGEG 164
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
337-498 |
1.22e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 337 VDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQV---RLDDWRSRLS 413
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQTPFLFSD-TVANNIALgqPGATQAQIEQAARLASVhedILRLpqgydTEVGERGVM------LSGGQKQRISIARA 486
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAY--PLREHTQLPAPLLHSTV---MMKL-----EAVGLRGAAklmpseLSGGMARRAALARA 157
|
170
....*....|..
gi 1574033397 487 LLLDAEILILDD 498
Cdd:PRK11831 158 IALEPDLIMFDE 169
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
348-549 |
1.44e-13 |
|
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: 70.00 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 348 PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPqvrlDDWRSRLSVVSQTPFLFSDtva 427
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEERGLYPK--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 nnialgqpgatQAQIEQAARLASVH--------EDILRLPQGYD-TEVGERGV-MLSGGQKQRISIARALLLDAEILILD 497
Cdd:cd03269 85 -----------MKVIDQLVYLAQLKglkkeearRRIDEWLERLElSEYANKRVeELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 498 DALSAVD---GRTEHQILHNLRSWGqdRTVIISAHRLSALTEASEILVMQHGGVA 549
Cdd:cd03269 154 EPFSGLDpvnVELLKDVIRELARAG--KTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
351-561 |
1.83e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.97 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpqvRLDD--WRS-RLSVVSQTPflfSDTVA 427
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL---HFGDysYRSqRIRMIFQDP---STSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQ-------------PGATQAQIEQAARLASVHEDilrlpqgydtEVGERGVMLSGGQKQRISIARALLLDAEIL 494
Cdd:PRK15112 102 PRQRISQildfplrlntdlePEQREKQIIETLRQVGLLPD----------HASYYPHMLAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 495 ILDDALSAVDGRTEHQILhNLRSWGQDR---TVIISAHRLSALTEAS-EILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK15112 172 IADEALASLDMSMRSQLI-NLMLELQEKqgiSYIYVTQHLGMMKHISdQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
351-554 |
3.59e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.50 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYH--------------------GLPLPQVR----LD 406
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkekekvleklVIQKTRFKkikkIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 407 DWRSRLSVVSQtpF----LFSDTVANNIALGqPGATQAQIEQAARLASVHEDILRLPQGYdteVGERGVMLSGGQKQRIS 482
Cdd:PRK13651 102 EIRRRVGVVFQ--FaeyqLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDESY---LQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 483 IARALLLDAEILILDDALSAVD--GRTEH-QILHNLRSWGqdRTVIISAHRL-SALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDpqGVKEIlEIFDNLNKQG--KTIILVTHDLdNVLEWTKRTIFFKDGKIIKDGDT 249
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
329-580 |
3.68e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 329 PAGRGVLEVdirafhypenphpaLHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDW 408
Cdd:PRK10535 15 PSGEEQVEV--------------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 409 ----RSRLSVVSQTPFLFSD-TVANNIALGqpgATQAQIEQAARLASVHEDILRLpqGYDTEVGERGVMLSGGQKQRISI 483
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHlTAAQNVEVP---AVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 484 ARALLLDAEILILDDALSAVDGRTEHQ---ILHNLRSWGQdrTVIISAHRLSALTEASEILVMQHGGV-----------A 549
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEvmaILHQLRDRGH--TVIIVTHDPQVAAQAERVIEIRDGEIvrnppaqekvnV 233
|
250 260 270
....*....|....*....|....*....|.
gi 1574033397 550 QRGDPAALAAQPGWyrdmyryQQLEAALDEA 580
Cdd:PRK10535 234 AGGTEPVVNTASGW-------RQFVSGFREA 257
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
355-555 |
3.89e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.48 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 355 LALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDvDQGQIRYHGLPLPQVRLDD---WRSRLSvvSQTPFLFSDTVANNIA 431
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAElarHRAYLS--QQQSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 LGQPGATQAQiEQAARLASVHEDiLRLPQGYDTEVGErgvmLSGGQKQRISIARALL-------LDAEILILDDALSAVD 504
Cdd:COG4138 92 LHQPAGASSE-AVEQLLAQLAEA-LGLEDKLSRPLTQ----LSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 505 GRteHQILhnLRSW-----GQDRTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPA 555
Cdd:COG4138 166 VA--QQAA--LDRLlrelcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETA 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
351-557 |
5.30e-13 |
|
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: 68.55 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQvRLDDWRSRLSVVSQTPFLFSD-TVANN 429
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 IAL-----GQPGATQAQ-IEQAARLASVHEDILRLPQGYdtevgergvmlSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:cd03265 94 LYIharlyGVPGAERRErIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 504 DGRTEHQILHNLRSW--GQDRTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAAL 557
Cdd:cd03265 163 DPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
350-557 |
5.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.77 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIqrqfdvdqgqiryHGLPLP---QVRLDDW--------------RSRL 412
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL-------------NGLHVPtqgSVRVDDTlitstsknkdikqiRKKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 413 SVVSQTP--FLFSDTVANNIALGqPGATQAQIEQAARLAsvhEDILRLpQGYDTEVGERGVM-LSGGQKQRISIARALLL 489
Cdd:PRK13649 88 GLVFQFPesQLFEETVLKDVAFG-PQNFGVSQEEAEALA---REKLAL-VGISESLFEKNPFeLSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 490 DAEILILDDALSAVD--GRTE-HQILHNLRSWGQdrTVIISAHRLSALTE-ASEILVMQHGGVAQRGDPAAL 557
Cdd:PRK13649 163 EPKILVLDEPTAGLDpkGRKElMTLFKKLHQSGM--TIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-539 |
6.45e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.35 E-value: 6.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 367 LCGPTGAGKSTLLSLIQRQFDVDQGqIRYHGLPLPQVR-------LDDWRSRLSVVSQTPFLFSDTVANNIALGQPGATQ 439
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLLGGRsifnyrdVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 440 AQIEQAARLASVHEDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWG 519
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180
....*....|....*....|
gi 1574033397 520 QDRTVIISAHRLSALTEASE 539
Cdd:PRK14271 211 DRLTVIIVTHNLAQAARISD 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
349-546 |
8.01e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.37 E-value: 8.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDW---------RSRLSVVSQTp 419
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgylpeerglYPKMKVGEQL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 flfsdtvannIALGQ-PGATQAQIEQAAR--LasvheDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILIL 496
Cdd:COG4152 93 ----------VYLARlKGLSKAEAKRRADewL-----ERLGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 497 DDALS-----AVDgrTEHQILHNLRSWGqdRTVIISAHRLSaLTE--ASEILVMQHG 546
Cdd:COG4152 154 DEPFSgldpvNVE--LLKDVIRELAAKG--TTVIFSSHQME-LVEelCDRIVIINKG 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-557 |
9.54e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 9.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQ-TPFLFSDTVAN 428
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQdTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALGQ-PGATQAQIEQAARLASVHEDILRlpqGYDTEVGERGVM-LSGGQKQRISIARALLLDAEILILDDALSAVDgr 506
Cdd:PRK09536 97 VVEMGRtPHRSRFDTWTETDRAAVERAMER---TGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTASLD-- 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 507 TEHQI--LHNLRSWGQD-RTVIISAHRLS-ALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:PRK09536 172 INHQVrtLELVRRLVDDgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADV 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
351-531 |
1.23e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 70.33 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPlpqVRLDDWRSRL----SVVSQTPFLFSD-T 425
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE---MRFASTTAALaagvAIIYQELHLVPEmT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQ-PGA------TQAQIEQAARLASVHEDIlrlpqGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDD 498
Cdd:PRK11288 96 VAENLYLGQlPHKggivnrRLLNYEAREQLEHLGVDI-----DPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 1574033397 499 ALSAVDGR-TEH--QILHNLRSWGqdRTVIISAHRL 531
Cdd:PRK11288 167 PTSSLSAReIEQlfRVIRELRAEG--RVILYVSHRM 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
351-561 |
1.32e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.96 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSrlsVVSQTPFLFSDTVAN-N 429
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA---VRSDIQMIFQDPLASlN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 ialgqPGATQAQIeQAARLASVHedilrlPQGYDTEVGER--GVML----------------SGGQKQRISIARALLLDA 491
Cdd:PRK15079 113 -----PRMTIGEI-IAEPLRTYH------PKLSRQEVKDRvkAMMLkvgllpnlinryphefSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 492 EILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDrVLVMYLGHAVELGTYDEVYHNP 253
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
350-557 |
2.65e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.04 E-value: 2.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpQVRLDDWRSRLSVVSQTPFLFSD-TVAN 428
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NI----ALGQPGATQAQIEQAARLasvhEDilrlpQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:TIGR01257 1023 HIlfyaQLKGRSWEEAQLEMEAML----ED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 505 GRTEHQILHNLRSWGQDRTVIISAHRL-SALTEASEILVMQHGGVAQRGDPAAL 557
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
359-539 |
3.11e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.75 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 359 LKPGQMLGLCGPTGAGKSTLLSLIQ---RQFDVD-QGQIRYHGLPLPQVRlDDWRSRLSVVSQT----PFL-FSDTVANN 429
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntDGFHIGvEGVITYDGITPEEIK-KHYRGDVVYNAETdvhfPHLtVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 IALGQPGATQAQI---EQAARLASVHEDILRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:TIGR00956 163 ARCKTPQNRPDGVsreEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190
....*....|....*....|....*....|....*.
gi 1574033397 504 DGRTEHQILHNLRSwgqdRTVIISAHRLSALTEASE 539
Cdd:TIGR00956 241 DSATALEFIRALKT----SANILDTTPLVAIYQCSQ 272
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
348-546 |
3.90e-12 |
|
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: 66.02 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 348 PHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLddwrsrlsvvsQTPFLFSDTVA 427
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL-----------GGGFNPELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQP--GATQAQIEQaaRLASVhEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVDG 505
Cdd:cd03220 103 ENIYLNGRllGLSRKEIDE--KIDEI-IEFSELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1574033397 506 RTE---HQILHNLRSwgQDRTVIISAHRLSALTE-ASEILVMQHG 546
Cdd:cd03220 176 AFQekcQRRLRELLK--QGKTVILVSHDPSSIKRlCDRALVLEKG 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
350-552 |
4.03e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.54 E-value: 4.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlpLPQVRLDDWRSR---LSVVSQTPFLFSD-T 425
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG--NPCARLTPAKAHqlgIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQPG--ATQAQIEQAARLASVHEDiLRLPQGyDTEVGERgvmlsggqkQRISIARALLLDAEILILDD---AL 500
Cdd:PRK15439 103 VKENILFGLPKrqASMQKMKQLLAALGCQLD-LDSSAG-SLEVADR---------QIVEILRGLMRDSRILILDEptaSL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 501 SAVDGRTEHQILHNLRSWGQDrTVIISaHRLSALTE-ASEILVMQHGGVAQRG 552
Cdd:PRK15439 172 TPAETERLFSRIRELLAQGVG-IVFIS-HKLPEIRQlADRISVMRDGTIALSG 222
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
16-283 |
4.56e-12 |
|
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: 67.10 E-value: 4.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGVTEKQ-MSTGVLLAW-LGLMIGTAIVVYLLRYvWRVLLFGAsyQLAVEL 92
Cdd:cd18567 1 KRALLQILLLsLALELFALASPLYLQLVIDEVIVSGdRDLLTVLAIgFGLLLLLQALLSALRS-WLVLYLST--SLNLQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 93 RENFYRQLSRQNPAFYLRHRTGDLMAR----------ATNDVDRVVFAAGEGVLTLVdslvmglvvlvvMSTQISWQLTV 162
Cdd:cd18567 78 TSNLFRHLLRLPLSYFEKRHLGDIVSRfgsldeiqqtLTTGFVEALLDGLMAILTLV------------MMFLYSPKLAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 163 LALIPMpLMAIAIKYYgdqLHQRFKSAQAAFSSLNDQAQ----ESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVA 238
Cdd:cd18567 146 IVLAAV-ALYALLRLA---LYPPLRRATEEQIVASAKEQshflETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQ 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1574033397 239 RVDARFDpTIYIAI-GASNLLAIGGGSWMVVNGSLTLGQLTSFVMY 283
Cdd:cd18567 222 RLQILFS-AANGLLfGLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
334-561 |
5.17e-12 |
|
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: 68.56 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEV-DIR-AFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKS----TLLSLIQRQFDVDQGQIRYHGLPLPQVRLDD 407
Cdd:COG4172 6 LLSVeDLSvAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 408 WR----SRLSVVSQTPF-----LFS--DTVANNIALGQpGATQAQIEQAAR--LASV--HEDILRLPQgYDTEvgergvm 472
Cdd:COG4172 86 LRrirgNRIAMIFQEPMtslnpLHTigKQIAEVLRLHR-GLSGAAARARALelLERVgiPDPERRLDA-YPHQ------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 473 LSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTE-ASEILVMQHGGVA 549
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
250
....*....|..
gi 1574033397 550 QRGDPAALAAQP 561
Cdd:COG4172 237 EQGPTAELFAAP 248
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
352-554 |
6.49e-12 |
|
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: 64.86 E-value: 6.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLI--QRQFDVDQGQIRYHGLPLPQVRLDDwRSRLSV--VSQTPFLFsdtva 427
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE-RARLGIflAFQYPPEI----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 nnialgqPGATQAqieqaarlasvheDILRlpqgydtEVGERgvmLSGGQKQRISIARALLLDAEILILDDALSAVD--- 504
Cdd:cd03217 90 -------PGVKNA-------------DFLR-------YVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDida 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 505 GRTEHQILHNLRSwgQDRTVIISAH--RLSALTEASEILVMQHGGVAQRGDP 554
Cdd:cd03217 140 LRLVAEVINKLRE--EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
303-497 |
1.14e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.40 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 303 RGSAAYSRIRSL---LNEAPAVQDG------PQALPAGRGVLEVDIRAFHYPEnpHPALHDLALTLKPGQMLGLCGPTGA 373
Cdd:COG0488 275 KAKQAQSRIKALeklEREEPPRRDKtveirfPPPERLGKKVLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 374 GKSTLLSLIQRQFDVDQGQIRY-HGLplpqvrlddwrsRLSVVSQTPFLF--SDTVANNIALGQPGATQAQIeqAARLAS 450
Cdd:COG0488 353 GKSTLLKLLAGELEPDSGTVKLgETV------------KIGYFDQHQEELdpDKTVLDELRDGAPGGTEQEV--RGYLGR 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1574033397 451 V---HEDIlrlpqgyDTEVGErgvmLSGGQKQRISIARALLLDAEILILD 497
Cdd:COG0488 419 FlfsGDDA-------FKPVGV----LSGGEKARLALAKLLLSPPNVLLLD 457
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
350-504 |
1.33e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.67 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKST----LLSLIQrqfdVDQGQIRYHG-----LPLPQvrlddwRSRLSV--VSQT 418
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGedithLPMHK------RARLGIgyLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 PFLFSD-TVANNI--ALGQPGATQAQIEQaaRLASVHED--ILRLpqgYDTevgeRGVMLSGGQKQRISIARALLLDAEI 493
Cdd:COG1137 87 ASIFRKlTVEDNIlaVLELRKLSKKEREE--RLEELLEEfgITHL---RKS----KAYSLSGGERRRVEIARALATNPKF 157
|
170
....*....|.
gi 1574033397 494 LILDDALSAVD 504
Cdd:COG1137 158 ILLDEPFAGVD 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
352-557 |
1.68e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPlpqvrLDDWRSRL------SVVSQTPFLFSDT 425
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-----LESWSSKAfarkvaYLPQQLPAAEGMT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNI---------ALGQPGAT-QAQIEQAARLASVHEDILRLPQGydtevgergvmLSGGQKQRISIARALLLDAEILI 495
Cdd:PRK10575 102 VRELVaigrypwhgALGRFGAAdREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRCLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 496 LDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLSALTEASEILVMQHGG--VAQrGDPAAL 557
Cdd:PRK10575 171 LDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGemIAQ-GTPAEL 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-529 |
1.73e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.55 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVD-----QGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSD-T 425
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPNlS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALG----QPGATQAQIEQAARLAsvhediLRLPQGYDtEVGER----GVMLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK14247 99 IFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWD-EVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190
....*....|....*....|....*....|..
gi 1574033397 498 DALSAVDGRTEHQILHNLRSWGQDRTVIISAH 529
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
347-554 |
2.04e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.72 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVR-LDDWRSRLSVVSQTP--FLFS 423
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKAGMVFQNPdnQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 DTVANNIALG------QPGATQAQIEQAARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK13633 101 TIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 498 DALSAVD--GRTEhqILHNLRSWGQDR--TVIISAHRLSALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK13633 170 EPTAMLDpsGRRE--VVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
352-515 |
3.03e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 63.68 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQV----RLDDWRSRLSVVSQTPFLFSD-TV 426
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 427 ANNIALgqP----GATQAQIEQAAR--LASVhedilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:PRK11629 105 LENVAM--PlligKKKPAEINSRALemLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170
....*....|....*
gi 1574033397 501 SAVDGRTEHQILHNL 515
Cdd:PRK11629 174 GNLDARNADSIFQLL 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
341-553 |
5.38e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.26 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 341 AFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKS-TLLSLIqRQFDVDQGQIRYHGLPL-------------PQVRLD 406
Cdd:PRK10261 21 AFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLrrrsrqvielseqSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 407 DWR-SRLSVVSQTP-------FLFSDTVANNIALGQPGATQAQIEQAARLAsvheDILRLPQGyDTEVGERGVMLSGGQK 478
Cdd:PRK10261 100 HVRgADMAMIFQEPmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRML----DQVRIPEA-QTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 479 QRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQDRT--VIISAHRLSALTE-ASEILVMQHGGVAQRGD 553
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
16-295 |
6.41e-11 |
|
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: 63.67 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGV-TEKQMSTGVLLAwlGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18588 1 KKLLGEVLLAsLFLQLFALVTPLFFQVIIDKVlVHRSLSTLDVLA--IGLLVVALFEAVLSGLRTYLFSHTTNRIDAELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 94 ENFYRQLSRQNPAFYLRHRTGDLMARAtNDVDRV-VFAAGEGVLTLVDSLVMGLVVLVVMstQISWQLTVLALIPMPLMA 172
Cdd:cd18588 79 ARLFRHLLRLPLSYFESRQVGDTVARV-RELESIrQFLTGSALTLVLDLVFSVVFLAVMF--YYSPTLTLIVLASLPLYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 173 I----AIKYYGDQLHQRFKSAQAAFSSLNdqaqESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTI 248
Cdd:cd18588 156 LlsllVTPILRRRLEEKFQRGAENQSFLV----ETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIV 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1574033397 249 YIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALA 295
Cdd:cd18588 232 QLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLV 278
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
367-529 |
7.34e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 367 LCGPTGAGKSTLLSLIQRQFDVDQ-----GQIRYHGLPL--PQVRLDDWRSRLSVVSQTPFLFSD-TVANNIALG----- 433
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFPHlTIYDNVAIGvklng 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 434 ---QPGATQAQIEQAARLASVHEDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQ 510
Cdd:PRK14267 115 lvkSKKELDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170
....*....|....*....
gi 1574033397 511 ILHNLRSWGQDRTVIISAH 529
Cdd:PRK14267 188 IEELLFELKKEYTIVLVTH 206
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
351-498 |
9.25e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQvrlddW------RSRLSVVSQTPFLFSD 424
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-----WqtakimREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 425 -TVANNIALGQPGATQAQIEQaaRLASVHEDILRLpqgYDTEVGERGVMlSGGQKQRISIARALLLDAEILILDD 498
Cdd:PRK11614 95 mTVEENLAMGGFFAERDQFQE--RIKWVYELFPRL---HERRIQRAGTM-SGGEQQMLAIGRALMSQPRLLLLDE 163
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
352-540 |
9.84e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.43 E-value: 9.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplPQVRLDDWRSRLSVVSQ----TPFLfsdTVA 427
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHrnamKPAL---TVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQP--GATQAQIEQAARLASVHeDILRLPQGYdtevgergvmLSGGQKQRISIARALLLDAEILILDDALSAVDG 505
Cdd:PRK13539 92 ENLEFWAAflGGEELDIAAALEAVGLA-PLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1574033397 506 RTEHQ----ILHNLRSWGqdrTVIISAHRLSALTEASEI 540
Cdd:PRK13539 161 AAVALfaelIRAHLAQGG---IVIAATHIPLGLPGAREL 196
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
346-562 |
1.09e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 346 ENPHPALHDLALTLKPGQMLGLCGPTGAGKS----TLLSLIQRQFDVDQGQIRYHGLPLPQVRLddwRSRL-SVVSQTP- 419
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCAL---RGRKiATIMQNPr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 --FLFSDTVANN-----IALGQPgATQAQIEQAARLASVhEDILRLPQGYDTEvgergvmLSGGQKQRISIARALLLDAE 492
Cdd:PRK10418 90 saFNPLHTMHTHaretcLALGKP-ADDATLTAALEAVGL-ENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 493 ILILDDALSAVDGRTEHQILHNLRSWGQDRT--VIISAHRLSALTE-ASEILVMQHGGVAQRGDPAALAAQPG 562
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPK 233
|
|
| 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 |
1.54e-10 |
|
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: 62.22 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLliVIAILQLLPPKLVGIIVDGV-TEKQMSTGVLLawlglMIGTAIVVY---LLRYVWRVLLFGASYQLAVE 91
Cdd:cd18566 4 LPQVLLASL--FINILALATPLFILQVYDRViPNESIPTLQVL-----VIGVVIAILlesLLRLLRSYILAWIGARFDHR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 92 LRENFYRQLSRQNPAFYLRHRTGDLMARaTNDVDRVV-FAAGEGVLTLVDSLVMGLVVLVVMStqISWQLTVLALIPMPL 170
Cdd:cd18566 77 LSNAAFEHLLSLPLSFFEREPSGAHLER-LNSLEQIReFLTGQALLALLDLPFVLIFLGLIWY--LGGKLVLVPLVLLGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 171 MAIAIKYYGDQLHQRFKSAqaafSSLNDQAQ----ESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDP 246
Cdd:cd18566 154 FVLVAILLGPILRRALKER----SRADERRQnfliETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQT 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1574033397 247 TIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALA 295
Cdd:cd18566 230 LGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAF 278
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
351-561 |
1.67e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGL---PLPQVRLDDWRSRLSVVSQTPFLFSD--- 424
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASLDprq 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNI--ALGQPGATQAQiEQAARLASVHEDILRLPQG---YDTEvgergvmLSGGQKQRISIARALLLDAEILILDDA 499
Cdd:PRK10261 419 TVGDSImePLRVHGLLPGK-AAAARVAWLLERVGLLPEHawrYPHE-------FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 500 LSAVDGRTEHQILHNLRSWGQDRTV--IISAHRLSALTEAS-EILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFENP 555
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
47-281 |
1.80e-10 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 62.29 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 47 TEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVllfgASYQLAVELRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDR 126
Cdd:cd18558 53 KLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGL----AAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 127 VVFAAGEGVLTLVDSLVMGLVVLVVMSTQiSWQLTVLALIPMPLMAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTS 206
Cdd:cd18558 129 INEGIGDKIGVIFQNIATFGTGFIIGFIR-GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEA 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 207 IRMIKAFGLEDHQSNRFA---DVAAQTGAKNMHVARVDARFdptIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFV 281
Cdd:cd18558 208 FRTVIAFGGQQKEETRYAqnlEIAKRNGIKKAITFNISMGA---AFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVF 282
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
351-531 |
1.82e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPlpqVRLDDWRSR----LSVVSQTPFLFSD-T 425
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE---VTFNGPKSSqeagIGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIALGQP-----GATQAQ--IEQAARLASVhediLRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILD- 497
Cdd:PRK10762 96 IAENIFLGREfvnrfGRIDWKkmYAEADKLLAR----LNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDe 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1574033397 498 --DALSAVDGRTEHQILHNLRSwgQDRTVIISAHRL 531
Cdd:PRK10762 168 ptDALTDTETESLFRVIRELKS--QGRGIVYISHRL 201
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
352-497 |
1.99e-10 |
|
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: 59.00 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHglplpqvrlddwrsrlsvvsqtpflfsdtvannia 431
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----------------------------------- 60
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 432 lgqPGATQAQIEQaarlasvhedilrlpqgydtevgergvmLSGGQKQRISIARALLLDAEILILD 497
Cdd:cd03221 61 ---STVKIGYFEQ----------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
352-504 |
2.50e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.28 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHglplPQVRLDDWRSRLSVVSQTPFlfsdTVANNIA 431
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN----GKLRIGYVPQKLYLDTTLPL----TVNRFLR 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1574033397 432 LgQPGATQAQIEQA-ARLASVHedILRLPQGydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:PRK09544 92 L-RPGTKKEDILPAlKRVQAGH--LIDAPMQ----------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-546 |
2.79e-10 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 59.75 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSR-LSVVSQTPF---LFSD 424
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 -TVANNIALGQpgatqaqieqaarlasvhedilrlpqgydtevgergvMLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:cd03215 93 lSVAENIALSS-------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 504 D-GRTE--HQILHNLRSWGqdRTVI-ISahrlSALTE----ASEILVMQHG 546
Cdd:cd03215 136 DvGAKAeiYRLIRELADAG--KAVLlIS----SELDEllglCDRILVMYEG 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-529 |
3.55e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 3.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 355 LALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSVVSQTPFLFSD-TVANNIALG 433
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAPGIKTTlSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 434 QPGATQAQIEQAarLASV----HEDIlrlPQGYdtevgergvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH 509
Cdd:cd03231 98 HADHSDEQVEEA--LARVglngFEDR---PVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 1574033397 510 QILHNLRS-WGQDRTVIISAH 529
Cdd:cd03231 163 RFAEAMAGhCARGGMVVLTTH 183
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
353-529 |
3.91e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.82 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 353 HDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSVVSQTPFLFSD-TVANNI- 430
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGHQPGIKTElTALENLr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 431 ---ALGQPgATQAQIEQAarLASV----HEDilrLPQGYdtevgergvmLSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:PRK13538 97 fyqRLHGP-GDDEALWEA--LAQVglagFED---VPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190
....*....|....*....|....*....|
gi 1574033397 504 D----GRTEHQILHNLRSWGqdrTVIISAH 529
Cdd:PRK13538 161 DkqgvARLEALLAQHAEQGG---MVILTTH 187
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
352-512 |
5.61e-10 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 59.75 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQvrLD-DWRSRL-----SVVSQT-PFLFSD 424
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA--LDeDARARLrarhvGFVFQSfQLLPTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 TVANNIALgqP----GATQAQiEQAAR-LASVhedilrlpqGydteVGERG----VMLSGGQKQRISIARALLLDAEILI 495
Cdd:COG4181 106 TALENVML--PlelaGRRDAR-ARARAlLERV---------G----LGHRLdhypAQLSGGEQQRVALARAFATEPAILF 169
|
170
....*....|....*..
gi 1574033397 496 LDDALSAVDGRTEHQIL 512
Cdd:COG4181 170 ADEPTGNLDAATGEQII 186
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-552 |
6.72e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 6.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG----------LPLPQVRLdDWRSRLSVVSQTP- 419
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlrdlyaLSEAERRR-LLRTEWGFVHQHPr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 --FLFSDTVANNI-----ALGQpgATQAQIEQAAR--LASVHEDILR---LPQGYdtevgergvmlSGGQKQRISIARAL 487
Cdd:PRK11701 100 dgLRMQVSAGGNIgerlmAVGA--RHYGDIRATAGdwLERVEIDAARiddLPTTF-----------SGGMQQRLQIARNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 488 LLDAEILILDDALSAVDGRTEHQILHNLRSWGQDR--TVIISAHRLS-ALTEASEILVMQHGGVAQRG 552
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAvARLLAHRLLVMKQGRVVESG 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
331-546 |
8.33e-10 |
|
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: 61.38 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 331 GRGVLEVDIRAFHYPENPH-PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI---------------QRQFDVD--QGQ 392
Cdd:TIGR02633 254 GDVILEARNLTCWDVINPHrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfgaypgkfegnvfinGKPVDIRnpAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 393 IRyHGLPLpqVRLDdwRSRLSVVSQTpflfsdTVANNIALG--QPGATQAQIEQAARLASVHEDILRL---PQGYDTEVG 467
Cdd:TIGR02633 334 IR-AGIAM--VPED--RKRHGIVPIL------GVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLkvkTASPFLPIG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 468 ErgvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQD--RTVIISAHRLSALTEASEILVMQH 545
Cdd:TIGR02633 403 R----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgvAIIVVSSELAEVLGLSDRVLVIGE 478
|
.
gi 1574033397 546 G 546
Cdd:TIGR02633 479 G 479
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
352-555 |
2.27e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVD--------QGQIRYHGLPLPQV---RLDDWRSRLSVVSQTPF 420
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIdapRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 LFSdtVANNIALGQPGATQAQIEQAARLASVHEDILRLpQGYDTEVGERGVMLSGGQKQRISIARAL---------LLDA 491
Cdd:PRK13547 97 AFS--AREIVLLGRYPHARRAGALTHRDGEIAWQALAL-AGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 492 EILILDDALSAVDGRTEHQILHNLRS----WGQDRTVIISAHRLSAlTEASEILVMQHGGVAQRGDPA 555
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPA 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
350-540 |
2.32e-09 |
|
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: 57.37 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSVVSQTPFLFSD-TVAN 428
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPElSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 429 NIALGQP--GATQAQIEQAarLASV----HEDilrLPQGYdtevgergvmLSGGQKQRISIARALLLDAEILILDDALSA 502
Cdd:TIGR01189 93 NLHFWAAihGGAQRTIEDA--LAAVgltgFED---LPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1574033397 503 VDGRTEHQILHNLRS-WGQDRTVIISAHRLSALTEASEI 540
Cdd:TIGR01189 158 LDKAGVALLAGLLRAhLARGGIVLLTTHQDLGLVEAREL 196
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
16-299 |
2.83e-09 |
|
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: 58.68 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGV-TEKQMSTGVLLAWLglMIGTAIVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18555 1 KKLLISILLLsLLLQLLTLLIPILTQYVIDNViVPGNLNLLNVLGIG--ILILFLLYGLFSFLRGYIIIKLQTKLDKSLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 94 ENFYRQLSRQNPAFYLRHRTGDLMARATNDV-------DRVVFAAGEGVLTLVdslvmglvvLVVMSTQISWQLTVLALI 166
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRANSNVyirqilsNQVISLIIDLLLLVI---------YLIYMLYYSPLLTLIVLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 167 PMPLMAIAI---KYYGDQLHQRFKSAQAAFSS-LNdqaqESMTSIRMIKAFGLED----HQSNRFADVAAQTGAKNmhva 238
Cdd:cd18555 150 LGLLIVLLLlltRKKIKKLNQEEIVAQTKVQSyLT----ETLYGIETIKSLGSEKniykKWENLFKKQLKAFKKKE---- 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 239 RVDARFDpTIYIAI-GASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFN 299
Cdd:cd18555 222 RLSNILN-SISSSIqFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYN 282
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
361-533 |
2.91e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.89 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 361 PGQMLGLCGPTGAGKSTLLSLIQrqfdvdqGQIRYHGLPlPQVRLDDWRSRLSVVSQTPFLFSD-------TVANNIA-- 431
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALA-------GRIQGNNFT-GTILANNRKPTKQILKRTGFVTQDdilyphlTVRETLVfc 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 --LGQPGATQAQIEQAARLASVHEdiLRLPQGYDTEVGE---RGVmlSGGQKQRISIARALLLDAEILILDDALSAVDGR 506
Cdd:PLN03211 165 slLRLPKSLTKQEKILVAESVISE--LGLTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEPTSGLDAT 240
|
170 180
....*....|....*....|....*...
gi 1574033397 507 TEHQILHNLRSWGQD-RTVIISAHRLSA 533
Cdd:PLN03211 241 AAYRLVLTLGSLAQKgKTIVTSMHQPSS 268
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
351-546 |
3.09e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.58 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDD---WRSRLSVVSQTPFLFSD-TV 426
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 427 ANNIA--LGQPGATQAQIEQAARLASVHEDILRLPQGYDtevgergVMLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:PRK10908 97 YDNVAipLIIAGASGDDIRRRVSAALDKVGLLDKAKNFP-------IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1574033397 505 GRTEHQILHNLRSWGQ-DRTVIISAHRLSALTEAS-EILVMQHG 546
Cdd:PRK10908 170 DALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
351-554 |
6.04e-09 |
|
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: 58.66 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQ--RQFDVDQGQIRYH----------------GLPLP-------QVRL 405
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIYHvalcekcgyverpskvGEPCPvcggtlePEEV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 406 DDW----------RSRLSVVSQTPFLF--SDTVANNI--ALGQPG-ATQAQIEQAARLASVhedilrlpqgydTEVGERg 470
Cdd:TIGR03269 95 DFWnlsdklrrriRKRIAIMLQRTFALygDDTVLDNVleALEEIGyEGKEAVGRAVDLIEM------------VQLSHR- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 471 VM-----LSGGQKQRISIARALLLDAEILILDDALSAVDGRTEhQILHNLRSWG---QDRTVIISAHRLSALTEASEILV 542
Cdd:TIGR03269 162 IThiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHNALEEAvkaSGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|...
gi 1574033397 543 -MQHGGVAQRGDP 554
Cdd:TIGR03269 241 wLENGEIKEEGTP 253
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-561 |
7.21e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 7.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 341 AFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKS-TLLSLIQ----RQFDVDQGQIRYHG---LPLPQVRLDDWR-SR 411
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRllpsPPVVYPSGDIRFHGeslLHASEQTLRGVRgNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 412 LSVVSQTPFLFSDTVANnialgqpgatqaqIE-QAARLASVHEDILRLP------QGYDtEVGERGV---------MLSG 475
Cdd:PRK15134 94 IAMIFQEPMVSLNPLHT-------------LEkQLYEVLSLHRGMRREAargeilNCLD-RVGIRQAakrltdyphQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 476 GQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQ--DRTVIISAHRLSALTE-ASEILVMQHGGVAQRG 552
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQN 239
|
....*....
gi 1574033397 553 DPAALAAQP 561
Cdd:PRK15134 240 RAATLFSAP 248
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
329-549 |
9.25e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.11 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 329 PAGRGVLEV-DIRAfhypenpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL----PQV 403
Cdd:COG1129 251 APGEVVLEVeGLSV-------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirsPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 404 RLddwRSRLSVVS---QTPFLFSD-TVANNIALGQPGA--------TQAQIEQAARLAsvheDILRL-PQGYDTEVGErg 470
Cdd:COG1129 324 AI---RAGIAYVPedrKGEGLVLDlSIRENITLASLDRlsrgglldRRRERALAEEYI----KRLRIkTPSPEQPVGN-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 471 vmLSGGQKQRISIARALLLDAEILILDDALSAVD-G-RTE-HQILHNLRSwgQDRTVI-IS---------AHRlsaltea 537
Cdd:COG1129 395 --LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvGaKAEiYRLIRELAA--EGKAVIvISselpellglSDR------- 463
|
250
....*....|..
gi 1574033397 538 seILVMQHGGVA 549
Cdd:COG1129 464 --ILVMREGRIV 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
329-504 |
1.69e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 329 PAGRGVLEVD-IRAFHyPENPH-PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIqrqFDV----DQGQIRYHGLPL-- 400
Cdd:PRK13549 254 TIGEVILEVRnLTAWD-PVNPHiKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCL---FGAypgrWEGEIFIDGKPVki 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 401 --PQ---------VRLDdwRSRLSVVSQTPflfsdtVANNIALG--QPGATQAQIEQAARLASVHEDILRL------Pqg 461
Cdd:PRK13549 330 rnPQqaiaqgiamVPED--RKRDGIVPVMG------VGKNITLAalDRFTGGSRIDDAAELKTILESIQRLkvktasP-- 399
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1574033397 462 yDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:PRK13549 400 -ELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
351-546 |
1.82e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.10 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPqvRLDDWRS----------RLSVVSQTpf 420
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN--KLDHKLAaqlgigiiyqELSVIDEL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 lfsdTVANNIALGQP------GATQAQIEQAARLASVHEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEIL 494
Cdd:PRK09700 96 ----TVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 495 ILDDALSAV-DGRTEH--QILHNLRSWGqdRTVIISAHRLSALTEASE-ILVMQHG 546
Cdd:PRK09700 168 IMDEPTSSLtNKEVDYlfLIMNQLRKEG--TAIVYISHKLAEIRRICDrYTVMKDG 221
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
334-537 |
2.35e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDiraFHYPEnpHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLdDWRSRLS 413
Cdd:PRK13540 4 VIELD---FDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLC-TYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 414 VVSQ----TPFLfsdTVANNIALG-QPGATQAQIEQAARLASVhEDILRLPQGydtevgergvMLSGGQKQRISIARALL 488
Cdd:PRK13540 78 FVGHrsgiNPYL---TLRENCLYDiHFSPGAVGITELCRLFSL-EHLIDYPCG----------LLSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1574033397 489 LDAEILILDDALSAVDGRTEHQILHNLRSW-GQDRTVIISAHRLSALTEA 537
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEHrAKGGAVLLTSHQDLPLNKA 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
353-554 |
2.64e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 353 HDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFLFSD-TVANNIA 431
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 LG----QPGATQAQIEQAARLASVHE--DILRLP-QGYDTevgergvmLSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:PRK10253 104 RGryphQPLFTRWRKEDEEAVTKAMQatGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1574033397 505 grTEHQI--LHNLRSWGQDRTVIISA--HRLS-ALTEASEILVMQHGGVAQRGDP 554
Cdd:PRK10253 176 --ISHQIdlLELLSELNREKGYTLAAvlHDLNqACRYASHLIALREGKIVAQGAP 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
349-517 |
3.94e-08 |
|
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: 53.81 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVD---QGQIRYHGLPLPQVRlDDWRSRLSVVSQtpflfSDt 425
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKYPGEIIYVSE-----ED- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 vanniaLGQPGATQAQ-IEQAARLasvhedilrlpQGYDTevgERGVmlSGGQKQRISIARALLLDAEILILDDALSAVD 504
Cdd:cd03233 93 ------VHFPTLTVREtLDFALRC-----------KGNEF---VRGI--SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170
....*....|...
gi 1574033397 505 GRTEHQILHNLRS 517
Cdd:cd03233 151 SSTALEILKCIRT 163
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-537 |
4.23e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 361 PGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYhglplpqVRLDDWRSRLSVvsqtpflfsdtvannialgqpgatqa 440
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 441 qieqaarlasvhedilrlpQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSW-- 518
Cdd:smart00382 48 -------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRll 108
|
170 180
....*....|....*....|....
gi 1574033397 519 -----GQDRTVIISAHRLSALTEA 537
Cdd:smart00382 109 lllksEKNLTVILTTNDEKDLGPA 132
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
21-311 |
6.42e-08 |
|
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: 54.21 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQmSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFYRQL 100
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGG-PWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 101 SRQNPAFYLRHRTGDLMARATNDVDRV----------VFAAGEGVLTLVdslvmglvvlVVMSTqISWQLTVLALIPMPL 170
Cdd:cd18561 80 LKLGPGYLEGERTGELQTTVVDGVEALeayygrylpqLLVALLGPLLIL----------IYLFF-LDPLVALILLVFALL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 171 MAIAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTIYI 250
Cdd:cd18561 149 IPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 251 AIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRI 311
Cdd:cd18561 229 ATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
349-530 |
6.68e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.42 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQ--FDVDQGQIRyhglplpqVRLDDWRSRLSVVSQTPFLFSDTV 426
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAlkGTPVAGCVD--------VPDNQFGREASLIDAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 427 ANNIaLGQPGATQAQieqaARLASVHEdilrlpqgydtevgergvmLSGGQKQRISIARALLLDAEILILDDALSAVDGR 506
Cdd:COG2401 115 AVEL-LNAVGLSDAV----LWLRRFKE-------------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 1574033397 507 TEHQILHNLRSWGQDR--TVIISAHR 530
Cdd:COG2401 171 TAKRVARNLQKLARRAgiTLVVATHH 196
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
346-561 |
6.93e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 54.85 E-value: 6.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 346 ENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVrldDWRSR-LSVVSQTPFLFSD 424
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPADRdIAMVFQNYALYPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 425 -TVANNIALG--QPGATQAQIEQ----AARLASVHEDILRLPQgydtevgergvMLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK11650 91 mSVRENMAYGlkIRGMPKAEIEErvaeAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 498 DALSAVDG------RTEHQILHnlRSWGQdrTVIISAH-RLSALTEASEILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK11650 160 EPLSNLDAklrvqmRLEIQRLH--RRLKT--TSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-531 |
7.95e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.18 E-value: 7.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTL---LSLIQRQFDVDqGQIRYHGLPlpqVRLDDWRS--RLSVV------SQTP 419
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLmkvLSGVYPHGSYE-GEILFDGEV---CRFKDIRDseALGIViihqelALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 FLfsdTVANNIALGQPGAT-------QAQIEQAARLASV--HEDilrlPqgyDTEVGERGVmlsgGQKQRISIARALLLD 490
Cdd:NF040905 92 YL---SIAENIFLGNERAKrgvidwnETNRRARELLAKVglDES----P---DTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1574033397 491 AEILILDD---ALSAVDGRTEHQILHNLRswGQDRTVIISAHRL 531
Cdd:NF040905 158 VKLLILDEptaALNEEDSAALLDLLLELK--AQGITSIIISHKL 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
352-504 |
1.14e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 54.11 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLK---PGQ-MLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDW----RSRLSVVSQTPFLFS 423
Cdd:PRK11144 10 LGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 D-TVANNIALGQPGATQAQIEQAARLASVhEDIL-RLPqgydtevgergVMLSGGQKQRISIARALLLDAEILILDDALS 501
Cdd:PRK11144 90 HyKVRGNLRYGMAKSMVAQFDKIVALLGI-EPLLdRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
...
gi 1574033397 502 AVD 504
Cdd:PRK11144 158 SLD 160
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
354-559 |
1.29e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG-----LPLPQvrlddwRSRLSV--VSQTPFLFSD-T 425
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHA------RARRGIgyLPQEASIFRRlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNI-ALGQ--PGATQAQIEQAAR--LASVHEDILRlpqgydtevGERGVMLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:PRK10895 95 VYDNLmAVLQirDDLSAEQREDRANelMEEFHIEHLR---------DSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 501 SAVDGRTE---HQILHNLRSWGQDrtVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAA 559
Cdd:PRK10895 166 AGVDPISVidiKRIIEHLRDSGLG--VLITDHNVRETLAVCErAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
350-546 |
1.41e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 350 PALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPL----PQVRLDDW-------RSRLSVVsqt 418
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrsPQDGLANGivyisedRKRDGLV--- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 419 pflFSDTVANNI---ALGQPGATQAQIEQAARLASVhEDILRL-----PqGYDTEVGergvMLSGGQKQRISIARALLLD 490
Cdd:PRK10762 343 ---LGMSVKENMsltALRYFSRAGGSLKHADEQQAV-SDFIRLfniktP-SMEQAIG----LLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 491 AEILILDDALSAVDGRTEHQILHNLRSWGQDRTVII--SAHRLSALTEASEILVMQHG 546
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIlvSSEMPEVLGMSDRILVMHEG 471
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
352-547 |
1.57e-07 |
|
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: 51.86 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLS-LIQRQFD-VDQGQIRYHGLPLPQvrldDWRSRLSVVSQTPFLFsdtvann 429
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILINGRPLDK----NFQRSTGYVEQQDVHS------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 ialgqPGATqaqIEQAARLASVHedilrlpqgydtevgeRGvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH 509
Cdd:cd03232 92 -----PNLT---VREALRFSALL----------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1574033397 510 ---QILHNLRSWGQdrTVIISAHRLSALTEAS--EILVMQHGG 547
Cdd:cd03232 146 nivRFLKKLADSGQ--AILCTIHQPSASIFEKfdRLLLLKRGG 186
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
342-498 |
1.61e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 342 FHYPENPHpALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRLDDWRSRLSVVSQTPFL 421
Cdd:PRK10522 330 FAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 422 FSDTvanniaLGQPGatqaqieQAARLASVHEDILRLPQGYDTEVGERGVM---LSGGQKQRISIARALLLDAEILILDD 498
Cdd:PRK10522 409 FDQL------LGPEG-------KPANPALVEKWLERLKMAHKLELEDGRISnlkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
92-283 |
2.54e-07 |
|
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: 52.47 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 92 LRENFYRQLSRQNPAFYLRHRTGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGLVVLVVMSTQISWQLTVLALIPMPLM 171
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSEN-LSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 172 AIAIKYYGdQLHQRF-KSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVArvdARFDPTIYI 250
Cdd:cd18589 150 LLVPKFVG-KFQQSLaVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEA---AAYAVSMWT 225
|
170 180 190
....*....|....*....|....*....|....*..
gi 1574033397 251 AIGASNLLAIG----GGSwMVVNGSLTLGQLTSFVMY 283
Cdd:cd18589 226 SSFSGLALKVGilyyGGQ-LVTAGTVSSGDLVTFVLY 261
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
16-295 |
2.67e-07 |
|
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: 52.55 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGVTEKQMST--GVLLAWLGLMIGTAIVVYLLRYVwrvLLFGASYQLAVEL 92
Cdd:cd18779 1 PGLLGQILLAsLLLQLLGLALPLLTGVLVDRVIPRGDRDllGVLGLGLAALVLTQLLAGLLRSH---LLLRLRTRLDTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 93 RENFYRQLSRQNPAFYLRHRTGDLMAR-ATNDVDRVVFAAGegVLTLV-DSLVMGL--VVLVVMSTQISWQLTVLALIPM 168
Cdd:cd18779 78 TLGFLEHLLRLPYRFFQQRSTGDLLMRlSSNATIRELLTSQ--TLSALlDGTLVLGylALLFAQSPLLGLVVLGLAALQV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 169 PLMAIAIKYYGDqLHQRFKSAQAAFSSlndQAQESMTSIRMIKAFGLE----DHQSNRFADVAAQTGAKNmhvaRVDARF 244
Cdd:cd18779 156 ALLLATRRRVRE-LMARELAAQAEAQS---YLVEALSGIETLKASGAEdralDRWSNLFVDQLNASLRRG----RLDALV 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1574033397 245 DPTIYIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALA 295
Cdd:cd18779 228 DALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLV 278
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
338-558 |
3.46e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 338 DIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI--QRQFDVDQGQIRYHGLPLPQVRLDDwRSRLSV- 414
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEE-RAHLGIf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 415 -----------VSQTPFLFSDTVANNIALGQPgatqaQIEQAARLASVHEdILRLpQGYDTEVGERGVM--LSGGQKQRI 481
Cdd:CHL00131 88 lafqypieipgVSNADFLRLAYNSKRKFQGLP-----ELDPLEFLEIINE-KLKL-VGMDPSFLSRNVNegFSGGEKKRN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 482 SIARALLLDAEILILDDALSAVD---GRTEHQILHNLRSwgQDRTVIISAH--RLSALTEASEILVMQHGGVAQRGDpAA 556
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDidaLKIIAEGINKLMT--SENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AE 237
|
..
gi 1574033397 557 LA 558
Cdd:CHL00131 238 LA 239
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
355-546 |
3.63e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.47 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 355 LALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDvDQGQIRYHGLPL---PQVRLDDWRSRLSvvSQTPFLFSDTVANNIA 431
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLeawSAAELARHRAYLS--QQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 432 LGQPgaTQAQIEQAARLASVHEDILRLPQGYDTEVGErgvmLSGGQKQRISIARALL-------LDAEILILDDALSAVD 504
Cdd:PRK03695 92 LHQP--DKTRTEAVASALNEVAEALGLDDKLGRSVNQ----LSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1574033397 505 GRTE---HQILHNLRSWGqdRTVIISAHRLS-ALTEASEILVMQHG 546
Cdd:PRK03695 166 VAQQaalDRLLSELCQQG--IAVVMSSHDLNhTLRHADRVWLLKQG 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
354-550 |
4.60e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIqrqFDVDQ---GQIRYHGLPL-PQVRLDDWRSRLSVVSQ----TPFLFSDT 425
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCL---FGVDKragGEIRLNGKDIsPRSPLDAVKKGMAYITEsrrdNGFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VANNIAL----------GQPGATQAQIEQaaRLASVHEDILRLP-QGYDTEVGErgvmLSGGQKQRISIARALLLDAEIL 494
Cdd:PRK09700 358 IAQNMAIsrslkdggykGAMGLFHEVDEQ--RTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 495 ILDDALSAVDGRTEHQILHNLRSWGQDRTVII--SAHRLSALTEASEILVMQHGGVAQ 550
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDGKVILmvSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
347-505 |
9.00e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 9.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 347 NPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRqfDVDQG-------------------QIRYH-GLPLPQVRLd 406
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysndltlfgrrrgsgetiwDIKKHiGYVSSSLHL- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 407 DWRSRLSVVSQTPFLFSDTVannialgqpGATQAQIEQAARLASVHEDILrlpqGYDTEVGERGVM-LSGGQKQRISIAR 485
Cdd:PRK10938 348 DYRVSTSVRNVILSGFFDSI---------GIYQAVSDRQQKLAQQWLDIL----GIDKRTADAPFHsLSWGQQRLALIVR 414
|
170 180
....*....|....*....|
gi 1574033397 486 ALLLDAEILILDDALSAVDG 505
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDP 434
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
351-561 |
1.13e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 50.37 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRY-----HGLPLPQVrlddwrSRLSVVS--QTPFLFS 423
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrgqhiEGLPGHQI------ARMGVVRtfQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 D-TVANNIALGQ---------------PGATQAQIEQAARlASVHEDILRLPQGYDTEVGErgvmLSGGQKQRISIARAL 487
Cdd:PRK11300 94 EmTVIENLLVAQhqqlktglfsgllktPAFRRAESEALDR-AATWLERVGLLEHANRQAGN----LAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1574033397 488 LLDAEILILDDALSAVDGRTEH---QILHNLRSwGQDRTVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAAQP 561
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKeldELIAELRN-EHNVTVLLIEHDMKLVMGISDrIYVVNQGTPLANGTPEEIRNNP 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
351-504 |
1.19e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQ--RQfdVDQGQIRYHGLPlpqvrLDDWRSRLSVVSQTPF-------- 420
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgaRK--IQQGRVEVLGGD-----MADARHRRAVCPRIAYmpqglgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 LFSD-TVANNIAL-----GQPGAtqaqiEQAARlasvhedILRL------------PQGydtevgergvMLSGGQKQRIS 482
Cdd:NF033858 89 LYPTlSVFENLDFfgrlfGQDAA-----ERRRR-------IDELlratglapfadrPAG----------KLSGGMKQKLG 146
|
170 180
....*....|....*....|..
gi 1574033397 483 IARALLLDAEILILDDALSAVD 504
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-498 |
2.82e-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: 50.32 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 344 YPENPHpALHDLALTLKPGQMLGLCGPTGAGKSTLLSL---IQRQFDvdqGQIR--------YhglpLPQ---------V 403
Cdd:TIGR03719 14 VPPKKE-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagVDKDFN---GEARpqpgikvgY----LPQepqldptktV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 404 R---------LDDWRSRLSVVSQtpfLFSDTVANNIALGQPGAT-QAQIEQA-----ARLASVHEDILRLPQGyDTEVGE 468
Cdd:TIGR03719 86 RenveegvaeIKDALDRFNEISA---KYAEPDADFDKLAAEQAElQEIIDAAdawdlDSQLEIAMDALRCPPW-DADVTK 161
|
170 180 190
....*....|....*....|....*....|
gi 1574033397 469 rgvmLSGGQKQRISIARALLLDAEILILDD 498
Cdd:TIGR03719 162 ----LSGGERRRVALCRLLLSKPDMLLLDE 187
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
21-127 |
3.14e-06 |
|
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: 49.33 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 21 AVVLLIVIAILQLLPPKLVGIIVDGVTEKQMSTGVLLAWLGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELRENFYRQL 100
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100
....*....|....*....|....*..
gi 1574033397 101 SRQNPAFYLRHRTGDLMARATNDVDRV 127
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDAL 107
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
357-529 |
4.18e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.24 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 357 LTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLPQVRlDDWRSRLSvVSQTPFLFSD-------TVANN 429
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD-EEARAKLR-AKHVGFVFQSfmliptlNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 IALgqPGATQAQIEQAARLASVHediLRLPQGYDTEVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEH 509
Cdd:PRK10584 109 VEL--PALLRGESSRQSRNGAKA---LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|..
gi 1574033397 510 QILHNLRSWGQDR--TVIISAH 529
Cdd:PRK10584 184 KIADLLFSLNREHgtTLILVTH 205
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-513 |
5.34e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 5.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPLpqvrldDWRSR-------LSVVSQTPFLFS 423
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI------DFKSSkealengISMVHQELNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 D-TVANNIALGQPGATQAQIEQaarlASVHEDILRLPQGYDTEVG--ERGVMLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:PRK10982 87 QrSVMDNMWLGRYPTKGMFVDQ----DKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170
....*....|...
gi 1574033397 501 SAVdgrTEHQILH 513
Cdd:PRK10982 163 SSL---TEKEVNH 172
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
301-532 |
6.09e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 49.36 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 301 VERGSAAYSRIRSLLNEAPAVQDGPqaLPAGRGVLEVD---IRAFHYP---ENPHPALHDLALTLKPGQMLGLCGPTGAG 374
Cdd:TIGR00954 413 VKSGNFKRPRVEEIESGREGGRNSN--LVPGRGIVEYQdngIKFENIPlvtPNGDVLIESLSFEVPSGNNLLICGPNGCG 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 375 KSTLLSLIQRQFDVDQGqiryhglplpqVRLDDWRSRLSVVSQTPFLFSDTVANNIA-------LGQPGATQAQIEQAar 447
Cdd:TIGR00954 491 KSSLFRILGELWPVYGG-----------RLTKPAKGKLFYVPQRPYMTLGTLRDQIIypdssedMKRRGLSDKDLEQI-- 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 448 LASVH-EDILRLPQGYDTeVGERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQdrTVII 526
Cdd:TIGR00954 558 LDNVQlTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGI--TLFS 634
|
....*.
gi 1574033397 527 SAHRLS 532
Cdd:TIGR00954 635 VSHRKS 640
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
351-560 |
6.41e-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: 49.03 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIryhglplpQVRL-DDW----------RSR----LSVV 415
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV--------NVRVgDEWvdmtkpgpdgRGRakryIGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 416 SQTPFLFSD-TVANN----IALGQPgatqaqiEQAARLASVHedILRLpQGYDTEVGERGV-----MLSGGQKQRISIAR 485
Cdd:TIGR03269 371 HQEYDLYPHrTVLDNlteaIGLELP-------DELARMKAVI--TLKM-VGFDEEKAEEILdkypdELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 486 ALLLDAEILILDDALSAVDGRTE----HQILHNLRSWGQdrTVIISAHRLSALTEASE-ILVMQHGGVAQRGDPAALAAQ 560
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEMEQ--TFIIVSHDMDFVLDVCDrAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-504 |
6.83e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.54 E-value: 6.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 341 AFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGLPlpqVRLDDWRSRLSVVSQTPF 420
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT---ATRGDRSRFMAYLGHLPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 421 LFSD--TVANNIALGQPGATQAQIEQAARLAsvhedILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDD 498
Cdd:PRK13543 93 LKADlsTLENLHFLCGLHGRRAKQMPGSALA-----IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*.
gi 1574033397 499 ALSAVD 504
Cdd:PRK13543 164 PYANLD 169
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
337-504 |
8.09e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 8.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 337 VDIRAFHYPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI--QRQFDVDQGQIRYHGLPL----PQVRLDD--- 407
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLlelsPEDRAGEgif 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 408 ----WRSRLSVVSQTPFLFSDTVANNIALGQPGAT----QAQIEQAARLASVHEDILRlpqgYDTEVGergvmLSGGQKQ 479
Cdd:PRK09580 82 mafqYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDrfdfQDLMEEKIALLKMPEDLLT----RSVNVG-----FSGGEKK 152
|
170 180
....*....|....*....|....*
gi 1574033397 480 RISIARALLLDAEILILDDALSAVD 504
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLD 177
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-497 |
9.76e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 358 TLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIryhglplpqvrldDWRSRLSVVSQtpFLFSDtvannialgQPGA 437
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELKISYKPQ--YIKPD---------YDGT 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1574033397 438 TQAQIEQAA-RLAS--VHEDI---LRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK13409 417 VEDLLRSITdDLGSsyYKSEIikpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLD 478
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
16-299 |
2.17e-05 |
|
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: 46.74 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGVTEKQ-MSTGVLLAwlGLMIGTAIVVYLLRYVWRVLLFGASYQLAVELR 93
Cdd:cd18783 1 KRLFRDVAIAsLILHVLALAPPIFFQIVIDKVLVHQsYSTLYVLT--IGVVIALLFEGILGYLRRYLLLVATTRIDARLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 94 ENFYRQLSRQNPAFYLRHRTGDLMaRATNDVDRV-VFAAGEGVLTLVDSLVMGLVVLVVMStqISWQLTVLALIPMPLMA 172
Cdd:cd18783 79 LRTFDRLLSLPIDFFERTPAGVLT-KHMQQIERIrQFLTGQLFGTLLDATSLLVFLPVLFF--YSPTLALVVLAFSALIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 173 IAIKYYGDQLHQRFKSAQAAFSSLNDQAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDA---------- 242
Cdd:cd18783 156 LIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNwpqtltgple 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 243 RFDPTIYIAIGASnllaigggswMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFN 299
Cdd:cd18783 236 KLMTVGVIWVGAY----------LVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQ 282
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
358-504 |
2.91e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 358 TLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHG-------------LPLPQVR--LDDWRSRLSVVSQTPFLF 422
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpaLPQPALEyvIDGDREYRQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 423 SDTVANNIAL--GQPGATQAQIEQaARLASVHEDIlrlpqGYDTEVGERGVM-LSGGQKQRISIARALLLDAEILILDDA 499
Cdd:PRK10636 103 ERNDGHAIATihGKLDAIDAWTIR-SRAASLLHGL-----GFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEP 176
|
....*
gi 1574033397 500 LSAVD 504
Cdd:PRK10636 177 TNHLD 181
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
329-495 |
5.02e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.17 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 329 PAGRGVLEV-DIRAFhyPENPHPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLI--QRQfdVDQGQIRYHGLPL----P 401
Cdd:COG3845 252 EPGEVVLEVeNLSVR--DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLRP--PASGSIRLDGEDItglsP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 402 QVRlddWRSRLSVVSQTPF---LFSD-TVANNIALG---QPGATQAQIEQAARLASVHEDILR----LPQGYDTEVGerg 470
Cdd:COG3845 328 RER---RRLGVAYIPEDRLgrgLVPDmSVAENLILGryrRPPFSRGGFLDRKAIRAFAEELIEefdvRTPGPDTPAR--- 401
|
170 180
....*....|....*....|....*
gi 1574033397 471 vMLSGGQKQRISIARALLLDAEILI 495
Cdd:COG3845 402 -SLSGGNQQKVILARELSRDPKLLI 425
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-379 |
6.76e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 45.08 E-value: 6.76e-05
10 20
....*....|....*....|....*....
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLL 379
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTI 65
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
334-579 |
9.44e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 44.73 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 334 VLEVDIRAFHYPENPHP--ALHDLALTLKPGQMLGLCGPTGAGKS----TLLSLIQRQFDVDQGQIRYHGLPLpqVRLDD 407
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDL--QRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 408 WRSRLSVVSQTPFLFSD---------TVANNI--ALG--QPGATQAQIEQAARLAS---VHEDILRL---PQgydtevge 468
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDpmtslnpcyTVGFQImeAIKvhQGGNKKTRRQRAIDLLNqvgIPDPASRLdvyPH-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 469 rgvMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQ--DRTVIISAHRLSALTEASE-ILVMQH 545
Cdd:PRK11022 153 ---QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEAAHkIIVMYA 229
|
250 260 270
....*....|....*....|....*....|....
gi 1574033397 546 GGVAQRGDPAALAAQPgwyRDMYRyQQLEAALDE 579
Cdd:PRK11022 230 GQVVETGKAHDIFRAP---RHPYT-QALLRALPE 259
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
352-497 |
1.97e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 352 LHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQrqfDVDQ---GQIR--------YhglpLPQ-VRLDDWRSRLSVVSQTp 419
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA---GVDKefeGEARpapgikvgY----LPQePQLDPEKTVRENVEEG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 420 flFSDTVA-----NNI--ALGQPGAT-------QA----------------QIEQAArlasvheDILRLPQGyDTEVGEr 469
Cdd:PRK11819 95 --VAEVKAaldrfNEIyaAYAEPDADfdalaaeQGelqeiidaadawdldsQLEIAM-------DALRCPPW-DAKVTK- 163
|
170 180
....*....|....*....|....*...
gi 1574033397 470 gvmLSGGQKQRISIARALLLDAEILILD 497
Cdd:PRK11819 164 ---LSGGERRRVALCRLLLEKPDMLLLD 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
354-395 |
3.37e-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: 43.39 E-value: 3.37e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRY 395
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
349-547 |
4.20e-04 |
|
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: 41.54 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQfdvdQGQIRYH-GLPLPQvrlddwRSRLSVVSQTPFLfSDTVA 427
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA----SGKARLIsFLPKFS------RNKLIFIDQLQFL-IDVGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 428 NNIALGQPGATqaqieqaarlasvhedilrlpqgydtevgergvmLSGGQKQRISIARALLLDAE--ILILDDALSAVDG 505
Cdd:cd03238 77 GYLTLGQKLST----------------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1574033397 506 RTEHQILHNLRSWG-QDRTVIISAHRLSALTEASEILVMQHGG 547
Cdd:cd03238 123 QDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
349-498 |
4.39e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 349 HPALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlDDWRSRL-----SVVSQTPFlfs 423
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ--------DLIVARLqqdppRNVEGTVY--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 424 DTVANNIA------------------------LGQPGATQAQIEQAA--RLAS-VHEDILRLPQGYDTEVGErgvmLSGG 476
Cdd:PRK11147 85 DFVAEGIEeqaeylkryhdishlvetdpseknLNELAKLQEQLDHHNlwQLENrINEVLAQLGLDPDAALSS----LSGG 160
|
170 180
....*....|....*....|..
gi 1574033397 477 QKQRISIARALLLDAEILILDD 498
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDE 182
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
300-389 |
5.58e-04 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 42.16 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 300 IVERGSAAYSRIRSLLNEAPAvqdgPQALPAGRGVLEVDIRAFhypenphpalhDLALTLKPGQMLGLCGPTGAGKSTLL 379
Cdd:cd01136 20 LDGKGLPDEPERRPLIAAPPN----PLKRAPIEQPLPTGVRAI-----------DGLLTCGEGQRIGIFAGSGVGKSTLL 84
|
90
....*....|
gi 1574033397 380 SLIQRQFDVD 389
Cdd:cd01136 85 GMIARNTDAD 94
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
354-547 |
8.18e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 42.35 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKS----TLLSLiqRQfdVDQGQIRYHGLPL----PQVRLDDWRSRLSVVSQTPFLFSDT 425
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTelaeTLYGL--RP--ARGGRIMLNGKEInalsTAQRLARGLVYLPEDRQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 426 VA--NNIAL--GQPGATQAQIEQAARLASVHEDI-LRLPQGyDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDAL 500
Cdd:PRK15439 357 PLawNVCALthNRRGFWIKPARENAVLERYRRALnIKFNHA-EQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1574033397 501 SAVDGRTEHQILHNLRSWGQDRTVI--ISahrlSALTE----ASEILVMqHGG 547
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVlfIS----SDLEEieqmADRVLVM-HQG 479
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
351-553 |
1.60e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.57 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 351 ALHDLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIRYHGlplpqvrlddwrsRLSVVSQTPFLFSD-TVANN 429
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVIAISAGLSGQlTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 430 IALGQ--PGATQAQIE----QAARLASVHEDILRLPQGYdtevgergvmlSGGQKQRISIARALLLDAEILILDDALSAV 503
Cdd:PRK13546 106 IEFKMlcMGFKRKEIKamtpKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1574033397 504 DGRTEHQILHNLRSWG-QDRTVIISAHRLSALTE-ASEILVMQHGGVAQRGD 553
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGE 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
461-549 |
1.75e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 461 GYDTEVGErgvmLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQ-DRTVI-ISAHRLSALTEAS 538
Cdd:PRK10982 384 GHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKkDKGIIiISSEMPELLGITD 459
|
90
....*....|.
gi 1574033397 539 EILVMQHGGVA 549
Cdd:PRK10982 460 RILVMSNGLVA 470
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
354-394 |
2.03e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 2.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1574033397 354 DLALTLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIR 394
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK 382
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
358-497 |
2.86e-03 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 358 TLKPGQMLGLCGPTGAGKSTLLSLIQRQFDVDQGQIryhglplpqvrldDWRSRLSVVSQtpFLFSDtvannialgQPGA 437
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLKISYKPQ--YISPD---------YDGT 417
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1574033397 438 TQAQIEQAA--RLAS--VHEDI---LRLPQGYDTEVGErgvmLSGGQKQRISIARALLLDAEILILD 497
Cdd:COG1245 418 VEEFLRSANtdDFGSsyYKTEIikpLGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLD 480
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
471-546 |
3.27e-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: 38.71 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 471 VMLSGGQKQRISIARALLLDAEILILDDALSAVDGRtehQILHNLR-----SWGQDRTVIISAHRLSALTEASEILVMQH 545
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE---QRLNAARairrlSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
.
gi 1574033397 546 G 546
Cdd:cd03222 147 G 147
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
16-291 |
3.83e-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: 39.51 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 16 RRYLGAVVLL-IVIAILQLLPPKLVGIIVDGV-TEKQMSTgvlLAWLGLMIGTAIVVY-LLRYVWRVLLFGASYQLAVEL 92
Cdd:cd18586 1 RRVFVEVGLFsFFINLLALAPPIFMLQVYDRVlPSGSLST---LLGLTLGMVVLLAFDgLLRQVRSRILQRVGLRLDVEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 93 RENFYRQLSRQNpafyLRHRTGDLMARATNDVDRV-VFAAGEGVLTLVDslVMGLVVLVVMSTQISWQLTVLALIPMPLM 171
Cdd:cd18586 78 GRRVFRAVLELP----LESRPSGYWQQLLRDLDTLrNFLTGPSLFAFFD--LPWAPLFLAVIFLIHPPLGWVALVGAPVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 172 ---AIAIKYYGDQLHQRFKSAQAAFSSLndqAQESMTSIRMIKAFGLEDHQSNRFADVAAQTGAKNMHVARVDARFDPTI 248
Cdd:cd18586 152 vglAWLNHRATRKPLGEANEAQAARDAL---AAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIG 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1574033397 249 YIAIGASNLLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPM 291
Cdd:cd18586 229 KTLRMALQSLILGVGAYLVIDGELTIGALIAASILSGRALAPI 271
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
467-562 |
4.39e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 467 GERGVMLSGGQKQRISIARALLLDAEILILDDALSAVDGRTEHQILHNLRSWGQD-RTVIISAHRLSALTE-ASEILVMQ 544
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*...
gi 1574033397 545 HGGVAQRGDPAALAAQPG 562
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
358-534 |
7.04e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.41 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 358 TLKPGQMLGLCGPTGAGKSTLLSLIQrqfdvdqGQI-----RYHGLPlpqvrldDWRSRLSVVSQTPFL--FSDTVANNI 430
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILS-------GELipnlgDYEEEP-------SWDEVLKRFRGTELQnyFKKLYNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1574033397 431 ALgqpgATQAQ-IEQAARL--ASVhEDILRlpqgydtEVGERGVM-------------------LSGGQKQRISIARALL 488
Cdd:PRK13409 161 KV----VHKPQyVDLIPKVfkGKV-RELLK-------KVDERGKLdevverlglenildrdiseLSGGELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1574033397 489 LDAEILILDDALSAVDGRTEHQILHNLRSWGQDRTVIISAHRLSAL 534
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVL 274
|
|
| |
