|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
115-699 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 616.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 115 AATGRSEVWKLLGLVRPERGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYgdsLTRLCAVLTCVFLCGAAAN 194
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA---LLLLLLLLLGLALLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 195 GIRVYLMQSSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFF 274
Cdd:COG1132 79 YLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 275 VSPSLATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQ 354
Cdd:COG1132 159 IDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 355 KEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELL 434
Cdd:COG1132 239 RAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 435 ERQPRLPFNEGmVLDEKTFQGALEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSG 514
Cdd:COG1132 319 DEPPEIPDPPG-AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 515 TVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGE 594
Cdd:COG1132 396 RILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 595 KGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKI 674
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
570 580
....*....|....*....|....*
gi 9506367 675 CEHGTHEELLLKpNGLYRKLMNKQS 699
Cdd:COG1132 553 VEQGTHEELLAR-GGLYARLYRLQF 576
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-694 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 558.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 8 ALLLIPRRGpavrawAPAVSSRIWLASeWTPLVRAWTSLIhkPGSGLRFPAPLSGLPG-----GVGQWAtssgarrcWVL 82
Cdd:TIGR00958 50 GVLWLGALG------ILLNKAGGLLAA-VKPLVAALCLAT--PSLSSLRALAFWEALDpavrvALGLWS--------WFV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 83 AGPRAAHPLFARLQGAAATGVRDLGNDSQRRPAAtgrSEVWKLLGLVRPERGRLSAAVGFLAVSSVITMSAPFFLGRIID 162
Cdd:TIGR00958 113 WSYGAALPAAALWAVLSSAGASEKEAEQGQSETA---DLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVID 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 163 VIYTnpSEGYgDSLTRLCAVLTCV----FLCGAAANGIRVYLMQSsgqsIVNRLRTSLFSSILRQEVAFFDKTRTGELIN 238
Cdd:TIGR00958 190 TLGG--DKGP-PALASAIFFMCLLsiasSVSAGLRGGSFNYTMAR----INLRIREDLFRSLLRQDLGFFDENKTGELTS 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 239 RLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQL 318
Cdd:TIGR00958 263 RLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQV 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 319 AEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSS 398
Cdd:TIGR00958 343 AEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 399 FLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRLPfNEGMvLDEKTFQGALEFRNVHFTYPARPEVSVFQDF 478
Cdd:TIGR00958 423 FLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP-LTGT-LAPLNLEGLIEFQDVSFSYPNRPDVPVLKGL 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGad 558
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYG-- 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 559 nLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQ 638
Cdd:TIGR00958 579 -LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ 657
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 639 EalDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPnGLYRKL 694
Cdd:TIGR00958 658 E--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHL 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
124-698 |
2.05e-173 |
|
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: 508.47 E-value: 2.05e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 124 KLLGLVRPERGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYgdsLTRLCAVLTCVFLCGAAANGIRVYLMQS 203
Cdd:TIGR02204 8 ALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGL---LNRYFAFLLVVALVLALGTAARFYLVTW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 204 SGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFV 283
Cdd:TIGR02204 85 LGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 284 LSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGf 363
Cdd:TIGR02204 165 LLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRAL- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 364 fgaagLSGNLIVLS------VLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQ 437
Cdd:TIGR02204 244 -----LTAIVIVLVfgaivgVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 438 PRLPFNEGMVLDEKTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVS 517
Cdd:TIGR02204 319 PDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 518 LDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGI 597
Cdd:TIGR02204 399 LDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPD---ATDEEVEAAARAAHAHEFISALPEGYDTYLGERGV 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 598 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEH 677
Cdd:TIGR02204 476 TLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQ 555
|
570 580
....*....|....*....|.
gi 9506367 678 GTHEELLLKpNGLYRKLMNKQ 698
Cdd:TIGR02204 556 GTHAELIAK-GGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
119-698 |
3.73e-158 |
|
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: 473.94 E-value: 3.73e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 119 RSEVWKLLGLVRPERGRLSAAVGFLAVSSVITMSAPFFLGRIID-VIytnPSEGYgDSLTRLCAVLTCVFLCGAAANGIR 197
Cdd:COG2274 141 PFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDrVL---PNQDL-STLWVLAIGLLLALLFEGLLRLLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 198 VYLMQSSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSsDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSP 277
Cdd:COG2274 217 SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 278 SLATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEA 357
Cdd:COG2274 296 PLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 358 LARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQ 437
Cdd:COG2274 376 RLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLP 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 438 PRLPFNEGMVlDEKTFQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVS 517
Cdd:COG2274 456 PEREEGRSKL-SLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 518 LDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGI 597
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDP---DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 598 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEH 677
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570 580
....*....|....*....|.
gi 9506367 678 GTHEELLLKpNGLYRKLMNKQ 698
Cdd:COG2274 691 GTHEELLAR-KGLYAELVQQQ 710
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
139-430 |
3.66e-155 |
|
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: 450.81 E-value: 3.66e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTN--PSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSL 216
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKEsgDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 217 FSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVI 296
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 297 YGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVL 376
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 9506367 377 SVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
458-698 |
3.73e-145 |
|
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: 423.10 E-value: 3.73e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 537
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 538 VSQEPVLFSCSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNP 617
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKP---DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 618 KILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEElLLKPNGLYRKLMNK 697
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDE-LMAQKGVYAKLVKA 237
|
.
gi 9506367 698 Q 698
Cdd:cd03249 238 Q 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
124-698 |
1.10e-139 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 421.82 E-value: 1.10e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 124 KLLGLVRPERGRL-SAAVGFLAVSSvitmSAPFFLGRIIDVIYTNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQ 202
Cdd:TIGR02203 4 RLWSYVRPYKAGLvLAGVAMILVAA----TESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 203 SSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATF 282
Cdd:TIGR02203 80 WVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 283 VLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAG 362
Cdd:TIGR02203 160 VVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 363 FFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRLpf 442
Cdd:TIGR02203 240 SSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK-- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 443 NEGMVLDEKTfQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHD 522
Cdd:TIGR02203 318 DTGTRAIERA-RGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 523 IRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGAdnLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGG 602
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR--TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGG 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 603 QKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEE 682
Cdd:TIGR02203 474 QRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNE 553
|
570
....*....|....*.
gi 9506367 683 LLLKpNGLYRKLMNKQ 698
Cdd:TIGR02203 554 LLAR-NGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
457-694 |
5.68e-117 |
|
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: 350.76 E-value: 5.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKN 616
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPG---ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKL 694
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
204-698 |
1.35e-114 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 357.41 E-value: 1.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 204 SGQsIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLaTFV 283
Cdd:PRK11176 93 SGK-VVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQL-SLI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 284 LSVVPPI-SVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAG 362
Cdd:PRK11176 171 LIVIAPIvSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSI 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 363 FFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGEL----SSflMYAFWVGLSigGLSSFYSELMKGLGAGGRLWELLERQP 438
Cdd:PRK11176 251 SDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItvvfSS--MIALMRPLK--SLTNVNAQFQRGMAACQTLFAILDLEQ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 439 RLpfNEGmVLDEKTFQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL 518
Cdd:PRK11176 327 EK--DEG-KRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 519 DGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSvtAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGIL 598
Cdd:PRK11176 403 DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYS--REQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHG 678
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
490 500
....*....|....*....|
gi 9506367 679 THEELLLKpNGLYRKLMNKQ 698
Cdd:PRK11176 561 THAELLAQ-NGVYAQLHKMQ 579
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
139-430 |
1.91e-110 |
|
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: 336.07 E-value: 1.91e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTnpsEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFS 218
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIK---GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 219 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYG 298
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 299 RYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSV 378
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 379 LYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
125-684 |
2.36e-108 |
|
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: 340.20 E-value: 2.36e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 125 LLGLVRPERGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSS 204
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPL--SALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 205 GQSIVNRLRTSLFSSILRQEVAFFDKTRTGELInrlssdtALLGRSVtENLsDGLRAG---AQASVGV------GMMFFV 275
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELA-------TLLTEGV-EAL-DGYFARylpQLFLAALvpllilVAVFPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 276 SPSLATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFG------KEMTEV-EKYTGRVDQ 348
Cdd:COG4988 157 DWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGrakaeaERIAEAsEDFRKRTMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 349 LLQLAQKEALArAGFFGAAGlsgnlIVLSVLYkGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGG 428
Cdd:COG4988 237 VLRVAFLSSAV-LEFFASLS-----IALVAVY-IGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 429 RLWELLERQPRLPfNEGMVLDEKTFQGALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRL 508
Cdd:COG4988 310 KIFALLDAPEPAA-PAGTAPLPAAGPPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 509 YDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGF 588
Cdd:COG4988 387 LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD---ASDEELEAALEAAGLDEFVAALPDGL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 589 DTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAV 668
Cdd:COG4988 464 DTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILV 543
|
570
....*....|....*.
gi 9506367 669 LDHGKICEHGTHEELL 684
Cdd:COG4988 544 LDDGRIVEQGTHEELL 559
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
457-698 |
3.90e-107 |
|
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: 325.34 E-value: 3.90e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKN 616
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD---ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMN 696
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWK 234
|
..
gi 9506367 697 KQ 698
Cdd:cd03253 235 AQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
325-699 |
6.87e-105 |
|
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: 332.55 E-value: 6.87e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 325 NIRTIRAFGKEMTEVEKYtgrvDQllQLAQKEALARAGFFGAAGLSG--NLI----VLSVLYKGGLLMGSAHMTVGELss 398
Cdd:COG5265 227 NYETVKYFGNEAREARRY----DE--ALARYERAAVKSQTSLALLNFgqALIialgLTAMMLMAAQGVVAGTMTVGDF-- 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 399 FLMYAFWVGLSI--GGLSSFYSELMKGLGAGGRLWELLERQPRlpfnegmVLDE------KTFQGALEFRNVHFTY-PAR 469
Cdd:COG5265 299 VLVNAYLIQLYIplNFLGFVYREIRQALADMERMFDLLDQPPE-------VADApdapplVVGGGEVRFENVSFGYdPER 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 470 PevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSV 549
Cdd:COG5265 372 P---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTI 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 550 AENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSAL 629
Cdd:COG5265 449 AYNIAYGRPD---ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 630 DAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQS 699
Cdd:COG5265 526 DSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQ 594
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
455-686 |
6.14e-103 |
|
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: 314.16 E-value: 6.14e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 455 GALEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSK 534
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALL 614
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN---ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 615 KNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLK 686
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
142-429 |
9.20e-100 |
|
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: 308.41 E-value: 9.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 142 FLAVSSVITMSAPFFLGRIIDVIYTNPSEGYGDS---LTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFS 218
Cdd:cd18780 4 ALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEAlraLNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 219 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYG 298
Cdd:cd18780 84 AIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 299 RYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSV 378
Cdd:cd18780 164 KYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLV 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9506367 379 LYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGR 429
Cdd:cd18780 244 LWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVR 294
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
148-699 |
1.66e-99 |
|
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: 321.31 E-value: 1.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 148 VITMSAPFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQEVAF 227
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVLVHRGL---STLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGY 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 228 FDKTRTGELINRLSSdtallgrsvTENLSDGLRAGAQAS--------VGVGMMFFVSPSLATFVLSVVPPISVLAVIYGR 299
Cdd:TIGR01846 230 FESRRVGDTVARVRE---------LEQIRNFLTGSALTVvldllfvvVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 300 YLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEmtevEKYTGRVDQLL--QLAQKEALARAGFFG--AAGLSGNLIV 375
Cdd:TIGR01846 301 ILRKRVEDKFERSAAATSFLVESVTGIETIKATATE----PQFQNRWDRQLaaYVAASFRVTNLGNIAgqAIELIQKLTF 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 376 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLErQPRLPFNEGMVLDEKtFQG 455
Cdd:TIGR01846 377 AILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALPE-LRG 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTY-PARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSK 534
Cdd:TIGR01846 455 AITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFSCSVAENIAYGADNLSSvtaQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALL 614
Cdd:TIGR01846 533 MGVVLQENVLFSRSIRDNIALCNPGAPF---EHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALV 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 615 KNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKL 694
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARL 688
|
....*
gi 9506367 695 MNKQS 699
Cdd:TIGR01846 689 WQQQS 693
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
208-696 |
2.67e-98 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 314.40 E-value: 2.67e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 208 IVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLA-TFVLSV 286
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALAlVLALGL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 287 VPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGA 366
Cdd:COG4987 166 LLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 367 AGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRLPFNEGM 446
Cdd:COG4987 246 LQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEP 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 447 VLDEKtfQGALEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQL 526
Cdd:COG4987 326 APAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 527 NPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQR 606
Cdd:COG4987 403 DEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD---ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEElLLK 686
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEE-LLA 558
|
490
....*....|
gi 9506367 687 PNGLYRKLMN 696
Cdd:COG4987 559 QNGRYRQLYQ 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
448-674 |
1.97e-89 |
|
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: 278.97 E-value: 1.97e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 448 LDEKTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN 527
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 528 PVWLRSKIGTVSQEPVLFSCSVAENIAYGadnLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRI 607
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKI 674
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
123-701 |
2.68e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 288.40 E-value: 2.68e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 123 WKLLGLVRPERGRlsaaVGFLAVSSV----ITMSAPFFLGRIIDVIYTNpsegygDSLTRLCAVLTCVFLCGAAAnGIRV 198
Cdd:PRK13657 8 ARVLQYLGAEKRL----GILLAVANVllaaATFAEPILFGRIIDAISGK------GDIFPLLAAWAGFGLFNIIA-GVLV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 199 YLmqsSGQSIVNRLR----TSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFF 274
Cdd:PRK13657 77 AR---HADRLAHRRRlavlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 275 VSPSLATFVLsvvppisVLAVIY---GRYLRKLSKATQDSLAEA-TQLAE---ERIGNIRTIRAFGKEMTEVEKYTGRVD 347
Cdd:PRK13657 154 MNWRLSLVLV-------VLGIVYtliTTLVMRKTKDGQAAVEEHyHDLFAhvsDAIGNVSVVQSYNRIEAETQALRDIAD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 348 QLLQlAQKEAL---ARAGffGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGLSIGGL---SSFYSELM 421
Cdd:PRK13657 227 NLLA-AQMPVLswwALAS--VLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFA---TLLIGRLdqvVAFINQVF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 422 KglgAGGRLWELLE-----RQPRLPFNegmVLDEKTFQGALEFRNVHFTYP-ARPEVSvfqDFSLSIPSGSVTALVGPSG 495
Cdd:PRK13657 301 M---AAPKLEEFFEvedavPDVRDPPG---AIDLGRVKGAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 496 SGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVA 575
Cdd:PRK13657 372 AGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD---ATDEEMRAAAERA 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 576 NAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAH 655
Cdd:PRK13657 449 QAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAH 528
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 9506367 656 RLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQSFL 701
Cdd:PRK13657 529 RLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRFAALLRAQGML 573
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
457-673 |
3.09e-87 |
|
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: 271.18 E-value: 3.09e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSCSVAENIaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLKN 616
Cdd:cd03228 80 YVPQDPFLFSGTIRENI---------------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGK 673
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
457-698 |
8.77e-86 |
|
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: 270.13 E-value: 8.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTY-PARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 535
Cdd:cd03252 1 ITFEHVRFRYkPDGPVI--LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFSCSVAENIAYGADNLSsvtAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLK 615
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMS---MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLM 695
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLY 234
|
...
gi 9506367 696 NKQ 698
Cdd:cd03252 235 QLQ 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
197-698 |
1.62e-80 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 267.35 E-value: 1.62e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 197 RVYLMQSSGQSIVnRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALL----GRSVTeNLSDGLRAGAqaSVGVGMM 272
Cdd:PRK10789 57 RVLLFGASYQLAV-ELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaaGEGVL-TLVDSLVMGC--AVLIVMS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 273 FFVSPSLATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKE------MTEVEKYTGRv 346
Cdd:PRK10789 133 TQISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEdrqsalFAADAEDTGK- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 347 dQLLQLAQKEALARAGFFGAAGLSgNLIVLSvlykGGLLM---GSahMTVGELSSFLMYafwVGLSIG---GLSSFYSEL 420
Cdd:PRK10789 212 -KNMRVARIDARFDPTIYIAIGMA-NLLAIG----GGSWMvvnGS--LTLGQLTSFVMY---LGLMIWpmlALAWMFNIV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 421 MKGLGAGGRLWELLERQPRLPFNEGMVLDEKtfqGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKST 500
Cdd:PRK10789 281 ERGSAAYSRIRAMLAEAPVVKDGSEPVPEGR---GELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKST 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 501 VVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEF 580
Cdd:PRK10789 357 LLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD---ATQQEIEHVARLASVHDD 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 581 IRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTI 660
Cdd:PRK10789 434 ILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSAL 513
|
490 500 510
....*....|....*....|....*....|....*...
gi 9506367 661 KNANFVAVLDHGKICEHGTHEELLLKPnGLYRKLMNKQ 698
Cdd:PRK10789 514 TEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
139-427 |
6.04e-80 |
|
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: 256.70 E-value: 6.04e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFS 218
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSR---EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 219 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYG 298
Cdd:cd18572 78 SLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 299 RYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSV 378
Cdd:cd18572 158 RYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 9506367 379 LYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAG 427
Cdd:cd18572 238 LFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAA 286
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
139-430 |
5.11e-77 |
|
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: 248.94 E-value: 5.11e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYtnpSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFS 218
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAAL---GGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 219 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYG 298
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 299 RYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSV 378
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 379 LYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
216-694 |
6.86e-77 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 261.03 E-value: 6.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSsdtalLGRSVTENLSDGLRAGAQASVGV----GMMFFVSPSLATFVLSVVPpIS 291
Cdd:TIGR03796 233 FLWHILRLPVRFFAQRHAGDIASRVQ-----LNDQVAEFLSGQLATTALDAVMLvfyaLLMLLYDPVLTLIGIAFAA-IN 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 292 VLAVIYGRYLRKLS--KATQDSlAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAgFFGA--A 367
Cdd:TIGR03796 307 VLALQLVSRRRVDAnrRLQQDA-GKLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQ-ILGVlpT 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 368 GLSGnLIVLSVLYKGGLLMGSAHMTVGELSSFLmyafwvglSIggLSSFYSELMKGLGAGGRLWEL---------LERQP 438
Cdd:TIGR03796 385 LLTS-LNSALILVVGGLRVMEGQLTIGMLVAFQ--------SL--MSSFLEPVNNLVGFGGTLQELegdlnrlddVLRNP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 439 RLPFNE------GMVLDEKTFQGALEFRNVHFTYpARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN 512
Cdd:TIGR03796 454 VDPLLEepegsaATSEPPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPW 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 513 SGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAygadnL--SSVTAQQVERAAEVANAAEFIRSFPQGFDT 590
Cdd:TIGR03796 533 SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLT-----LwdPTIPDADLVRACKDAAIHDVITSRPGGYDA 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 591 VVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRlmEGRTVLIIAHRLSTIKNANFVAVLD 670
Cdd:TIGR03796 608 ELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLE 685
|
490 500
....*....|....*....|....
gi 9506367 671 HGKICEHGTHEELLLKPnGLYRKL 694
Cdd:TIGR03796 686 RGKVVQRGTHEELWAVG-GAYARL 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
124-684 |
1.78e-76 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 257.34 E-value: 1.78e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 124 KLLGLVRPERGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNpsegyGDSLTRLCAVLTCVF----LCGAAANGIRVY 199
Cdd:PRK10790 13 RLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAK-----GNLPLGLVAGLAAAYvglqLLAAGLHYAQSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 200 LMQSSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSL 279
Cdd:PRK10790 88 LFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRM 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 280 ATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKyTGRVDQLLQLAQKEALA 359
Cdd:PRK10790 168 ALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGER-MGEASRSHYMARMQTLR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 360 RAGFFgaagLSGNLIVLSVLYKGGLLM-----GSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELL 434
Cdd:PRK10790 247 LDGFL----LRPLLSLFSALILCGLLMlfgfsASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 435 ERqPRLPFNEgmvlDEKTFQ-GALEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNS 513
Cdd:PRK10790 323 DG-PRQQYGN----DDRPLQsGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 514 GTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVG 593
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD----ISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 594 EKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGK 673
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
570
....*....|.
gi 9506367 674 ICEHGTHEELL 684
Cdd:PRK10790 552 AVEQGTHQQLL 562
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
144-696 |
2.72e-74 |
|
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: 254.28 E-value: 2.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 144 AVSSVITMSAPFFLGRIIDVIYTNPSEGygdSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQ 223
Cdd:TIGR01193 166 IIVTLISIAGSYYLQKIIDTYIPHKMMG---TLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFEL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 224 EVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGvgmMFFVSPSLATFVLSVVPpISVLAVIYGRYLRK 303
Cdd:TIGR01193 243 PMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVG---LFLVRQNMLLFLLSLLS-IPVYAVIIILFKRT 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 304 LSKATQDSLAEATQLAE---ERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFfGAAGLSGNLIV-LSVL 379
Cdd:TIGR01193 319 FNKLNHDAMQANAVLNSsiiEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQ-QAIKAVTKLILnVVIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 380 YKGGLLMGSAHMTVGELSSF-LMYAFWVGlSIGGLSSFYSELMKGLGAGGRLWE--LLERQprlpFNEGMVLDEKT-FQG 455
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFnALLSYFLT-PLENIINLQPKLQAARVANNRLNEvyLVDSE----FINKKKRTELNnLNG 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 535
Cdd:TIGR01193 473 DIVINDVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFSCSVAENIAYGADnlSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLK 615
Cdd:TIGR01193 551 NYLPQEPYIFSGSILENLLLGAK--ENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLMEgRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYRKLM 695
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR-NGFYASLI 706
|
.
gi 9506367 696 N 696
Cdd:TIGR01193 707 H 707
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
455-674 |
8.98e-73 |
|
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: 235.18 E-value: 8.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 455 GALEFRNVHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSK 534
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFSCSVAENIAYGAdnlSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALL 614
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA---PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 615 KNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKI 674
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
269-684 |
1.96e-68 |
|
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: 234.64 E-value: 1.96e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 269 VGMMFFVSPSLATFVL--SVVppISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGkeMTE--VEKYTG 344
Cdd:COG4618 147 LAVLFLFHPLLGLLALvgALV--LVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMG--MLPalRRRWQR 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 345 RVDQLLQLaQKEALARAGFFGAAGLSGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMyafwvG-------LSIGGLS 414
Cdd:COG4618 223 ANARALAL-QARASDRAGGFSALSKFLRLLLQSaVLGLGAYLVIQGEITPGAMiaASILM-----GralapieQAIGGWK 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 415 SFyselMKGLGAGGRLWELLERQPRLPfnEGMVLdeKTFQGALEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPS 494
Cdd:COG4618 297 QF----VSARQAYRRLNELLAAVPAEP--ERMPL--PRPKGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPS 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 495 GSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAygadNLSSVTAQQVERAAEV 574
Cdd:COG4618 368 GSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA----RFGDADPEKVVAAAKL 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 575 ANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLII 653
Cdd:COG4618 444 AGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVI 523
|
410 420 430
....*....|....*....|....*....|.
gi 9506367 654 AHRLSTIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:COG4618 524 THRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
135-669 |
6.57e-68 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 232.56 E-value: 6.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 135 RLSAAVGFLAVSSVITMSapFFLGRIIDVIYtnpSEGYG-DSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLR 213
Cdd:TIGR02857 6 ALLALLGVLGALLIIAQA--WLLARVVDGLI---SAGEPlAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 214 TSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVL 293
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 294 AVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEV-------EKYTGRVDQLLQLAQKEALARAgFFGA 366
Cdd:TIGR02857 161 MILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAaairrssEEYRERTMRVLRIAFLSSAVLE-LFAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 367 AGLSGNLIVLSVLYKGGLLMGSAHMTVgelssfLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRlPFNEGM 446
Cdd:TIGR02857 240 LSVALVAVYIGFRLLAGDLDLATGLFV------LLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPR-PLAGKA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 447 VLDEKTFQgALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQL 526
Cdd:TIGR02857 313 PVTAAPAS-SLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 527 NPVWLRSKIGTVSQEPVLFSCSVAENIAYGAdnlSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQR 606
Cdd:TIGR02857 390 DADSWRDQIAWVPQHPFLFAGTIAENIRLAR---PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQR 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVL 669
Cdd:TIGR02857 467 LALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
132-713 |
1.07e-67 |
|
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: 233.24 E-value: 1.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 132 ERGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSegygdsltrlCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNR 211
Cdd:TIGR01192 17 HKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSD----------VLPTLALWAGFGVFNTIAYVLVAREADRLAHG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 212 LRTSL----FSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLragaqaSVGVGMMFFVSPSLATFV-LSV 286
Cdd:TIGR01192 87 RRATLlteaFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHL------ATFVALFLLIPTAFAMDWrLSI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 287 VppISVLAVIY---GRYLRKLSKATQDSLAEATQL----AEERIGNIRTIRAFGK---EMTEVEKYTGRvdqlLQLAQKE 356
Cdd:TIGR01192 161 V--LMVLGILYiliAKLVMQRTKNGQAAVEHHYHNvfkhVSDSISNVSVVHSYNRieaETSALKQFTNN----LLSAQYP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 357 ALARAGFfgAAGL---SGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGLSIGGLSSFYSELMKGLGAGGRLWEL 433
Cdd:TIGR01192 235 VLDWWAL--ASGLnrmASTISMMCILVIGTVLVIKGELSVGEVIAFIGFA---NLLIGRLDQMSGFITQIFEARAKLEDF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 434 LE-----RQPRLPFNEGMVldeKTFQGALEFRNVHFTYPARPEvSVFqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRL 508
Cdd:TIGR01192 310 FDledsvFQREEPADAPEL---PNVKGAVEFRHITFEFANSSQ-GVF-DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 509 YDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGF 588
Cdd:TIGR01192 385 YDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGRE---GATDEEVYEAAKAAAAHDFILKRSNGY 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 589 DTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAV 668
Cdd:TIGR01192 462 DTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLF 541
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 9506367 669 LDHGKICEHGTHEELLLKpNGLYRKLMNKQSFLSYNGAEQFLEPA 713
Cdd:TIGR01192 542 LDQGRLIEKGSFQELIQK-DGRFYKLLRRSGLLTNQPATKPLRKA 585
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
455-679 |
4.24e-66 |
|
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: 217.36 E-value: 4.24e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 455 GALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS 533
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARAL 613
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL----DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGT 679
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
113-698 |
3.35e-65 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 228.69 E-value: 3.35e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 113 RPAATGRSEVWKLLGLVRPERGRLSAAVGFLAV-SSVITMSAPFFLGRIID-VIytnpSEGYGDSLTRLCAVLTCVFLCG 190
Cdd:TIGR03797 114 RPLPDKALGLRDLLRFALRGARRDLLAILAMGLlGTLLGMLVPIATGILIGtAI----PDADRSLLVQIALALLAAAVGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 191 AA---ANGIRVYLMQSSGQSivnRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTA----LLGRSVTENLSdglraGA 263
Cdd:TIGR03797 190 AAfqlAQSLAVLRLETRMDA---SLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQirriLSGSTLTTLLS-----GI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 264 QASVGVGMMFFVSPSLATF-VLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEeRIGNIRTIRAFGKEMTEVEKY 342
Cdd:TIGR03797 262 FALLNLGLMFYYSWKLALVaVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQ-LINGISKLRVAGAENRAFARW 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 343 TGRVDQLLQLAQKEALARAGF--FGAAglsgnLIVLS---VLYKGGLLMGSAHMTVGELSSFlMYAF-WVGLSIGGLSSF 416
Cdd:TIGR03797 341 AKLFSRQRKLELSAQRIENLLtvFNAV-----LPVLTsaaLFAAAISLLGGAGLSLGSFLAF-NTAFgSFSGAVTQLSNT 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 417 YSELMKGLGAGGRLWELLERQPRlpfNEGMVLDEKTFQGALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSG 495
Cdd:TIGR03797 415 LISILAVIPLWERAKPILEALPE---VDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSG 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 496 SGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGAdnlsSVTAQQVERAAEVA 575
Cdd:TIGR03797 490 SGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA----PLTLDEAWEAARMA 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 576 NAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVliIAH 655
Cdd:TIGR03797 566 GLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIV--IAH 643
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 9506367 656 RLSTIKNANFVAVLDHGKICEHGTHEELLLKPnGLYRKLMNKQ 698
Cdd:TIGR03797 644 RLSTIRNADRIYVLDAGRVVQQGTYDELMARE-GLFAQLARRQ 685
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
129-686 |
2.02e-63 |
|
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: 220.68 E-value: 2.02e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 129 VRPERGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYGDSLTRLCAVLtCVFLCGAAAngIRVYLMQSSGQSI 208
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGL-YLFLGLLDA--LRSFVLVRIGEKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 209 VNRLRTSLFSSILRQEVAFFDKtRTGELINrlssDTALLGRSVTenlSDGLRAGAQAS---VGVGMMFFVSPSLATFVLS 285
Cdd:TIGR01842 78 DGALNQPIFAASFSATLRRGSG-DGLQALR----DLDQLRQFLT---GPGLFAFFDAPwmpIYLLVCFLLHPWIGILALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 286 VVPPISVLAVIYGRYLRK-LSKATQDSLAeATQLAEERIGNIRTIRAFGKeMTEVEKYTGRVDQLLQLAQKEALARAGFF 364
Cdd:TIGR01842 150 GAVVLVGLALLNNRATKKpLKEATEASIR-ANNLADSALRNAEVIEAMGM-MGNLTKRWGRFHSKYLSAQSAASDRAGML 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 365 GAAGLSGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMYAFW--VGLSIGGLSSFyselMKGLGAGGRLWELLERQPr 439
Cdd:TIGR01842 228 SNLSKYFRIVLQSlVLGLGAYLAIDGEITPGMMiaGSILVGRALapIDGAIGGWKQF----SGARQAYKRLNELLANYP- 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 440 lPFNEGMVLDEKtfQGALEFRNVHFTyPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLD 519
Cdd:TIGR01842 303 -SRDPAMPLPEP--EGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 520 GHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILL 599
Cdd:TIGR01842 379 GADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 600 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHG 678
Cdd:TIGR01842 456 SGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
....*...
gi 9506367 679 THEELLLK 686
Cdd:TIGR01842 536 ERDEVLAK 543
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-702 |
5.64e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 228.76 E-value: 5.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 152 SAPFFLGrIIDVIYTNPSegYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQEVAFFDKT 231
Cdd:PTZ00265 75 TLPFFVS-VFGVIMKNMN--LGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 232 RTgeliNRLSSDTALLGRSVTENL-SDGLRAGAQASVGVGMMF---FVSPSLATFVLSVVPPISVLAVIYGRYLrKLSKA 307
Cdd:PTZ00265 152 PG----SKLTSDLDFYLEQVNAGIgTKFITIFTYASAFLGLYIwslFKNARLTLCITCVFPLIYICGVICNKKV-KINKK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 308 TQDSLAEAT-QLAEERIGNIRTIRAFGKEMTEVEKYtgrvdQLLQLAQKEALARAGFFGA--AGLSGNLIVLSvlYKGGL 384
Cdd:PTZ00265 227 TSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKKF-----NLSEKLYSKYILKANFMESlhIGMINGFILAS--YAFGF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 385 LMGSaHMTVGELSSFLMYAFWVGLSI-----GGLSSFY---------SELMKGLGAGGRLWELLERQPRLPFNEgmvlDE 450
Cdd:PTZ00265 300 WYGT-RIIISDLSNQQPNNDFHGGSVisillGVLISMFmltiilpniTEYMKSLEATNSLYEIINRKPLVENND----DG 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 451 KTFQG--ALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL-DGHDIRQLN 527
Cdd:PTZ00265 375 KKLKDikKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDIN 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 528 PVWLRSKIGTVSQEPVLFSCSVAENIAY------------------GADNLSSVTAQQVERA------------------ 571
Cdd:PTZ00265 455 LKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedGNDSQENKNKRNSCRAkcagdlndmsnttdsnel 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 572 ------------AEVANAA------EFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN 633
Cdd:PTZ00265 535 iemrknyqtikdSEVVDVSkkvlihDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 634 EHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAVL---------------------------DHGK----------- 673
Cdd:PTZ00265 615 EYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnKNNKddnnnnnnnnn 694
|
650 660 670
....*....|....*....|....*....|....*...
gi 9506367 674 ---------ICEHGTHEELLLKPNGLYRKLMNKQSFLS 702
Cdd:PTZ00265 695 nkinnagsyIIEQGTHDALMKNKNGIYYTMINNQKVSS 732
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
205-693 |
5.04e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 222.98 E-value: 5.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 205 GQSIVNRLRTSLFSSILRQEVAFFDKTRT--GELINRLSSDTALLGRSVTENLSdglragaqASVGVGMMFFVSPSLATF 282
Cdd:PTZ00265 894 GEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNIV--------IFTHFIVLFLVSMVMSFY 965
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 283 VLSVVPpiSVLAVIYGRYLR------KLSKATQDSLAEATQ-------------------LAEERIGNIRTIRAFGKE-- 335
Cdd:PTZ00265 966 FCPIVA--AVLTGTYFIFMRvfairaRLTANKDVEKKEINQpgtvfaynsddeifkdpsfLIQEAFYNMNTVIIYGLEdy 1043
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 336 -MTEVEKytgRVDQLLQLAQKEALARAGFFGAAGlSGNLIVLSVLYK-GGLLMGSAHMTVGELSSFLMYAFWVGLSIGGL 413
Cdd:PTZ00265 1044 fCNLIEK---AIDYSNKGQKRKTLVNSMLWGFSQ-SAQLFINSFAYWfGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 414 SSFYSELMKGLGAGGRLWELLERQPRLPF--NEGMVLDEKT-FQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTAL 490
Cdd:PTZ00265 1120 MSLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIRIKNKNdIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAI 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 491 VGPSGSGKSTVVSLLLRLYD------------------------------------------------------PNSGTV 516
Cdd:PTZ00265 1200 VGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKI 1279
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 517 SLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKG 596
Cdd:PTZ00265 1280 LLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED---ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYG 1356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 597 ILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLDH--- 671
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdr 1436
|
570 580
....*....|....*....|....
gi 9506367 672 -GKICE-HGTHEELLLKPNGLYRK 693
Cdd:PTZ00265 1437 tGSFVQaHGTHEELLSVQDGVYKK 1460
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
139-430 |
2.87e-60 |
|
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: 204.25 E-value: 2.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFS 218
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNT---ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 219 SILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYG 298
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 299 RYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSV 378
Cdd:cd18575 158 RRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 379 LYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18575 238 LWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
429-698 |
1.69e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 210.45 E-value: 1.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 429 RLWELLERQPRLPFNEGMVLDEKtfQGALEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRL 508
Cdd:PRK11160 313 RINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 509 YDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLS----SVTAQQVERAAEVANaaefirsf 584
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASdealIEVLQQVGLEKLLED-------- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 585 PQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNAN 664
Cdd:PRK11160 462 DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFD 541
|
250 260 270
....*....|....*....|....*....|....
gi 9506367 665 FVAVLDHGKICEHGTHEELLLKpNGLYRKLMNKQ 698
Cdd:PRK11160 542 RICVMDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
154-429 |
4.81e-59 |
|
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: 201.23 E-value: 4.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 154 PFFLGRIIDVIYT---NPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQEVAFFDK 230
Cdd:cd18574 16 PLLLGDLVNVISRslkETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 231 TRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRYLRKLSKATQD 310
Cdd:cd18574 96 HRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 311 SLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAH 390
Cdd:cd18574 176 QVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGE 255
|
250 260 270
....*....|....*....|....*....|....*....
gi 9506367 391 MTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGR 429
Cdd:cd18574 256 LTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGAR 294
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
142-430 |
3.20e-57 |
|
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: 196.38 E-value: 3.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 142 FLAVSSVITMSAPFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSIL 221
Cdd:cd18784 4 FLLAAAVGEIFIPYYTGQVIDGIVIEKSQ---DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 222 RQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRYL 301
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 302 RKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYK 381
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 9506367 382 GGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
136-430 |
8.11e-57 |
|
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: 194.96 E-value: 8.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTnpsegyGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSA------GGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAV 295
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 296 IYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIV 375
Cdd:cd18551 155 PLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLAL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 376 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18551 235 LVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
136-430 |
6.72e-56 |
|
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: 192.77 E-value: 6.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIytnPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV---IPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAV 295
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 296 IYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIV 375
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 376 LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
136-403 |
2.00e-55 |
|
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: 190.93 E-value: 2.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDvIYTNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILD-VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAV 295
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 296 IYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIV 375
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260
....*....|....*....|....*...
gi 9506367 376 LSVLYKGGLLMGSAHMTVGELSSFLMYA 403
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
457-684 |
8.69e-55 |
|
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: 187.54 E-value: 8.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPV--LFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRIAIAR 611
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLglpREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELL 684
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
479-698 |
2.01e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 193.91 E-value: 2.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRlYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGAD 558
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 559 NLSsvtAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQ 638
Cdd:PRK11174 449 DAS---DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 639 EALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMNKQ 698
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
211-657 |
2.10e-53 |
|
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: 192.58 E-value: 2.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 211 RLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSP--------SLATF 282
Cdd:TIGR02868 87 ALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVpaalilaaGLLLA 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 283 VLsVVPPISVLAV-IYGRYLRKLSKATQDSLAEATQLAEErignirtIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARA 361
Cdd:TIGR02868 167 GF-VAPLVSLRAArAAEQALARLRGELAAQLTDALDGAAE-------LVASGALPAALAQVEEADRELTRAERRAAAATA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 362 GFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLE-----R 436
Cdd:TIGR02868 239 LGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDaagpvA 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 437 QPRLPFNEGMVLDEKTfqgaLEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV 516
Cdd:TIGR02868 319 EGSAPAAGAVGLGKPT----LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 517 SLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKG 596
Cdd:TIGR02868 393 TLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPD---ATDEELWAALERVGLADWLRALPDGLDTVLGEGG 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 597 ILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRL 657
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
457-693 |
3.63e-52 |
|
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: 188.96 E-value: 3.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP--EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV---WL 531
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQEPvlFSC-----SVAENIAYGADNLSSVTAQQV-ERAAEVANA----AEFIRSFPQGFdtvvgekgillSG 601
Cdd:COG1123 341 RRRVQMVFQDP--YSSlnprmTVGDIIAEPLRLHGLLSRAERrERVAELLERvglpPDLADRYPHEL-----------SG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 602 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 678
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDG 487
|
250
....*....|....*
gi 9506367 679 THEELLLKPNGLYRK 693
Cdd:COG1123 488 PTEEVFANPQHPYTR 502
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
136-430 |
5.13e-52 |
|
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: 182.24 E-value: 5.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDL---EALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAV 295
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 296 IYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAG------FFGAAGL 369
Cdd:cd18552 158 RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALssplmeLLGAIAI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 370 SGnlivlsVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18552 238 AL------VLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
457-655 |
6.14e-52 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.86 E-value: 6.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSCSVAENIAYgadnlssvTAQQVERAAEVANAAEFIRSFpqGFDTVVGEKGI-LLSGGQKQRIAIARALLK 615
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPF--------PFQLRERKFDRERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAH 655
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
457-674 |
3.06e-50 |
|
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: 173.17 E-value: 3.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSCSVAENIaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLKN 616
Cdd:cd03246 80 YLPQDDELFSGSIAENI---------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANFVAVLDHGKI 674
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
457-683 |
1.63e-49 |
|
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: 173.14 E-value: 1.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD-----PNSGTVSLDGHDIRQL--NPV 529
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 530 WLRSKIGTVSQEPVLFSCSVAENIAYG--------ADNLSSVTAQQVERAA---EVANAAefirsfpqgfdtvvgeKGIL 598
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiklKEELDERVEEALRKAAlwdEVKDRL----------------HALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEH 677
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEF 221
|
....*.
gi 9506367 678 GTHEEL 683
Cdd:cd03260 222 GPTEQI 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
457-678 |
2.26e-49 |
|
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: 172.69 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 532
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPvlFSC-----SVAENIA------YGADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSG 601
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHE-----------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 602 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 678
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
457-684 |
2.76e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.56 E-value: 2.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 536
Cdd:COG1131 1 IEVRGLTKRYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLF-SCSVAENIAYGADnLSSVTAQQVERAAEvanaaEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLK 615
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFAR-LYGLPRKEARERID-----ELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELL 684
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
457-687 |
6.99e-49 |
|
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: 171.61 E-value: 6.99e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 532
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPVLFSC-SVAENIAYGADNLSSVTAQQVERAAEV---ANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIA 608
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELlelVGLEDKADAYPAQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 609 IARALLKNPKILLLDEATSALDAENehlVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 682
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPET---TQSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....*
gi 9506367 683 LLLKP 687
Cdd:cd03258 228 VFANP 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
457-687 |
7.00e-49 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 174.88 E-value: 7.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 532
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPVLF-SCSVAENIAY-----GADnlssvTAQQVERAAEVANA---AEFIRSFP-QgfdtvvgekgilLSGG 602
Cdd:COG1135 82 RKIGMIFQHFNLLsSRTVAENVALpleiaGVP-----KAEIRKRVAELLELvglSDKADAYPsQ------------LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 603 QKQRIAIARALLKNPKILLLDEATSALDAENEH----LVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEH 677
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRsildLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
250
....*....|
gi 9506367 678 GTHEELLLKP 687
Cdd:COG1135 223 GPVLDVFANP 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
456-684 |
7.61e-48 |
|
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: 169.45 E-value: 7.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 535
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVL-FSCSVAENIAYG----ADNLSSVTA---QQVERAAEVANAAEFI-RSFPQgfdtvvgekgilLSGGQKQR 606
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphLGLFGRPSAedrEAVEEALERTGLEHLAdRPVDE------------LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEEL 683
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 9506367 684 L 684
Cdd:COG1120 226 L 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
211-684 |
1.02e-47 |
|
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: 182.45 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 211 RLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGVGMMFFVSPSLATFVlsvVPPI 290
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNV-IGALIVILLATPIAAVI---IPPL 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 291 SVLAVIYGRYL----RKLSKATQDSLAEATQLAEERIGNIRTIRAFgkemTEVEKYTGRVDQLLQLAQKEALAR--AGFF 364
Cdd:TIGR00957 1115 GLLYFFVQRFYvassRQLKRLESVSRSPVYSHFNETLLGVSVIRAF----EEQERFIHQSDLKVDENQKAYYPSivANRW 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 365 GAAGLS--GNLIVL-SVLYKgglLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRLP 441
Cdd:TIGR00957 1191 LAVRLEcvGNCIVLfAALFA---VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAP 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 442 FNEGMVLDEKTF--QGALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL 518
Cdd:TIGR00957 1268 WQIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 519 DGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGIL 598
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL----DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHG 678
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFG 1501
|
....*.
gi 9506367 679 THEELL 684
Cdd:TIGR00957 1502 APSNLL 1507
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
458-673 |
1.95e-47 |
|
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: 166.87 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 537
Cdd:cd03225 1 ELKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 538 VSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAaefirsfpqgfdtvVGEKGIL------LSGGQKQRIAI 609
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALEL--------------VGLEGLRdrspftLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 610 ARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGK 673
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
142-429 |
7.73e-47 |
|
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: 167.90 E-value: 7.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 142 FLAVSSVITMSAPFFLGRIIDVIytnpSEGYGDSLTRLCAVLTCVFLCGAA-ANGIRVYLMQSSGQSIVNRLRTSLFSSI 220
Cdd:cd18590 4 FLTLAVICETFIPYYTGRVIDIL----GGEYQHNAFTSAIGLMCLFSLGSSlSAGLRGGLFMCTLSRLNLRLRHQLFSSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 221 LRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRY 300
Cdd:cd18590 80 VQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 301 LRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLY 380
Cdd:cd18590 160 HQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 9506367 381 KGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGR 429
Cdd:cd18590 240 CGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAK 288
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
138-406 |
8.15e-47 |
|
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: 167.99 E-value: 8.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 138 AAVGFLAVSSVITMSAPFFLGRIIDVIYTnpsEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLF 217
Cdd:cd18542 3 LAILALLLATALNLLIPLLIRRIIDSVIG---GGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 218 SSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIY 297
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 298 GRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLS 377
Cdd:cd18542 160 FKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVL 239
|
250 260
....*....|....*....|....*....
gi 9506367 378 VLYKGGLLMGSAHMTVGELSSFLMYAFWV 406
Cdd:cd18542 240 VLWVGGYLVINGEITLGELVAFISYLWML 268
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
457-673 |
2.16e-46 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 163.79 E-value: 2.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVSVF--QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlrsK 534
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFSCSVAENIAYGA--DNlssvtaqqvERAAEVANAAEF---IRSFPQGFDTVVGEKGILLSGGQKQRIAI 609
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpfDE---------ERYEKVIKACALepdLEILPDGDLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 610 ARALLKNPKILLLDEATSALDAE-NEHLVQEAL-DRLMEGRTVLIIAHRLSTIKNANFVAVLDHGK 673
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
457-684 |
4.82e-46 |
|
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: 163.88 E-value: 4.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 536
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFS-CSVAENIAYGAdnlssvTAQQVERAAEVANAAEFIRSF--PQGFDTVVGEkgilLSGGQKQRIAIARAL 613
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYFA------ELYGLFDEELKKRIEELIELLglEEFLDRRVGE----LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
456-690 |
1.10e-45 |
|
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: 170.85 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPVWLR 532
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQgfdtvvgekgiLLSGGQKQRI 607
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAvglERRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
....*.
gi 9506367 685 LKPNGL 690
Cdd:COG1123 232 AAPQAL 237
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
457-687 |
3.29e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 161.70 E-value: 3.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDI----RQLNP 528
Cdd:COG1126 2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKST----LLRcinlLEEPDSGTITVDGEDLtdskKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 vwLRSKIGTVSQEPVLFS-CSVAENIAYGadnlsSVTAQQVERAAEVANA---------AEFIRSFP-Qgfdtvvgekgi 597
Cdd:COG1126 75 --LRRKVGMVFQQFNLFPhLTVLENVTLA-----PIKVKKMSKAEAEERAmellervglADKADAYPaQ----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 598 lLSGGQKQRIAIARALLKNPKILLLDEATSALDAEnehLVQEALDrLM-----EGRTVLIIAHRLSTIKN-ANFVAVLDH 671
Cdd:COG1126 137 -LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMrdlakEGMTMVVVTHEMGFAREvADRVVFMDG 211
|
250
....*....|....*.
gi 9506367 672 GKICEHGTHEELLLKP 687
Cdd:COG1126 212 GRIVEEGPPEEFFENP 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
456-684 |
5.21e-45 |
|
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: 160.92 E-value: 5.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLR 532
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQV-ERAAEVANA---AEFIRSFPqgfdtvvGEkgilLSGGQKQRI 607
Cdd:COG1127 82 RRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIrELVLEKLELvglPGAADKMP-------SE----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 608 AIARALLKNPKILLLDEATSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 682
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
..
gi 9506367 683 LL 684
Cdd:COG1127 229 LL 230
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
446-687 |
5.49e-45 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 161.74 E-value: 5.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 446 MVLDEKTFQGALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD--PN---SGTVSLDG 520
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 521 HDI--RQLNPVWLRSKIGTVSQEPVLFSCSVAENIAYGA----DNLSSVTAQQVE----RAA---EVANaaefirsfpqg 587
Cdd:COG1117 78 EDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgIKSKSELDEIVEeslrKAAlwdEVKD----------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 588 fdtVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAH------RLStik 661
Cdd:COG1117 147 ---RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS--- 220
|
250 260
....*....|....*....|....*.
gi 9506367 662 naNFVAVLDHGKICEHGTHEELLLKP 687
Cdd:COG1117 221 --DYTAFFYLGELVEFGPTEQIFTNP 244
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
155-430 |
6.08e-45 |
|
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: 163.03 E-value: 6.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 155 FFLGRIIDVI-----YTNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQEVAFFD 229
Cdd:cd18577 20 IVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 230 KTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRYLRKLSKATQ 309
Cdd:cd18577 100 KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 310 DSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSA 389
Cdd:cd18577 180 EAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDG 259
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 9506367 390 HMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18577 260 EISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
457-690 |
6.90e-45 |
|
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: 161.83 E-value: 6.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW-LRSKI 535
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRIAIA 610
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLgvpREEMRKRVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL---- 684
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFsqve 228
|
....*..
gi 9506367 685 -LKPNGL 690
Cdd:TIGR04520 229 lLKEIGL 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
457-678 |
8.05e-45 |
|
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: 158.25 E-value: 8.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIG 536
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSCSVAENIaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekGILLSGGQKQRIAIARALLKN 616
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHG 678
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
458-673 |
8.81e-45 |
|
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: 157.41 E-value: 8.81e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 537
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 538 VSQepvlfscsvaeniaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLKNP 617
Cdd:cd00267 78 VPQ----------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 618 KILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNA-NFVAVLDHGK 673
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
457-687 |
1.25e-44 |
|
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: 160.16 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPA-RPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 535
Cdd:cd03295 1 IEFENVTKRYGGgKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEV-----ANAAEFIRSFPqgfdtvvGEkgilLSGGQKQRIAI 609
Cdd:cd03295 78 GYVIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADELlalvgLDPAEFADRYP-------HE----LSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 610 ARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRL-STIKNANFVAVLDHGKICEHGTHEELLLK 686
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
.
gi 9506367 687 P 687
Cdd:cd03295 227 P 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
456-684 |
2.82e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.10 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnpvwlRSKI 535
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVL---FSCSVAENIAYGADN-------LSSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQ 605
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVLMGRYGrrglfrrPSRADREAVDEALERVGLEDLA-------DRPIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICeHGTHEEL 683
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRGLVA-HGPPEEV 225
|
.
gi 9506367 684 L 684
Cdd:COG1121 226 L 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
456-674 |
5.26e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.90 E-value: 5.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPA-RPEVSVFQDFSLSIPSGSVTALVGPSGSGKST---VVSLLLRlydPNSGTVSLDGHDIRQLNP--- 528
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSErel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 -VWLRSKIGTVSQE----PVLfscSVAENIAYGADnLSSVTAQQV-ERAAEVANA---AEFIRSFPqgfdtvvGEkgilL 599
Cdd:COG1136 81 aRLRRRHIGFVFQFfnllPEL---TALENVALPLL-LAGVSRKERrERARELLERvglGDRLDHRP-------SQ----L 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 600 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLDHGKI 674
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
456-655 |
1.34e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.94 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlrsK 534
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPqgfdtvvGEkgilLSGGQKQRIAIA 610
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLELvglAGFEDAYP-------HQ----LSGGMRQRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH 655
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
126-439 |
2.02e-43 |
|
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: 159.15 E-value: 2.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 126 LGLVRPERGRLsaAVGFLAvsSVITMSAP----FFLGRIIDVIYTNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLM 201
Cdd:cd18578 1 LKLNKPEWPLL--LLGLIG--AIIAGAVFpvfaILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 202 QSSGQSIVNRLRTSLFSSILRQEVAFFDKTR--TGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSL 279
Cdd:cd18578 77 GIAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 280 ATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALA 359
Cdd:cd18578 157 ALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 360 RAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPR 439
Cdd:cd18578 237 SGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
457-674 |
3.09e-43 |
|
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: 153.71 E-value: 3.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 536
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFscsvaeniaygaDNLSsvtaqqveraaevanAAEFIRsfpqgfdtvvgekgilLSGGQKQRIAIARALLKN 616
Cdd:cd03230 77 YLPEEPSLY------------ENLT---------------VRENLK----------------LSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 674
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
457-655 |
4.59e-43 |
|
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: 154.94 E-value: 4.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlrsKI 535
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQKQRIAIAR 611
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELvglSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH 655
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTH 190
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
455-679 |
6.33e-43 |
|
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: 154.11 E-value: 6.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 455 GALEFRNVHFTYpaRPEV-SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS 533
Cdd:cd03369 5 GEIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQVERAAEVAnaaefirsfpqgfdtvvgEKGILLSGGQKQRIAIARAL 613
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL----DPFDEYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGT 679
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
475-627 |
2.18e-42 |
|
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: 150.49 E-value: 2.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFS-CSVAENI 553
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 554 AYGA---DNLSSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:pfam00005 81 RLGLllkGLSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
199-696 |
2.85e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 165.92 E-value: 2.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 199 YLMQSSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsvgvgmmffvsps 278
Cdd:PLN03232 972 FWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQL------------- 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 279 LATFVL-SVVPPISVLAVI------YGRYLRKLSKATQ----DSLAEATQLAE--ERIGNIRTIRAFgKEMTEVEKYTGR 345
Cdd:PLN03232 1039 LSTFALiGTVSTISLWAIMpllilfYAAYLYYQSTSREvrrlDSVTRSPIYAQfgEALNGLSSIRAY-KAYDRMAKINGK 1117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 346 -VDQLLQlaqkealaragfFGAAGLSGN--LIVLSVLYKGGLLMGSAHMTV---GELSSFLMYAFWVGLSIGGLSSFYSE 419
Cdd:PLN03232 1118 sMDNNIR------------FTLANTSSNrwLTIRLETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTL 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 420 LMKGLGAGGRLWELLERQPR------LPfNEGMVLDEKT-------FQGALEFRNVHFTYpaRPEVS-VFQDFSLSIPSG 485
Cdd:PLN03232 1186 LSGVLRQASKAENSLNSVERvgnyidLP-SEATAIIENNrpvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPS 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 486 SVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIaygaDNLSSVTA 565
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI----DPFSEHND 1338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 566 QQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM 645
Cdd:PLN03232 1339 ADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF 1418
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 9506367 646 EGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMN 696
Cdd:PLN03232 1419 KSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
199-694 |
2.94e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 166.07 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 199 YLMQSSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVtenlsdglragaqaSVGVGM-MFFVSP 277
Cdd:PLN03130 975 YWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV--------------AVFVNMfLGQIFQ 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 278 SLATFVL-SVVPPISVLAVI------YGRYLRKLSKATQ----DSLAEATQLAE--ERIGNIRTIRAF----------GK 334
Cdd:PLN03130 1041 LLSTFVLiGIVSTISLWAIMpllvlfYGAYLYYQSTAREvkrlDSITRSPVYAQfgEALNGLSTIRAYkaydrmaeinGR 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 335 EMTEVEKYTgrvdqLLQLAQKEALA-RAGFFGA--AGLSGNLIVL---------SVLYKGGLLMGSAHMTVGELSSFLMY 402
Cdd:PLN03130 1121 SMDNNIRFT-----LVNMSSNRWLAiRLETLGGlmIWLTASFAVMqngraenqaAFASTMGLLLSYALNITSLLTAVLRL 1195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 403 AfwvglsigglssfySELMKGLGAGGRLWELLERQPRLPfnegMVLDEK------TFQGALEFRNVHFTYpaRPEVS-VF 475
Cdd:PLN03130 1196 A--------------SLAENSLNAVERVGTYIDLPSEAP----LVIENNrpppgwPSSGSIKFEDVVLRY--RPELPpVL 1255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIay 555
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL-- 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 556 gaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEH 635
Cdd:PLN03130 1334 --DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 636 LVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKL 694
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
136-429 |
4.09e-42 |
|
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: 154.87 E-value: 4.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYG---DSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRL 212
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 213 RTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISV 292
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 293 LAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKealarAGFFGAA----- 367
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK-----AQFYSGLlmpim 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 368 GLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGR 429
Cdd:cd18547 236 NFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
141-426 |
5.38e-42 |
|
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: 154.55 E-value: 5.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 141 GFLAVSSVITMSAPFFLGRIIDVIYTNPS-EGYGDSLTrLCAVLT-----CVFLCgaaaNGIRVYLMQSsgqsIVNRLRT 214
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDApEAFTAAIT-VMSLLTiasavSEFVC----DLIYNITMSR----IHSRLQG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 215 SLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLA 294
Cdd:cd18589 74 LVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 295 VIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLI 374
Cdd:cd18589 154 KFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLAL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 375 VLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGA 426
Cdd:cd18589 234 KVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGS 285
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
456-688 |
6.31e-42 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 156.03 E-value: 6.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQLnPVWL 531
Cdd:COG3842 5 ALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGL-PPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RsKIGTVSQEPVLFS-CSVAENIAYG--ADNLS-SVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRI 607
Cdd:COG3842 77 R-NVGMVFQDYALFPhLTVAENVAFGlrMRGVPkAEIRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 608 AIARALLKNPKILLLDEATSALDAEN-EHLVQEaLDRLME--GRTVLIIAHRLS---TIknANFVAVLDHGKICEHGTHE 681
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLrEEMREE-LRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPE 221
|
....*..
gi 9506367 682 ELLLKPN 688
Cdd:COG3842 222 EIYERPA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
457-683 |
1.55e-41 |
|
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: 151.12 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---RS 533
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEPVLF-SCSVAENIAY-----GADNLSSVTAQQVERAAEVaNAAEFIRSFPqgfdtvvGEkgilLSGGQKQRI 607
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFplrehTRLSEEEIREIVLEKLEAV-GLRGAEDLYP-------AE----LSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 683
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
457-678 |
2.06e-41 |
|
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: 149.98 E-value: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRsKIG 536
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERR-NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAEVA---NAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARA 612
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLelvGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 613 LLKNPKILLLDEATSALDAE-NEHLVQEALDRLME-GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHG 678
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKlREELREELKELQRElGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
457-673 |
3.59e-41 |
|
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: 148.10 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN--PVWLRSK 534
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFS-CSVAENIAYGadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARAL 613
Cdd:cd03229 78 IGMVFQDFALFPhLTVLENIALG------------------------------------------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGK 673
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
477-688 |
5.51e-41 |
|
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: 149.79 E-value: 5.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTVSQEPVLF-SCSVAENIAY 555
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 556 GadnLSSVTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEH 635
Cdd:cd03299 95 G---LKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 636 LVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 688
Cdd:cd03299 167 KLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
456-684 |
1.92e-40 |
|
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: 148.80 E-value: 1.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSK 534
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLfSC----SVAENIA-----YGADNlssvTAQQVERAAE-VANAAEFIRSFP-QgfdtvvgekgilLSGGQ 603
Cdd:COG1124 81 VQMVFQDPYA-SLhprhTVDRILAeplriHGLPD----REERIAELLEqVGLPPSFLDRYPhQ------------LSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 604 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTH 680
Cdd:COG1124 144 RQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTV 223
|
....
gi 9506367 681 EELL 684
Cdd:COG1124 224 ADLL 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
457-655 |
2.01e-40 |
|
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: 147.64 E-value: 2.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---- 531
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQE----PVLfscSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQK 604
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEELLERvglGDRLNHYPSE-----------LSGGQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9506367 605 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAH 655
Cdd:cd03255 147 QRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTH 199
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
457-682 |
7.51e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.97 E-value: 7.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLRS 533
Cdd:COG2884 2 IRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQE-PVLFSCSVAENIAY-----GADnlSSVTAQQVERAAEVANAAEFIRSFPqgfdtvvgekgILLSGGQKQRI 607
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKS--RKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANF-VAVLDHGKICEHGTHEE 682
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
136-402 |
1.17e-39 |
|
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: 147.92 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDViYTNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDD-YIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQAS---VGV-GMMFFVSPSLATFVLSVVPPIS 291
Cdd:cd18544 80 LFSHIQRLPLSFFDRTPVGRLVTRVTNDTE----ALNELFTSGLVTLIGDLlllIGIlIAMFLLNWRLALISLLVLPLLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 292 VLAVIYGRYLRKLSKATQDSLAEA-TQLAeERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLS 370
Cdd:cd18544 156 LATYLFRKKSRKAYREVREKLSRLnAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELL 234
|
250 260 270
....*....|....*....|....*....|..
gi 9506367 371 GNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 402
Cdd:cd18544 235 SSLALALVLWYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
451-684 |
2.24e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 146.29 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 451 KTFQGALEFRNVHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW 530
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 LRSKIGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 605
Cdd:PRK13632 81 IRKKIGIIFQNPdnQFIGATVEDDIAFGLENKkvpPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL 683
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
.
gi 9506367 684 L 684
Cdd:PRK13632 230 L 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
458-674 |
1.13e-38 |
|
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: 141.42 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 537
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 538 VSQepvlfscsvaeniaygadnlssvtaqqverAAEVANAAEFIRsfpQGFDTvvgekgilLSGGQKQRIAIARALLKNP 617
Cdd:cd03214 78 VPQ------------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 618 KILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKI 674
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
457-684 |
1.16e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.97 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIG 536
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFS-CSVAENIAYGAD---NLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARA 612
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGLRpglKLTAEQRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 613 LLKNPKILLLDEATSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
457-687 |
2.24e-38 |
|
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: 145.20 E-value: 2.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPVWLR 532
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 S----KIGTVSQEPvlFSC-----SVAENIAYGADNLSSVTAQQV-ERAAEV------ANAAEFIRSFP-Qgfdtvvgek 595
Cdd:COG0444 82 KirgrEIQMIFQDP--MTSlnpvmTVGDQIAEPLRIHGGLSKAEArERAIELlervglPDPERRLDRYPhE--------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 596 gilLSGGQKQRIAIARALLKNPKILLLDEATSALDAenehLVQ-EALDRLME-----GRTVLIIAHRLSTIKN-ANFVAV 668
Cdd:COG0444 151 ---LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNLLKDlqrelGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*....
gi 9506367 669 LDHGKICEHGTHEELLLKP 687
Cdd:COG0444 224 MYAGRIVEEGPVEELFENP 242
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
136-403 |
2.45e-38 |
|
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: 144.19 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIID-VIYTNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRT 214
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 215 SLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGVG-MMFFVSPSLATFVLSVVPPISVL 293
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMI-IGIGvVLFSLNWKLALLVLIPVPLVVWG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 294 AVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNL 373
Cdd:cd18563 160 SYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSL 239
|
250 260 270
....*....|....*....|....*....|
gi 9506367 374 IVLSVLYKGGLLMGSAHMTVGELSSFLMYA 403
Cdd:cd18563 240 GTLIVWYFGGRQVLSGTMTLGTLVAFLSYL 269
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
457-674 |
4.98e-38 |
|
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: 140.74 E-value: 4.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI----RQLNPvwLR 532
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINE--LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPVLFS-CSVAENIAygadnLSSVTAQQVERAAEVANA---------AEFIRSFPQGfdtvvgekgilLSGG 602
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENIT-----LAPIKVKGMSKAEAEERAlellekvglADKADAYPAQ-----------LSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 603 QKQRIAIARALLKNPKILLLDEATSALDAEnehLVQEALDrLM-----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 674
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMkdlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
136-399 |
1.07e-37 |
|
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: 142.24 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYgdsLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGL---LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAV 295
Cdd:cd18550 78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 296 IYGRYLRKLSKATQDSLAEATQLAEER--IGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNL 373
Cdd:cd18550 158 RVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAI 237
|
250 260
....*....|....*....|....*.
gi 9506367 374 IVLSVLYKGGLLMGSAHMTVGELSSF 399
Cdd:cd18550 238 GPALVYWVGGLLVIGGGLTIGTLVAF 263
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
136-402 |
2.29e-37 |
|
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: 141.39 E-value: 2.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTA--SQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRND 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQASVG----VGMMFFVSPSLATFVLSVVPPIS 291
Cdd:cd18541 79 LFAHLLTLSPSFYQKNRTGDLMARATNDLN----AVRMALGPGILYLVDALFLgvlvLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 292 VLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSG 371
Cdd:cd18541 155 LLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLI 234
|
250 260 270
....*....|....*....|....*....|.
gi 9506367 372 NLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 402
Cdd:cd18541 235 GLSFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
458-678 |
2.37e-37 |
|
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: 138.82 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnpvwlRSKIGT 537
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 538 VSQEPVL---FSCSVAENIAYGAD-------NLSSVTAQQVERAAEVANAAEFI-RSFpqgfdtvvGEkgilLSGGQKQR 606
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYghkglfrRLSKADKAKVDEALERVGLSELAdRQI--------GE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICeHG 678
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVVA-SG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
458-687 |
3.00e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 142.63 E-value: 3.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS--- 533
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQE-PVLFSCSVAENIAYgADNLSSVTAQQVERAA----EVANAAEFIRSFP-QgfdtvvgekgilLSGGQKQRI 607
Cdd:PRK11153 83 QIGMIFQHfNLLSSRTVFDNVAL-PLELAGTPKAEIKARVtellELVGLSDKADRYPaQ------------LSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVF 229
|
...
gi 9506367 685 LKP 687
Cdd:PRK11153 230 SHP 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
457-683 |
4.00e-37 |
|
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: 139.24 E-value: 4.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---RS 533
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEPVLFS-CSVAENIAYGADN--------LSSVTAQQVERAAEVANAAEFIRSFPQGFDTvvgekgilLSGGQK 604
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQRADQ--------LSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 605 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIK-NANFVAVLDHGKICEHGTHE 681
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 9506367 682 EL 683
Cdd:cd03256 231 EL 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
456-674 |
8.43e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 138.27 E-value: 8.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---R 532
Cdd:COG3638 2 MLELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPVLFS-CSVAENIAYGADN--------LSSVTAQQVERAAEVanaaefirsfpqgFDTVvgekGIL----- 598
Cdd:COG3638 80 RRIGMIFQQFNLVPrLSVLTNVLAGRLGrtstwrslLGLFPPEDRERALEA-------------LERV----GLAdkayq 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 ----LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDH 671
Cdd:COG3638 143 radqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRD 222
|
...
gi 9506367 672 GKI 674
Cdd:COG3638 223 GRV 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
457-687 |
8.54e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.44 E-value: 8.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIrqlnPVWL- 531
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTT----LLRiiagLETPDSGRIVLNGRDL----FTNLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 --RSKIGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAE----VaNAAEFIRSFP-QgfdtvvgekgilLSGGQ 603
Cdd:COG1118 72 prERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelV-QLEGLADRYPsQ------------LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 604 KQRIAIARALLKNPKILLLDEATSALDA----ENEHLVQEALDRLmeGRTVLIIAH------RLstiknANFVAVLDHGK 673
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGR 211
|
250
....*....|....
gi 9506367 674 ICEHGTHEELLLKP 687
Cdd:COG1118 212 IEQVGTPDEVYDRP 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
461-674 |
1.73e-36 |
|
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: 136.23 E-value: 1.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 461 NVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdiRQLNPVWLRSKIGTVSQ 540
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 541 EP--VLFSCSVAENIAYGADNLSSVtAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPK 618
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAG-NEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 619 ILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 674
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
456-697 |
2.77e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 138.01 E-value: 2.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPEvSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLL--LRLYDPNSGT-VSLDGHDIRQLNpVW-L 531
Cdd:PRK13640 5 IVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSkITVDGITLTAKT-VWdI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQEP--VLFSCSVAENIAYGADNlSSVTAQQ----VERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 605
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGLEN-RAVPRPEmikiVRDVLADVGMLDYIDSEPAN-----------LSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL 683
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
250 260
....*....|....*....|...
gi 9506367 684 -----LLKPNGL----YRKLMNK 697
Cdd:PRK13640 231 fskveMLKEIGLdipfVYKLKNK 253
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
476-687 |
1.35e-35 |
|
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: 135.46 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL----RSKIGTVSQEPVLF-SCSVA 550
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENIAYGADnLSSVTAQQ-VERAAEVANA---AEFIRSFPqgfdtvvGEkgilLSGGQKQRIAIARALLKNPKILLLDEAT 626
Cdd:cd03294 121 ENVAFGLE-VQGVPRAErEERAAEALELvglEGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506367 627 SALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:cd03294 189 SALDPLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
482-695 |
1.81e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 135.04 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 482 IPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIaygaDNLS 561
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL----DPEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 562 SVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEAL 641
Cdd:cd03288 120 KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9506367 642 DRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLM 695
Cdd:cd03288 200 MTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
457-683 |
3.33e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.76 E-value: 3.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYP--ARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdiRQLNP--VW-L 531
Cdd:PRK13635 6 IRVEHISFRYPdaATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEetVWdV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVER---AAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQR 606
Cdd:PRK13635 80 RRQVGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERvdqALRQVGMEDFLNREPHR-----------LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL 683
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
457-688 |
8.20e-34 |
|
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: 129.28 E-value: 8.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIG 536
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFS-CSVAENIAYG---ADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARA 612
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 613 LLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKPN 688
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
479-683 |
1.08e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 131.78 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLRSKIGTVSQEPvlFSC-----SVA 550
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDP--YASlnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENIAYGADNLSSVTAQQV-ERAAE----VANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLLDEA 625
Cdd:COG4608 116 DIIAEPLRIHGLASKAERrERVAEllelVGLRPEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 626 TSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 683
Cdd:COG4608 185 VSALDvsiqAQVLNLLEDLQDEL--GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
455-691 |
1.40e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 132.12 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 455 GALEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQLNPVw 530
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTSGEILIGGRDVTDLPPK- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 lRSKIGTVSQEPVLF-SCSVAENIAYGadnLS------SVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQ 603
Cdd:COG3839 74 -DRNIAMVFQSYALYpHMTVYENIAFP---LKlrkvpkAEIDRRVREAAELLGLEDLLDRKPKQ-----------LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 604 KQRIAIARALLKNPKILLLDEATSALDAE-NEHLVQEaLDRLME--GRTVLI----------IAHRlstiknanfVAVLD 670
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDAKlRVEMRAE-IKRLHRrlGTTTIYvthdqveamtLADR---------IAVMN 208
|
250 260
....*....|....*....|.
gi 9506367 671 HGKICEHGTHEELLLKPNGLY 691
Cdd:COG3839 209 DGRIQQVGTPEELYDRPANLF 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
457-705 |
1.31e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.17 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIR---SFPQGfdtvvgekgilLSGGQKQRIAIAR 611
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLEradYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIA--HRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNG 689
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235
|
250 260
....*....|....*....|....*....
gi 9506367 690 LY-------------RKLMNKQSFLSYNG 705
Cdd:PRK13648 236 LTrigldlpfpikinQMLGHQTSFLTYEG 264
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
136-402 |
2.45e-32 |
|
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: 127.24 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIID-VIYTNPSEGYGDS-----------LTRLCAVLTCVFLCGAAANGIRVYLMQS 203
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDdVLGDKPLPGLLGLapllgpdplalLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 204 SGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFV 283
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 284 LSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGF 363
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 9506367 364 FGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 402
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
457-678 |
3.18e-32 |
|
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: 124.23 E-value: 3.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARpevSVFQDFSLSIPSGsVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 536
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLF-SCSVAENIAYGAdNLSSVTA----QQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIAR 611
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYIA-WLKGIPSkevkARVDEVLELVNLGDRA-------KKKIGS----LSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 678
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
472-682 |
3.28e-32 |
|
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: 124.86 E-value: 3.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 472 VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIGTVS--QEPVLF-SCS 548
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 549 VAENIAYGADNLSSVTAQQV----ERAAEVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDE 624
Cdd:cd03219 92 VLENVMVAAQARTGSGLLLArarrEEREARERAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 625 ATSAL-DAENEHLVqEALDRL-MEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 682
Cdd:cd03219 170 PAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
457-687 |
9.10e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 123.66 E-value: 9.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNV--HFTyparpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR--QLNPVWLR 532
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPVLFSCSVA-ENIAYGADNLSSVTAQQVERAAEVANA----AEFIRSFPqgfdtvvGEkgilLSGGQKQRI 607
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFGPLRVRGASKEEAEKQARELLAkvglAERAHHYP-------SE----LSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLL 685
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
..
gi 9506367 686 KP 687
Cdd:PRK09493 226 NP 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
457-674 |
1.31e-31 |
|
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: 122.52 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN----PvWLR 532
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiP-YLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQE-PVLFSCSVAENIAYG---ADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIA 608
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYENVAFAlevTGVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 609 IARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANF-VAVLDHGKI 674
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
457-681 |
1.32e-31 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 122.90 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSCSVAENIAYGAdnlsSVTAQQVERAAEVANAAEFirsfpqGFDTVVGEKGI-LLSGGQKQRIAIARALLK 615
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW----QIRNQQPDPAIFLDDLERF------ALPDTILTKNIaELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNANFVAVLD-HGKICEHGTHE 681
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVReqNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
135-420 |
1.54e-31 |
|
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: 124.50 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 135 RLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNpsegyGD--SLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRL 212
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPN-----GDlsGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 213 RTSLFSSILRQEVAFFDKTRTGELINRLSSDtallgrsvTENLSDGLRAGAQASVG--------VGMMFFVSPSLATFVL 284
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVIND--------VNSLSDLLSNGLINLIPdlltlvgiVIIMFSLNVRLALVTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 285 SVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFF 364
Cdd:cd18545 148 AVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFW 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 365 GAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA--FWvgLSIGGLSSFYSEL 420
Cdd:cd18545 228 PLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVgrFW--QPIRNLSNFYNQL 283
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
457-684 |
2.20e-31 |
|
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: 122.16 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSKI 535
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLF-SCSVAENIAYGADNLS-SVTAQQVERAAEVanaaefirsFPQgFDTVVGEKGILLSGGQKQRIAIARAL 613
Cdd:cd03224 78 GYVPEGRRIFpELTVEENLLLGAYARRrAKRKARLERVYEL---------FPR-LKERRKQLAGTLSGGEQQMLAIARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 614 LKNPKILLLDEATSALdAENehLVQEALDRLM----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:cd03224 148 MSRPKLLLLDEPSEGL-APK--IVEEIFEAIRelrdEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
456-688 |
2.87e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 123.31 E-value: 2.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKI 535
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEP--VLFSCSVAENIAYGADNLsSVTAQQVERAAEVANAA----EFIRSFPQGfdtvvgekgilLSGGQKQRIAI 609
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVNM-GLDKDEVERRVEEALKAvrmwDFRDKPPYH-----------LSYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 610 ARALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGThEELLLKP 687
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDE 228
|
.
gi 9506367 688 N 688
Cdd:PRK13647 229 D 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
456-657 |
4.28e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.83 E-value: 4.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLRSK 534
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFSC-SVAENIAYGADNLSSVTaqqVERAAEVANAAEFIRSFpqGFD----TVVGEkgilLSGGQKQRIAI 609
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLGREPRRGGL---IDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9506367 610 ARALLKNPKILLLDEATSAL-DAENEHLVqEALDRLM-EGRTVLIIAHRL 657
Cdd:COG1129 152 ARALSRDARVLILDEPTASLtEREVERLF-RIIRRLKaQGVAIIYISHRL 200
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
134-715 |
7.31e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 130.28 E-value: 7.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 134 GRLSAAVGFLA---VSSVITMSAPFFLGRiidviYTNPSEGYGDSlTRLCAVLTCVFLcGAAANGIRVYLMQSSGQSIVN 210
Cdd:PTZ00243 959 GGLHAAGFVLAtfaVTELVTVSSGVWLSM-----WSTRSFKLSAA-TYLYVYLGIVLL-GTFSVPLRFFLSYEAMRRGSR 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 211 RLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPslatFVLSVVPPI 290
Cdd:PTZ00243 1032 NMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQP----FVLVALVPC 1107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 291 SV----LAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVD-----QLLQLAQKEALA-R 360
Cdd:PTZ00243 1108 GYlyyrLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDvvyscSYLENVANRWLGvR 1187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 361 AGFFGaaglsgNLIVLSVLYKG--GLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGAGGRLW------- 431
Cdd:PTZ00243 1188 VEFLS------NIVVTVIALIGviGTMLRATSQEIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLyytdevp 1261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 432 -----ELLERQPRLPFNEGMVLD----------------EKTFQ-GALEFRNVHFTYpaRPEVS-VFQDFSLSIPSGSVT 488
Cdd:PTZ00243 1262 hedmpELDEEVDALERRTGMAADvtgtvviepasptsaaPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKV 1339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 489 ALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQV 568
Cdd:PTZ00243 1340 GIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV----DPFLEASSAEV 1415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 569 ERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLK-NPKILLLDEATSALDAENEHLVQEALDRLMEG 647
Cdd:PTZ00243 1416 WAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSA 1495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 648 RTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMNKqsfLSYNGAEQFLEPARA 715
Cdd:PTZ00243 1496 YTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA---LGRSEAKRFLQLVGR 1560
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
457-690 |
2.49e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 121.28 E-value: 2.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARpevSVFQ-----DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQ 525
Cdd:PRK13634 3 ITFQKVEHRYQYK---TPFErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 526 LNPvwLRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAAE----VANAAEFIRSFPqgFDtvvgekgilL 599
Cdd:PRK13634 80 LKP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREmielVGLPEELLARSP--FE---------L 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 600 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 676
Cdd:PRK13634 147 SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKekGLTTVLVTHSMEDAARyADQIVVMHKGTVFL 226
|
250
....*....|....
gi 9506367 677 HGTHEELLLKPNGL 690
Cdd:PRK13634 227 QGTPREIFADPDEL 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
211-695 |
2.74e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 128.56 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 211 RLRTSLFSSILRQEVAFFDKTR----TGELINRLSSDTALLgRSVTENLSdGLRAgAQASVGVGMMFF-----VSPSLAT 281
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANAL-QQIAEQLH-GLWS-APFRIIVSMVLLyqqlgVASLFGS 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 282 FVLSVVPPISVLAViygRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARA 361
Cdd:PLN03232 448 LILFLLIPLQTLIV---RKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 362 gfFGAAGLSGNLIVLSVLYKGG-LLMGSAHMTVGELSSFLMYAFwVGLSIGGLSSFYSELMKGLGAGGRLWELLERQPRL 440
Cdd:PLN03232 525 --FNSFILNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLFAV-LRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERI 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 441 -----PFNEGMvldektfqGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPNSGT 515
Cdd:PLN03232 602 laqnpPLQPGA--------PAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL-SHAET 672
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 516 VSLDghdirqlnpvwLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSvtaqQVERAAEVANAAEFIRSFPQGFDTVVGEK 595
Cdd:PLN03232 673 SSVV-----------IRGSVAYVPQVSWIFNATVRENILFGSDFESE----RYWRAIDVTALQHDLDLLPGRDLTEIGER 737
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 596 GILLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRLM----EGRTVLIIAHRLSTIKNANFVAVLDH 671
Cdd:PLN03232 738 GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA---HVAHQVFDSCMkdelKGKTRVLVTNQLHFLPLMDRIILVSE 814
|
490 500
....*....|....*....|....
gi 9506367 672 GKICEHGTHEElLLKPNGLYRKLM 695
Cdd:PLN03232 815 GMIKEEGTFAE-LSKSGSLFKKLM 837
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
454-687 |
3.42e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 119.63 E-value: 3.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 454 QGALEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD--PN---SGTVSLDGHDIRQLNP 528
Cdd:PRK14247 1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 VWLRSKIGTVSQEP-VLFSCSVAENIAYGA--DNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEkgilLSGGQKQ 605
Cdd:PRK14247 78 IELRRRVQMVFQIPnPIPNLSIFENVALGLklNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAH------RLStiknaNFVAVLDHGKICEHGT 679
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGP 228
|
....*...
gi 9506367 680 HEELLLKP 687
Cdd:PRK14247 229 TREVFTNP 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
479-687 |
3.88e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 119.50 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN-----SGTVSLDGHDI--RQLNPVWLRSKIGTVSQEPVLFSCSVAE 551
Cdd:PRK14239 25 SLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIAYG----ADNLSSVTAQQVERAAEVANAAEFIRSfpQGFDTVVGekgilLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:PRK14239 105 NVVYGlrlkGIKDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTS 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 628 ALDAENEHLVQEALDRLMEGRTVLIIAH------RLSTiKNANFVAvldhGKICEHGTHEELLLKP 687
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRsmqqasRISD-RTGFFLD----GDLIEYNDTKQMFMNP 238
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
476-682 |
6.28e-30 |
|
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: 118.99 E-value: 6.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvWLRSKIGtVS---QEPVLF-SCSVAE 551
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLG-IArtfQNPRLFpELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIAYGA---------DNLSSVTAQQVERAAEVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLL 622
Cdd:COG0411 99 NVLVAAharlgrgllAALLRLPRARREEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 623 DEATSALdaeNEHLVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 682
Cdd:COG0411 177 DEPAAGL---NPEETEELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
136-417 |
6.53e-30 |
|
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: 119.95 E-value: 6.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIytNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLV--TIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGVG-MMFFVSPSLATFVLSVVPPISVLA 294
Cdd:cd18778 79 LYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTL-VGVAiILFSINPKLALLTLIPIPFLALGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 295 VIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLI 374
Cdd:cd18778 158 WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 9506367 375 VLSVLYKGGLLMGSAHMTVGELSSFLMYafwvglsiggLSSFY 417
Cdd:cd18778 238 TVLVLGFGGRLVLAGELTIGDLVAFLLY----------LGLFY 270
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
457-655 |
7.17e-30 |
|
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: 117.19 E-value: 7.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQlNPVWLR 532
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRD-AREDYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEPVLF-SCSVAENIAYGADNL-SSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIA 610
Cdd:COG4133 75 RRLAYLGHADGLKpELTVRENLRFWAALYgLRADREAIDEALEAVGLAGLA-------DLPVRQ----LSAGQKRRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLVQEALDR-LMEGRTVLIIAH 655
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
456-684 |
1.06e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.34 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLRL----YDPNSGTVSLDGHDIRQLNPvWL 531
Cdd:PRK13548 2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKST----LLRAlsgeLSPDSGEVRLNGRPLADWSP-AE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKI-GTVSQEPVL-FSCSVAENIAYGADNLSSVTAQQ---VERAAEVANAAEFI-RSFPQgfdtvvgekgilLSGGQKQ 605
Cdd:PRK13548 74 LARRrAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDdalVAAALAQVDLAHLAgRDYPQ------------LSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALL------KNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLstikN-----ANFVAVLDHG 672
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDL----NlaaryADRIVLLHQG 217
|
250
....*....|..
gi 9506367 673 KICEHGTHEELL 684
Cdd:PRK13548 218 RLVADGTPAEVL 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
457-695 |
1.09e-29 |
|
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: 124.03 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPAR--------PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLyDPNSGTVSLDGHDI----- 523
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglsr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 524 RQLNPvwLRSKIGTVSQEPvlFSC-----SVAENIAYG----ADNLSSvtAQQVERAA----EVANAAEFIRSFPQGFdt 590
Cdd:COG4172 355 RALRP--LRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSA--AERRARVAealeEVGLDPAARHRYPHEF-- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 591 vvgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDAenehLVQ-EALDRLME-----GRTVLIIAHRLSTIKN-A 663
Cdd:COG4172 427 ---------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQaQILDLLRDlqrehGLAYLFISHDLAVVRAlA 493
|
250 260 270
....*....|....*....|....*....|...
gi 9506367 664 NFVAVLDHGKICEHGTHEELLLKPNGLY-RKLM 695
Cdd:COG4172 494 HRVMVMKDGKVVEQGPTEQVFDAPQHPYtRALL 526
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
136-402 |
1.22e-29 |
|
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: 119.13 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDviyTNPSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGID---SGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTallgrsvtENLSDGLRAG-AQASVGVGMMFFVS-------PSLATFVLSVV 287
Cdd:cd18546 78 VFAHLQRLSLDFHERETSGRIMTRMTSDI--------DALSELLQTGlVQLVVSLLTLVGIAvvllvldPRLALVALAAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 288 PPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAA 367
Cdd:cd18546 150 PPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGV 229
|
250 260 270
....*....|....*....|....*....|....*
gi 9506367 368 GLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 402
Cdd:cd18546 230 ELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
456-688 |
1.23e-29 |
|
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: 117.83 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwLRSKI 535
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFS-CSVAENIAYGAdnlssvtaqQVERAAEVANAAEfIRSFPQGFDTVVGEKGIL------LSGGQKQRIA 608
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGL---------RVKPRSERPPEAE-IRAKVHELLKLVQLDWLAdrypaqLSGGQRQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 609 IARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLL 685
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
...
gi 9506367 686 KPN 688
Cdd:cd03296 227 HPA 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
450-691 |
1.32e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 121.10 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 450 EKTFQGALEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPv 529
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 530 wLRSKIGTVSQEPVLFS-CSVAENIAYG--ADNLSSV-TAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 605
Cdd:PRK11607 89 -YQRPINMMFQSYALFPhMTVEQNIAFGlkQDKLPKAeIASRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALLKNPKILLLDEATSALDAE----NEHLVQEALDRLmeGRTVLIIAH-RLSTIKNANFVAVLDHGKICEHGTH 680
Cdd:PRK11607 157 RVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
250
....*....|.
gi 9506367 681 EELLLKPNGLY 691
Cdd:PRK11607 235 EEIYEHPTTRY 245
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
456-684 |
1.34e-29 |
|
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: 117.88 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSG-TVSLDGHDIRQLNPVWLRSK 534
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVS---QEPVLFSCSVAENIAYGA-DNL---SSVTAQQVERAAEVA---NAAEFI-RSFPQgfdtvvgekgilLSGGQ 603
Cdd:COG1119 80 IGLVSpalQLRFPRDETVLDVVLSGFfDSIglyREPTDEQRERARELLellGLAHLAdRPFGT------------LSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 604 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKNA-NFVAVLDHGKICEHGTH 680
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227
|
....
gi 9506367 681 EELL 684
Cdd:COG1119 228 EEVL 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
456-708 |
1.74e-29 |
|
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: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYpARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDpnsgtvSLDGHdirqlnpVWLRSKI 535
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFSCSVAENIAYGAdNLSSVTAQQVERAAEVANAAEFIrsfPQGFDTVVGEKGILLSGGQKQRIAIARALLK 615
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENILFGK-ALNEKYYQQVLEACALLPDLEIL---PSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 616 NPKILLLDEATSALDAE-NEHLVQEAL--DRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKpNGLYR 692
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR-DGAFA 856
|
250
....*....|....*.
gi 9506367 693 KLMNkqsflSYNGAEQ 708
Cdd:TIGR00957 857 EFLR-----TYAPDEQ 867
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
456-681 |
1.96e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 117.04 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI---RQLNP---V 529
Cdd:COG4161 2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEkaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 530 WLRSKIGTVSQE----PVLfscSVAEN-IAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQgfdtvvgekgiLLSG 601
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENlIEAPCKVLGLSKEQAREKAMKLLARlrlTDKADRFPL-----------HLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 602 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGT 679
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGD 224
|
..
gi 9506367 680 HE 681
Cdd:COG4161 225 AS 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
476-657 |
2.70e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 117.58 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYD--PN---SGTVSLDGHDI--RQLNPVWLRSKIGTVSQEPVLFSCS 548
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 549 VAENIAYGAD------NLSSVTAQQVERAA---EVANAaefirsfpqgfdtvVGEKGILLSGGQKQRIAIARALLKNPKI 619
Cdd:PRK14243 107 IYDNIAYGARingykgDMDELVERSLRQAAlwdEVKDK--------------LKQSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 9506367 620 LLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRL 657
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
136-419 |
3.36e-29 |
|
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: 117.97 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGygdSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRS---ALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSvtenLSDGLRA---GAQASVGVGMMFFVSPSLATFVLSVVPPISV 292
Cdd:cd18543 78 LFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRF----LAFGPFLlgnLLTLVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 293 LAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGN 372
Cdd:cd18543 154 VARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPE 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 9506367 373 LIVLSVLYKGGLLMGSAHMTVGELSSFLMYAF---WVGLSIGGLSSFYSE 419
Cdd:cd18543 234 LGLAAVLALGGWLVANGSLTLGTLVAFSAYLTmlvWPVRMLGWLLAMAQR 283
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
457-674 |
3.63e-29 |
|
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: 113.68 E-value: 3.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLRSKI 535
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQepvlfscsvaeniaygadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARALLK 615
Cdd:cd03216 78 AMVYQ----------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 616 NPKILLLDEATSAL-DAENEHLVqEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKI 674
Cdd:cd03216 100 NARLLILDEPTAALtPAEVERLF-KVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
477-658 |
5.63e-29 |
|
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: 115.08 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIP---SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDG---HDIRQ---LNPVwlRSKIGTVSQEPVLFS- 546
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQ--QRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 547 CSVAENIAYGADNLS-SVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEA 625
Cdd:cd03297 90 LNVRENLAFGLKRKRnREDRISVDELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190
....*....|....*....|....*....|....*
gi 9506367 626 TSALDAENEHLVQEALDRLME--GRTVLIIAHRLS 658
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLS 193
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
457-683 |
5.77e-29 |
|
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: 114.91 E-value: 5.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIG 536
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFS-CSVAENIAYGAdNLSSVTAQQVEraAEVANAAEFIRSFPQGfDTVVGEkgilLSGGQKQRIAIARALLK 615
Cdd:cd03263 79 YCPQFDALFDeLTVREHLRFYA-RLKGLPKSEIK--EEVELLLRVLGLTDKA-NKRART----LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 683
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
457-691 |
6.51e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 119.28 E-value: 6.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIG 536
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFS-CSVAENIAYGAdNLSSVTAQQVERaaEVANAAEFIRsfpqgFDTVVGEKGILLSGGQKQRIAIARALLK 615
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGL-RMQKTPAAEITP--RVMEALRMVQ-----LEEFAQRKPHQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH-RLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLY 691
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLF 240
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
456-679 |
6.57e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 116.77 E-value: 6.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPA-RP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQLN 527
Cdd:PRK13649 2 GINLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 528 PVwlRSKIGTVSQ--EPVLFSCSVAENIAYGADN--LSSVTAQQV--ERAAEVANAAEFIRSFPqgFDtvvgekgilLSG 601
Cdd:PRK13649 82 QI--RKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALarEKLALVGISESLFEKNP--FE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 602 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGT 679
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
456-673 |
7.29e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.29 E-value: 7.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSK 534
Cdd:COG3845 5 ALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLF-SCSVAENIAYGADNLSSVtaqQVERAAEVANAAEFIRSFpqGF----DTVVGEkgilLSGGQKQRIAI 609
Cdd:COG3845 82 IGMVHQHFMLVpNLTVAENIVLGLEPTKGG---RLDRKAARARIRELSERY--GLdvdpDAKVED----LSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 610 ARALLKNPKILLLDEATSAL-DAENEHLVqEALDRLM-EGRTVLIIAHRLSTIK-NANFVAVLDHGK 673
Cdd:COG3845 153 LKALYRGARILILDEPTAVLtPQEADELF-EILRRLAaEGKSIIFITHKLREVMaIADRVTVLRRGK 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
456-690 |
8.58e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.47 E-value: 8.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTY-PARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR----QLNPV 529
Cdd:PRK13641 2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 530 WLRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSsVTAQQVERAAevanaAEFIRSFpqGFDTVVGEKGIL-LSGGQKQR 606
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFG-FSEDEAKEKA-----LKWLKKV--GLSEDLISKSPFeLSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAENEH-LVQEALDRLMEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIF 233
|
....*.
gi 9506367 685 LKPNGL 690
Cdd:PRK13641 234 SDKEWL 239
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
470-672 |
1.21e-28 |
|
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: 114.35 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 470 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--------RLYDPNSGTVSLDGHDIRQLNpvwlRSKIGTVSQE 541
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILgemqtlegKVHWSNKNESEPSFEATRSRN----RYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 542 PVLFSCSVAENIAYGadnlSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILL 621
Cdd:cd03290 88 PWLLNATVEENITFG----SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9506367 622 LDEATSALDAE-NEHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAVLDHG 672
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
474-678 |
1.22e-28 |
|
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: 113.85 E-value: 1.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWlrSKIGTVSQEPVLF-SCSVAEN 552
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTAREN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 553 IAYGAdNLSSVTAQQVERAAEVAnaaefirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 632
Cdd:cd03268 93 LRLLA-RLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9506367 633 NEHLVQEALDRLM-EGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHG 678
Cdd:cd03268 161 GIKELRELILSLRdQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
457-674 |
1.47e-28 |
|
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: 113.89 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIG 536
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLF-SCSVAENIAYGadnLSSVTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLK 615
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFG---LKLRKVPKDEIDERVREVAELL-----QIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH-RLSTIKNANFVAVLDHGKI 674
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
138-404 |
1.68e-28 |
|
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: 115.96 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 138 AAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYgdsLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLF 217
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSY---ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 218 SSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIY 297
Cdd:cd18548 80 EKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 298 GRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLS 377
Cdd:cd18548 160 MKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVA 239
|
250 260
....*....|....*....|....*..
gi 9506367 378 VLYKGGLLMGSAHMTVGELSSFLMYAF 404
Cdd:cd18548 240 ILWFGGHLINAGSLQVGDLVAFINYLM 266
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
477-678 |
1.79e-28 |
|
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: 113.36 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTVSQEPVLFS-CSVAENIAY 555
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 556 GAD---NLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 632
Cdd:cd03298 94 GLSpglKLTAEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 633 nehLVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 678
Cdd:cd03298 163 ---LRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
457-690 |
2.00e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 115.21 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpVW-LRSKI 535
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN-VWdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERaaeVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARAL 613
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKER---VNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 614 LKNPKILLLDEATSALDAENE-HLVQEALD-RLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGL 690
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRlELIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDL 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
477-684 |
2.11e-28 |
|
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: 117.12 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGSVTALVGPSGSGKSTVVSL---LLRlydPNSGTVSLDGH-----DIRQLNPVWLRSkIGTVSQEPVLFS-C 547
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdsARGIFLPPHRRR-IGYVFQEARLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 548 SVAENIAYGAdnlssvtaqqvERAAEVANAAEFirsfpqgfDTVVGEKGI---------LLSGGQKQRIAIARALLKNPK 618
Cdd:COG4148 93 SVRGNLLYGR-----------KRAPRAERRISF--------DEVVELLGIghlldrrpaTLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 619 ILLLDEATSALDAENEHLVQEALDRLmegRT-----VLIIAH------RLstiknANFVAVLDHGKICEHGTHEELL 684
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERL---RDeldipILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
456-681 |
3.09e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 113.57 E-value: 3.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH-----------DIR 524
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 525 QLnpvwlRSKIGTVSQE----PVLfscSVAENIAYGADNLSSVTAQQ-VERAAEVANA---AEFIRSFPQGfdtvvgekg 596
Cdd:PRK11124 79 EL-----RRNVGMVFQQynlwPHL---TVQQNLIEAPCRVLGLSKDQaLARAEKLLERlrlKPYADRFPLH--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 597 ilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTI-KNANFVAVLDHGKI 674
Cdd:PRK11124 142 --LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVYMENGHI 219
|
....*..
gi 9506367 675 CEHGTHE 681
Cdd:PRK11124 220 VEQGDAS 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
473-687 |
3.11e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 114.37 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 473 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRL---YDPN---SGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFS 546
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 547 -CSVAENIAYGADNLSSVTAQQVERAAEvanaaEFIRS---FPQGFDTVvGEKGILLSGGQKQRIAIARALLKNPKILLL 622
Cdd:PRK14246 104 hLSIYDNIAYPLKSHGIKEKREIKKIVE-----ECLRKvglWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 623 DEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
473-684 |
4.95e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 473 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVL-FSCSVAE 551
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIAYGAD-------NLSSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDE 624
Cdd:PRK11231 96 LVAYGRSpwlslwgRLSAEDNARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 625 ATSALDAenEHLVQeaLDRLM-----EGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK11231 165 PTTYLDI--NHQVE--LMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
457-690 |
7.02e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.64 E-value: 7.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVS---VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW-LR 532
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRI 607
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLgipPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEEL-- 683
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIfk 233
|
250
....*....|
gi 9506367 684 ---LLKPNGL 690
Cdd:PRK13633 234 eveMMKKIGL 243
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
123-402 |
9.57e-28 |
|
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: 113.70 E-value: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 123 WKLLGLVrpergrLSAAVgflaVSSVITMSAPFFLGRIIDVIYTNPSegyGDSLTRLCAVLTCVFLCGAAANGIRVYLMQ 202
Cdd:cd18549 1 KKLFFLD------LFCAV----LIAALDLVFPLIVRYIIDDLLPSKN---LRLILIIGAILLALYILRTLLNYFVTYWGH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 203 SSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTallgRSVTEnLS-----DGLRAGAQASVGVGMMFFVSP 277
Cdd:cd18549 68 VMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDL----FDISE-LAhhgpeDLFISIITIIGSFIILLTINV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 278 SLATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTgRVDQLLQLAQKEA 357
Cdd:cd18549 143 PLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFD-EGNDRFLESKKKA 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 9506367 358 L-ARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 402
Cdd:cd18549 222 YkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLY 267
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
474-691 |
1.06e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.20 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnpvwlRS----KIGTVSQEPVLFS-CS 548
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSiqqrDICMVFQSYALFPhMS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 549 VAENIAYGADNL---SSVTAQQVERAAEVANAAefirsfpqGF-DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDE 624
Cdd:PRK11432 95 LGENVGYGLKMLgvpKEERKQRVKEALELVDLA--------GFeDRYVDQ----ISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 625 ATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKPNGLY 691
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
456-655 |
1.51e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 112.26 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPA-RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnPVWLRsk 534
Cdd:COG4525 3 MLTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 iGTVSQEPVLFS-CSVAENIAYGadnlssVTAQQVERAAEVANAAEFIRSFP-QGFdtvvGEKGIL-LSGGQKQRIAIAR 611
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFG------LRLRGVPKAERRARAEELLALVGlADF----ARRRIWqLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAH 655
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
457-659 |
1.53e-27 |
|
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: 110.33 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVSVFQ---DFSLSIPSGSVTALVGPSGSGKSTVVSLL--LRLYDPNSGTVSLDGHDIRqlnPVWL 531
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKQllkNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQEPVLFSC-SVAENIAYGAdNLSSvtaqqveraaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIA 610
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMFAA-KLRG------------------------------------LSGGERKRVSIA 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLST 659
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTIICSIHQPSS 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
457-674 |
1.57e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFT-YPARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK 534
Cdd:COG1101 2 LELKNLSKTfNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 -IGTVSQEPVLFSC---SVAEN--IAYG---ADNLS-SVTAQQVERAAEvanaaeFIRSFPQGF----DTVVGekgiLLS 600
Cdd:COG1101 81 yIGRVFQDPMMGTApsmTIEENlaLAYRrgkRRGLRrGLTKKRRELFRE------LLATLGLGLenrlDTKVG----LLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 601 GGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLS-TIKNANFVAVLDHGKI 674
Cdd:COG1101 151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
474-687 |
2.00e-27 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.41 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlRS-KIGTVSQEPVLFS-CSVAE 551
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKVGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIAYGADNL-------SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDE 624
Cdd:PRK10851 94 NIAFGLTVLprrerpnAAAIKAKVTQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 625 ATSALDAENEHLVQEALDRLMEG---RTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEElkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
457-684 |
3.41e-27 |
|
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: 110.46 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK-- 534
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLF-SCSVAENI---AYGADNLSSVtAQQVERAAEVanaaefirsFPqgfdtVVGE----KGILLSGGQKQR 606
Cdd:COG0410 80 IGYVPEGRRIFpSLTVEENLllgAYARRDRAEV-RADLERVYEL---------FP-----RLKErrrqRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 607 IAIARALLKNPKILLLDEATSALdAENehLVQE---ALDRLM-EGRTVLII---AHRLSTIknANFVAVLDHGKICEHGT 679
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGL-APL--IVEEifeIIRRLNrEGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGT 219
|
....*
gi 9506367 680 HEELL 684
Cdd:COG0410 220 AAELL 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
457-676 |
1.02e-26 |
|
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: 109.89 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYP------ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVW 530
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 ---LRSKIGTVSQE---PVLFSCSVAENIAYGADNLSSVT-AQQVERAAEVANA----AEFIRSFPQGFdtvvgekgill 599
Cdd:TIGR02769 83 rraFRRDVQLVFQDspsAVNPRMTVRQIIGEPLRHLTSLDeSEQKARIAELLDMvglrSEDADKLPRQL----------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 600 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 676
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
474-687 |
1.11e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.45 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV--------WLRSKIGTVSQEPVLF 545
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 SC-SVAENIAYGadnlsSVTAQQVERAAEVANAAEFI---------RSFPQgfdtvvgekgiLLSGGQKQRIAIARALLK 615
Cdd:PRK11264 98 PHrTVLENIIEG-----PVIVKGEPKEEATARARELLakvglagkeTSYPR-----------RLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 616 NPKILLLDEATSALDAEnehLVQEALDRLM----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:PRK11264 162 RPEVILFDEPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
457-683 |
1.73e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.40 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL--RSK 534
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEP--VLFSCSVAENIAYGADNLSsVTAQQVERAAEVANAAEFIrsfpQGFDTVVGEKgilLSGGQKQRIAIARA 612
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLG-LSKEEVEKRVKEALKAVGM----EGFENKPPHH---LSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 613 LLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 683
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
457-632 |
1.90e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.57 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPvwLRS 533
Cdd:COG4136 2 LSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEPVLFS-CSVAENIAYGADNLSSVTA--QQVERAAEVANAAEFIRSFPqgfDTvvgekgilLSGGQKQRIAIA 610
Cdd:COG4136 77 RIGILFQDDLLFPhLSVGENLAFALPPTIGRAQrrARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVALL 145
|
170 180
....*....|....*....|..
gi 9506367 611 RALLKNPKILLLDEATSALDAE 632
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLDAA 167
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
458-684 |
2.29e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 108.63 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGT 537
Cdd:COG4604 3 EIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 538 VSQEPVLFS-CSVAENIAYG-----ADNLSSVTAQQVERAAEVANAAEFIRSFpqgFDTvvgekgilLSGGQKQRIAIAR 611
Cdd:COG4604 80 LRQENHINSrLTVRELVAFGrfpysKGRLTAEDREIIDEAIAYLDLEDLADRY---LDE--------LSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 612 ALLKNPKILLLDEATSALDAenEHLVQ--EALDRLME--GRTVLIIAHRLstiknaNFVAVL-DH------GKICEHGTH 680
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDM--KHSVQmmKLLRRLADelGKTVVIVLHDI------NFASCYaDHivamkdGRVVAQGTP 220
|
....
gi 9506367 681 EELL 684
Cdd:COG4604 221 EEII 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
457-684 |
3.74e-26 |
|
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: 107.24 E-value: 3.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK-- 534
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAEVAnaAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARAL 613
Cdd:cd03218 77 IGYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEELL--EEF------HITHLRKSKASSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
429-697 |
3.86e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 115.22 E-value: 3.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 429 RLWELL---ER--QPRLPFNEGmvldektfQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVS 503
Cdd:PLN03130 590 RLEELLlaeERvlLPNPPLEPG--------LPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 504 LLLRLYDPNSGTVsldghdirqlnpVWLRSKIGTVSQEPVLFSCSVAENIAYGADnlssVTAQQVERAAEVANAAEFIRS 583
Cdd:PLN03130 662 AMLGELPPRSDAS------------VVIRGTVAYVPQVSWIFNATVRDNILFGSP----FDPERYERAIDVTALQHDLDL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 584 FPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRL----MEGRTVLIIAHRLST 659
Cdd:PLN03130 726 LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGRQVFDKCikdeLRGKTRVLVTNQLHF 802
|
250 260 270
....*....|....*....|....*....|....*....
gi 9506367 660 IKNANFVAVLDHGKICEHGTHEELLlkPNG-LYRKLMNK 697
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEEGTYEELS--NNGpLFQKLMEN 839
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
472-683 |
5.20e-26 |
|
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: 106.69 E-value: 5.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 472 VSVFQDF------SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIGTVSQEPVLf 545
Cdd:cd03265 7 VKKYGDFeavrgvSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 scsvaENIAYGADNL----------SSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLK 615
Cdd:cd03265 85 -----DDELTGWENLyiharlygvpGAERRERIDELLDFVGLLEAA-------DRLVKT----YSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 683
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
471-687 |
7.83e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 108.78 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 471 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLD----GHDIRQLNPVW------------LRSK 534
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSF----PQGfdtvvgekgilLSGGQKQRIA 608
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYlersPFG-----------LSGGQKRRVA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 609 IARALLKNPKILLLDEATSALDAENEH-LVQEALDRLMEGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEELLLK 686
Cdd:PRK13631 187 IAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTD 266
|
.
gi 9506367 687 P 687
Cdd:PRK13631 267 Q 267
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
457-692 |
1.32e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.20 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIAR 611
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLgldEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 688
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
....
gi 9506367 689 GLYR 692
Cdd:PRK13652 231 LLAR 234
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
136-403 |
1.53e-25 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 107.65 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGY------------GDSLTRLCAVLTCVFLCGAAANGIRVYLMQS 203
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEASFLplvpaslgpadpRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 204 SGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFV 283
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 284 LSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQlAQKEAL-ARAG 362
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRD-ANWRAIrLRAA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 9506367 363 FFGAAGLSGNLIVLSVLYKGGLL------MGSAHMTVGELSSFLMYA 403
Cdd:cd18565 240 FFPVIRLVAGAGFVATFVVGGYWvldgppLFTGTLTVGTLVTFLFYT 286
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
457-686 |
2.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 2.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVsvFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH--DIRQLNPVWLRSK 534
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEvANAAEFIRSFPQGFdtvvgekgilLSGGQKQRIAI 609
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLklpEDEVRKRVDNALK-RTGIEHLKDKPTHC----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 610 ARALLKNPKILLLDEATSALD----AENEHLVQEALDRLmeGRTVLIIAHRLSTIK-NANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
..
gi 9506367 685 LK 686
Cdd:PRK13636 231 AE 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
457-684 |
2.48e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.11 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK-- 534
Cdd:COG1137 4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLF-SCSVAENIAYGADNLSSVTAQQVERAAEVAnaAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARAL 613
Cdd:COG1137 80 IGYLPQEASIFrKLTVEDNILAVLELRKLSKKEREERLEELL--EEF------GITHLRKSKAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 614 LKNPKILLLDEATSALD----AENEHLVQEALDRlmeGRTVLIIAHR----LSTIKNAnfvAVLDHGKICEHGTHEELL 684
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GIGVLITDHNvretLGICDRA---YIISEGKVLAEGTPEEIL 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
456-687 |
2.78e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 105.89 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNS-----GTVSLDGHDI--RQLNP 528
Cdd:PRK14258 7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 VWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSVTAQQVERAAEVA-NAAEFirsfpqgFDTV---VGEKGILLSGGQK 604
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESAlKDADL-------WDEIkhkIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 605 QRIAIARALLKNPKILLLDEATSALDA----ENEHLVQEAldRLMEGRTVLIIAHRLSTIKN-ANFVAVLDH-----GKI 674
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQL 234
|
250
....*....|...
gi 9506367 675 CEHGTHEELLLKP 687
Cdd:PRK14258 235 VEFGLTKKIFNSP 247
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
456-687 |
3.17e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 3.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN-----SGTVSLDGHDI--RQLNP 528
Cdd:PRK14267 4 AIETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 VWLRSKIGTVSQEPVLFS-CSVAENIAYGA---------DNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgil 598
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPhLTIYDNVAIGVklnglvkskKELDERVEWALKKAALWDEVKDRLNDYPSN----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHR-LSTIKNANFVAVLDHGKICEH 677
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEV 229
|
250
....*....|
gi 9506367 678 GTHEELLLKP 687
Cdd:PRK14267 230 GPTRKVFENP 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
125-655 |
4.17e-25 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 110.27 E-value: 4.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 125 LLGLVRPERGRLSAAVGFLAVSSVITMsapFFLGRIIDVIytnpsEGYGDSLTRL----CAVLTCVFLCGAAANGIRVYL 200
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANA---GLIALINQAL-----NATGAALARLlllfAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 201 mqssGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVtENLSDGLRAGAQASVGVGMMFFVSPSLA 280
Cdd:COG4615 76 ----GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 281 TFVLSVVppisVLAVIYGRYL-----RKLSKA--TQDSLAEATQ-----LAEERIGNIRTIRAFGKEMTE----VEKYTG 344
Cdd:COG4615 151 LLTLVLL----GLGVAGYRLLvrrarRHLRRAreAEDRLFKHFRallegFKELKLNRRRRRAFFDEDLQPtaerYRDLRI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 345 RVDqllqlaqkealaraGFFGAAGLSGNLIVLSVLykGGLLMGSAHMTVGELSSFLMYA----FWVGlSIGGLSSFYSEL 420
Cdd:COG4615 227 RAD--------------TIFALANNWGNLLFFALI--GLILFLLPALGWADPAVLSGFVlvllFLRG-PLSQLVGALPTL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 421 MKGLGAGGRLWEL---LERQPRLPFNEGMVLDEKTFQgALEFRNVHFTYPARPEVSVFQ--DFSLSIPSGSVTALVGPSG 495
Cdd:COG4615 290 SRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 496 SGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFscsvaeniaygaDNLssvtaQQVERAAEVA 575
Cdd:COG4615 369 SGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF------------DRL-----LGLDGEADPA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 576 NAAEFIRSFpqGFDTVVG-EKGIL----LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLV-QEALDRLME-GR 648
Cdd:COG4615 432 RARELLERL--ELDHKVSvEDGRFsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFyTELLPELKArGK 509
|
....*..
gi 9506367 649 TVLIIAH 655
Cdd:COG4615 510 TVIAISH 516
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
476-691 |
4.59e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.20 E-value: 4.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS----KIGTVSQEPVLFS-CSVA 550
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENIAYGADnLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALD 630
Cdd:PRK10070 125 DNTAFGME-LAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506367 631 AENEHLVQEALDRLM--EGRTVLIIAHRL-STIKNANFVAVLDHGKICEHGTHEELLLKPNGLY 691
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
466-694 |
5.01e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.79 E-value: 5.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 466 YPARPEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdirqlnpvWLRSKIGTVSQEPVLF 545
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 SCSVAENIAYGADnlssvtaqqvERAAEVANAAEF------IRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKI 619
Cdd:PTZ00243 734 NATVRGNILFFDE----------EDAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDV 803
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 620 LLLDEATSALDAE-NEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPngLYRKL 694
Cdd:PTZ00243 804 YLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATL 877
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
457-678 |
6.32e-25 |
|
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: 103.60 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTY-PARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKI 535
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFS-CSVAENIAYGADnLSSVTAQQ----VERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIA 610
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYFAG-LYGLKGDEltarLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 678
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
461-682 |
6.38e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.51 E-value: 6.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 461 NVHFTY-PARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI--RQLNPVWLRSKIG 536
Cdd:PRK13637 7 NLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARALL 614
Cdd:PRK13637 87 LVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGL------DYEDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 615 KNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEE 682
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
456-655 |
6.53e-25 |
|
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: 103.67 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLN----PVW 530
Cdd:COG4181 8 IIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 LRSKIGTVSQ-EPVLFSCSVAENIAY-----GADNlssvtAQQveRAAEVANA---AEFIRSFPQGfdtvvgekgilLSG 601
Cdd:COG4181 88 RARHVGFVFQsFQLLPTLTALENVMLplelaGRRD-----ARA--RARALLERvglGHRLDHYPAQ-----------LSG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 602 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH 655
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTH 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
457-684 |
7.29e-25 |
|
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: 102.61 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFtypARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRL--YDPNSGTVSLDGHDIRQLnPVWLRSK 534
Cdd:cd03217 1 LEIKDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL-PPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IG-TVS-QEPVLFScsvaeniaygadnlssvtaqqveraaEVANAaEFIRSFPQGFdtvvgekgillSGGQKQRIAIARA 612
Cdd:cd03217 77 LGiFLAfQYPPEIP--------------------------GVKNA-DFLRYVNEGF-----------SGGEKKRNEILQL 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 613 LLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH--RLSTIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
457-684 |
1.03e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.40 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpVW-LRSKI 535
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIrsfpqGFDTvvgEKGILLSGGQKQRIAIARAL 613
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKT---REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 614 LKNPKILLLDEATSALD----AENEHLVQEALDRLMegRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK13642 156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
457-684 |
1.33e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.43 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTY-PARPEVS-VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghDI--------RQL 526
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFASrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstskqKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 527 NPVwlRSKIGTVSQEP--VLFSCSVAENIAYGADNLsSVTAQQVERAAevANAAEFIrsfpqGFDTVVGEKGIL-LSGGQ 603
Cdd:PRK13643 80 KPV--RKKVGVVFQFPesQLFEETVLKDVAFGPQNF-GIPKEKAEKIA--AEKLEMV-----GLADEFWEKSPFeLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 604 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHE 681
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPS 229
|
...
gi 9506367 682 ELL 684
Cdd:PRK13643 230 DVF 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
457-683 |
1.50e-24 |
|
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: 102.60 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL-RSKI 535
Cdd:TIGR03410 1 LEVSNLNVYYGQSH---ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVanaaefirsFPQGFDtVVGEKGILLSGGQKQRIAIARALL 614
Cdd:TIGR03410 78 AYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYEL---------FPVLKE-MLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 615 KNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 683
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
477-688 |
1.56e-24 |
|
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: 105.58 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDG---HDIRQ---LNPVwlRSKIGTVSQEPVLFS-CSV 549
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPE--KRRIGYVFQEARLFPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 550 AENIAYGadnLSSVTAQQVEraaevANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSAL 629
Cdd:TIGR02142 93 RGNLRYG---MKRARPSERR-----ISFERVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 630 DAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 688
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
457-686 |
2.12e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.45 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHftypARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--RLYDPNSGTVSLDGHDIRQLnPVWLRS 533
Cdd:COG0396 1 LEIKNLH----VSVEgKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILEL-SPDERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 K--IGTVSQEPVLFS-CSVAE--NIAYGADNLSSVTAQQV-----ERAAEVANAAEFI-RSFPQGFdtvvgekgillSGG 602
Cdd:COG0396 76 RagIFLAFQYPVEIPgVSVSNflRTALNARRGEELSAREFlkllkEKMKELGLDEDFLdRYVNEGF-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 603 QKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH--RLSTIKNANFVAVLDHGKICEHGT 679
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*..
gi 9506367 680 hEELLLK 686
Cdd:COG0396 225 -KELALE 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
471-702 |
3.01e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 102.74 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 471 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR-------QLNPV------WLRSKIGT 537
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVAdknqlrLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 538 VSQEPVLFS-CSVAENIAYGADNLSSVTAQQV-ERAAEVANAAefirsfpqGFD-TVVGEKGILLSGGQKQRIAIARALL 614
Cdd:PRK10619 97 VFQHFNLWShMTVLENVMEAPIQVLGLSKQEArERAVKYLAKV--------GIDeRAQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 615 KNPKILLLDEATSALDAEnehLVQEALdRLM-----EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPn 688
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPE---LVGEVL-RIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP- 243
|
250
....*....|....
gi 9506367 689 glyrKLMNKQSFLS 702
Cdd:PRK10619 244 ----QSPRLQQFLK 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
459-674 |
4.67e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.69 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 459 FRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhDIRqlnpvwlrskIGTV 538
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 539 SQEPVLFS-CSVAENIAYGADNLSSVTAQ-------------QVERAAEV-------------ANAAEFIRS--FPQG-F 588
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAEleeleaklaepdeDLERLAELqeefealggweaeARAEEILSGlgFPEEdL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 589 DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EHLVQEaldrlmEGrTVLIIAH-R--LSTI 660
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY------PG-TVLVVSHdRyfLDRV 215
|
250
....*....|....
gi 9506367 661 knANFVAVLDHGKI 674
Cdd:COG0488 216 --ATRILELDRGKL 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
457-687 |
6.59e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.12 E-value: 6.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPAR-----PE--VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------ 523
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkPErlVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 524 -----RQ------------LNPvwlRSKIGTVSQEPVLFSCsvaeniaygadNLSSvtAQQVERAAE----VANAAEFIR 582
Cdd:PRK11308 86 aqkllRQkiqivfqnpygsLNP---RKKVGQILEEPLLINT-----------SLSA--AERREKALAmmakVGLRPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 583 SFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDAEnehlVQ-EALDRLME-----GRTVLIIAHR 656
Cdd:PRK11308 150 RYPHMF-----------SGGQRQRIAIARALMLDPDVVVADEPVSALDVS----VQaQVLNLMMDlqqelGLSYVFISHD 214
|
250 260 270
....*....|....*....|....*....|..
gi 9506367 657 LSTIKN-ANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:PRK11308 215 LSVVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
456-681 |
7.52e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 102.58 E-value: 7.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKI 535
Cdd:PRK13537 7 PIDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQ----EPvlfSCSVAENI-AYGadNLSSVTAQQVEraAEVANAAEFIRsFPQGFDTVVGEkgilLSGGQKQRIAIA 610
Cdd:PRK13537 83 GVVPQfdnlDP---DFTVRENLlVFG--RYFGLSAAAAR--ALVPPLLEFAK-LENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHG-KICEHGTHE 681
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGrKIAEGAPHA 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
468-676 |
8.25e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 101.69 E-value: 8.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 468 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQL--------------------- 526
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafrrdiqmvfqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 527 --NPvwlRSKIGTVSQEPV--LFSCSVAENIAYGADNLssvtaQQVERAAEVANaaefiRSFPQgfdtvvgekgilLSGG 602
Cdd:PRK10419 101 avNP---RKTVREIIREPLrhLLSLDKAERLARASEML-----RAVDLDDSVLD-----KRPPQ------------LSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 603 QKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRLME-----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 676
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDL---VLQAGVIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
429-656 |
1.03e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.04 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 429 RLWEL---LERQPRLPFNEGMVLDEKtfQGALEFRNVHFTYPA-RPevsVFQDFSLSIPSGSVTALVGPSGSGKSTvvsl 504
Cdd:COG4178 334 RLAGFeeaLEAADALPEAASRIETSE--DGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKST---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 505 LLR----LYDPNSGTVSL-DGHDIrqlnpVWLrskigtvSQEPVLFSCSVAENIAYGADNlSSVTAQQVERAAEVANAAE 579
Cdd:COG4178 405 LLRaiagLWPYGSGRIARpAGARV-----LFL-------PQRPYLPLGTLREALLYPATA-EAFSDAELREALEAVGLGH 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 580 FIrsfpQGFDTVVgEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHR 656
Cdd:COG4178 472 LA----ERLDEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
457-696 |
1.10e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.54 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRN--VHFTYPARpEVSVFQDFSLSIPSGSVTALVGPSGSGKStVVSL-LLRLYDPN----SGTVSLDGHDIRQLNPV 529
Cdd:COG4172 7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKS-VTALsILRLLPDPaahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 530 WLR----SKIGTVSQEPV-----LFSCS--VAENIAYGAdNLSSVTAQQveRAAE------VANAAEFIRSFP-Qgfdtv 591
Cdd:COG4172 85 ELRrirgNRIAMIFQEPMtslnpLHTIGkqIAEVLRLHR-GLSGAAARA--RALEllervgIPDPERRLDAYPhQ----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 592 vgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAenehLVQ-EALDRLME-----GRTVLIIAHRLSTIKN-AN 664
Cdd:COG4172 157 -------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDLLKDlqrelGMALLLITHDLGVVRRfAD 225
|
250 260 270
....*....|....*....|....*....|...
gi 9506367 665 FVAVLDHGKICEHGTHEELLLKPNGLY-RKLMN 696
Cdd:COG4172 226 RVAVMRQGEIVEQGPTAELFAAPQHPYtRKLLA 258
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
473-687 |
1.21e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 101.33 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 473 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDP-----NSGTVSLDGHDIRQLNPVW-LRSKIGTVSQEPVLFS 546
Cdd:PRK14271 35 TVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 547 CSVAENIAYGAdnlssvtaqqveRAAEVANAAEFiRSFPQGFDTVVG----------EKGILLSGGQKQRIAIARALLKN 616
Cdd:PRK14271 115 MSIMDNVLAGV------------RAHKLVPRKEF-RGVAQARLTEVGlwdavkdrlsDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
207-684 |
1.30e-23 |
|
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: 107.30 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 207 SIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAgaqASVGVGMMFFVSpSLATFVLSV 286
Cdd:TIGR01271 955 TVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQL---TLIVLGAIFVVS-VLQPYIFIA 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 287 VPPISVLAVIYGRYLRKLSKATQDSLAEA-TQLAEERIGNIR---TIRAFGKE---------------------MTEVEK 341
Cdd:TIGR01271 1031 AIPVAVIFIMLRAYFLRTSQQLKQLESEArSPIFSHLITSLKglwTIRAFGRQsyfetlfhkalnlhtanwflyLSTLRW 1110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 342 YTGRVDQLLQLaqkealaragFFGAAglsgnlIVLSVLYKG------GLLMGSAHMtvgeLSSFLMYAFWVGLSIGGLSS 415
Cdd:TIGR01271 1111 FQMRIDIIFVF----------FFIAV------TFIAIGTNQdgegevGIILTLAMN----ILSTLQWAVNSSIDVDGLMR 1170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 416 FYSELMKGLGAGGRLWELLERQPRLPFNEGMVLDEKTFQ------GALEFRN--VHFTYPARpevSVFQDFSLSIPSGSV 487
Cdd:TIGR01271 1171 SVSRVFKFIDLPQEEPRPSGGGGKYQLSTVLVIENPHAQkcwpsgGQMDVQGltAKYTEAGR---AVLQDLSFSVEGGQR 1247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 488 TALVGPSGSGKSTVVSLLLRLYDpNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAENIaygaDNLSSVTAQQ 567
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL----DPYEQWSDEE 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 568 VERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEG 647
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN 1402
|
490 500 510
....*....|....*....|....*....|....*..
gi 9506367 648 RTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:TIGR01271 1403 CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
456-683 |
1.79e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.34 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPEVsvfQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpvwlRSKI 535
Cdd:COG4152 1 MLELKGLTKRFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLF-SCSVAENIAYGADnLSSVTAQQVERAA-------EVANAAefirsfpqgfDTVVGEkgilLSGGQKQRI 607
Cdd:COG4152 74 GYLPEERGLYpKMKVGEQLVYLAR-LKGLSKAEAKRRAdewlerlGLGDRA----------NKKVEE----LSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 683
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
456-681 |
3.94e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 3.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlNPV-----W 530
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVVN---GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG------VPVpararL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 LRSKIGTVSQEPVL-FSCSVAEN-IAYGadNLSSVTAQQVEraAEVANAAEFIRsFPQGFDTVVGEkgilLSGGQKQRIA 608
Cdd:PRK13536 112 ARARIGVVPQFDNLdLEFTVRENlLVFG--RYFGMSTREIE--AVIPSLLEFAR-LESKADARVSD----LSGGMKRRLT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 609 IARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHG-KICEHGTHE 681
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHA 258
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
468-655 |
8.36e-23 |
|
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: 97.34 E-value: 8.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 468 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKST---VVSLLLRLYDPNSGTVSLDGhdiRQLNPVWLRSKIGTVSQEPVL 544
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 545 FSC-SVAENIAYGADNLSSVTAQQVERAAEVAnaaefIRSFPQGFDTVVGE---KGIllSGGQKQRIAIARALLKNPKIL 620
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVE-----DVLLRDLALTRIGGnlvKGI--SGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 9506367 621 LLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH 655
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIH 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
457-688 |
1.75e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV---SLDGHDIRQLNPVwlRS 533
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGI--RK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEP--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIA 608
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFGPENLclpPIEIRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQCVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 609 IARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
.
gi 9506367 688 N 688
Cdd:PRK13644 227 S 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
478-684 |
2.15e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 478 FSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTVSQEPVLFS-CSVAENIAYG 556
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 557 AD---NLSSVTAQQVERAAEVANAAEFIRSFPqgfdtvvGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAEn 633
Cdd:PRK10771 96 LNpglKLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPA- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 634 ehLVQEALDRLME-----GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK10771 164 --LRQEMLTLVSQvcqerQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
457-655 |
3.25e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPE-VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---- 531
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANAAefirsfpqGFDTVVGEKGILLSGGQKQRIAIA 610
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLRAQELLQRL--------GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAH 655
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTH 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
457-683 |
4.34e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTY-PARP-EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQLNP 528
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 VwlRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSfpqgfdtVVGEKGILLSGGQKQR 606
Cdd:PRK13646 83 V--RKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRD-------VMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTI-KNANFVAVLDHGKICEHGTHEEL 683
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
459-691 |
5.42e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.56 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 459 FRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwlRSKIGTV 538
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 539 SQEPVLFS-CSVAENIAYG---ADNLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALL 614
Cdd:PRK11000 81 FQSYALYPhLSVAENMSFGlklAGAKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 615 KNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAH-RLSTIKNANFVAVLDHGKICEHGtheelllKPNGLY 691
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG-------KPLELY 222
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
480-682 |
5.97e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.02 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 480 LSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH---DIRQlnPVWL---RSKIGTVSQEPVLFS-CSVAEN 552
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLppeKRRIGYVFQDARLFPhYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 553 IAYGADnlssvtaqqveraaevanaaefiRSFPQGFDTVVGEKGI---------LLSGGQKQRIAIARALLKNPKILLLD 623
Cdd:PRK11144 97 LRYGMA-----------------------KSMVAQFDKIVALLGIeplldrypgSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506367 624 EATSALDAENEHLVQEALDRLmeGRTV----LIIAHRLSTI-KNANFVAVLDHGKICEHGTHEE 682
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERL--AREInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
457-678 |
6.04e-22 |
|
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: 94.65 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpvwlRSKIG 536
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLF-SCSVAENIAYGADnLSSVTAQQveraaevanAAEFIRSFPQGFDTVVGEKGIL--LSGGQKQRIAIARAL 613
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQ-LKGLKKEE---------ARRRIDEWLERLELSEYANKRVeeLSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHG 678
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
471-655 |
6.30e-22 |
|
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: 95.19 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 471 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH----DIRQLNPVWL----RSKIGTVSQ-- 540
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREIlalrRRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 541 -------------EPVLfscsvaeniaygadnlssvtAQQVERAAEVANAAEFIRSF----------PQGFdtvvgekgi 597
Cdd:COG4778 103 rviprvsaldvvaEPLL--------------------ERGVDREEARARARELLARLnlperlwdlpPATF--------- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 598 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH 655
Cdd:COG4778 154 --SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFH 210
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
133-430 |
9.30e-22 |
|
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: 96.36 E-value: 9.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 133 RGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNpseGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRL 212
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPS---GDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 213 RTSLFSSILRQEVAFFDKTRTGELINRLsSDT----ALLGRSVTENLSDGLragaQASVGVGMMFFVSPSLATFVLSVVP 288
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRF-NDAnkirEAISSTTISLFLDLL----MVIISGIILFFYNWKLFLITLLIIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 289 pisVLAVIYGRYLRKLSKATQDSLAEATQLAE---ERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFG 365
Cdd:cd18570 153 ---LYILIILLFNKPFKKKNREVMESNAELNSyliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSS 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 366 AAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFL-MYAFWVGlSIGGLSSFYSELMKGLGAGGRL 430
Cdd:cd18570 230 IKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNaLLGYFLG-PIENLINLQPKIQEAKVAADRL 294
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
456-667 |
1.19e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdIRQLNPVWLRski 535
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQ-EPVLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFirsfpQGFdtvvGEKGIL-LSGGQKQRIAIARAL 613
Cdd:PRK11248 73 GVVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-----EGA----EKRYIWqLSGGQRQRVGIARAL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHrlsTIKNANFVA 667
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH---DIEEAVFMA 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
471-687 |
1.37e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.60 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 471 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVL-FSCSV 549
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 550 AENIAYGA-------DNLSSVTAQQVERAAEVANAAEFIrsfPQGFDTvvgekgilLSGGQKQRIAIARALLKNPKILLL 622
Cdd:PRK09536 95 RQVVEMGRtphrsrfDTWTETDRAAVERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 623 DEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKP 687
Cdd:PRK09536 164 DEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
466-669 |
1.56e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.68 E-value: 1.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 466 YPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdiRQLNPVWLRSKIgtvsqePVLF 545
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSEV------PDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 SCSVAENIAYGA-------DNLSSVTAQQVERAAEVANAAEFIRsfpQGFDTvvgekgilLSGGQKQRIAIARALLKNPK 618
Cdd:NF040873 71 PLTVRDLVAMGRwarrglwRRLTRDDRAAVDDALERVGLADLAG---RQLGE--------LSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 619 ILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFVAVL 669
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
473-684 |
1.67e-21 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 94.92 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 473 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDpNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSCSVAEN 552
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 553 IaygaDNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 632
Cdd:cd03289 97 L----DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 633 NEHLVQEALDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:cd03289 173 TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
457-655 |
1.91e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.60 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLdGHDIrqlnpvwlrsKIG 536
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQEPVLFSC--SVAENIAYGADNLSSVTaqqveraaevanaaefIRSFPQGF-------DTVVGEkgilLSGGQKQRI 607
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRDGAPGGTEQE----------------VRGYLGRFlfsgddaFKPVGV----LSGGEKARL 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9506367 608 AIARALLKNPKILLLDEATSALDAENEHLVQEALDRLmEGrTVLIIAH 655
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSH 487
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
463-700 |
2.11e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.92 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 463 HFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlrsKIGTVSQEP 542
Cdd:cd03291 44 NLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 543 VLFSCSVAENIAYGADN-----LSSVTAQQVEraaevanaaEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNP 617
Cdd:cd03291 108 WIMPGTIKENIIFGVSYdeyryKSVVKACQLE---------EDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 618 KILLLDEATSALDAENEHLVQEA-LDRLMEGRTVLIIAHRLSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMN 696
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMG 258
|
....
gi 9506367 697 KQSF 700
Cdd:cd03291 259 YDTF 262
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
154-703 |
2.67e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 99.60 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 154 PFFLGRIIDVIytNPSEGYGDSLTRLCAVLTCVFLCgaaangIRVYLMQSSG---QSIVNRLRTSLFSSI----LRQEVA 226
Cdd:TIGR01271 100 PLLLGRIIASY--DPFNAPEREIAYYLALGLCLLFI------VRTLLLHPAIfglHHLGMQMRIALFSLIykktLKLSSR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 227 FFDKTRTGELINRLSSDTALLGRSVtenlsdGLR-----AGAQASVGVGMMFfvsPSLATFVLSVVPPISVLAVIYGRYL 301
Cdd:TIGR01271 172 VLDKISTGQLVSLLSNNLNKFDEGL------ALAhfvwiAPLQVILLMGLIW---ELLEVNGFCGLGFLILLALFQACLG 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 302 RKLSKATQD---SLAEATQLAEERIGNIRTIRAFGKEmTEVEKYTGRVDQL-LQLAQKEALARAGFFGAAGLSGNLIVLS 377
Cdd:TIGR01271 243 QKMMPYRDKragKISERLAITSEIIENIQSVKAYCWE-EAMEKIIKNIRQDeLKLTRKIAYLRYFYSSAFFFSGFFVVFL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 378 VLYKGGLLMGSAHMTVGELSSFLMYafwVGLSI-----GGLSSFYSELmkglGAGGRLWELLERQPR--LPFN------- 443
Cdd:TIGR01271 322 SVVPYALIKGIILRRIFTTISYCIV---LRMTVtrqfpGAIQTWYDSL----GAITKIQDFLCKEEYktLEYNlttteve 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 444 ---------EGM-VLDEKTFQ-----------GALEFRNvhFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVV 502
Cdd:TIGR01271 395 mvnvtaswdEGIgELFEKIKQnnkarkqpngdDGLFFSN--FSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLL 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 503 SLLLRLYDPNSGTVSLDGhdirqlnpvwlrsKIGTVSQEPVLFSCSVAENIAYGADN-----LSSVTAQQVEraaevana 577
Cdd:TIGR01271 470 MMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGLSYdeyryTSVIKACQLE-------- 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 578 aEFIRSFPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEA-LDRLMEGRTVLIIAHR 656
Cdd:TIGR01271 529 -EDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSK 607
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 9506367 657 LSTIKNANFVAVLDHGKICEHGTHEELLLKPNGLYRKLMNKQSFLSY 703
Cdd:TIGR01271 608 LEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAFDNF 654
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
451-678 |
3.59e-21 |
|
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: 92.60 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 451 KTFQGALEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlNPVW 530
Cdd:cd03220 14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 LrskIG-TVSQEPVLfscSVAENIA-----YGADNlssvtaqqveraAEVANAAEFIRSF---PQGFDTVVGEkgilLSG 601
Cdd:cd03220 88 L---LGlGGGFNPEL---TGRENIYlngrlLGLSR------------KEIDEKIDEIIEFselGDFIDLPVKT----YSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 602 GQKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRLME----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICE 676
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDA---AFQEKCQRRLREllkqGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222
|
..
gi 9506367 677 HG 678
Cdd:cd03220 223 DG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
456-699 |
4.78e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.84 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYP-------------------ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV 516
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 517 SLDGhdirqlNPVWLrskIG-TVSQEPVLfscSVAENI-----AYGadnlssVTAQQV-ERAAEVANAAEfIRSFpqgFD 589
Cdd:COG1134 84 EVNG------RVSAL---LElGAGFHPEL---TGRENIylngrLLG------LSRKEIdEKFDEIVEFAE-LGDF---ID 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 590 TVVGekgiLLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneHLVQEALDRLME----GRTVLIIAHRLSTIKN-AN 664
Cdd:COG1134 142 QPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA---AFQKKCLARIRElresGRTVIFVSHSMGAVRRlCD 214
|
250 260 270
....*....|....*....|....*....|....*
gi 9506367 665 FVAVLDHGKICEHGTHEELLlkpnGLYRKLMNKQS 699
Cdd:COG1134 215 RAIWLEKGRLVMDGDPEEVI----AAYEALLAGRE 245
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
452-697 |
1.35e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 452 TFQGALEFRNVHFTYPARP--EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH----DIRQ 525
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 526 LNPVW-LRSKIGTVSQEP--VLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFpqgfdtvVGEKGILLSGG 602
Cdd:PRK13645 82 IKEVKrLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY-------VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 603 QKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHGKICEHG- 678
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234
|
250 260
....*....|....*....|....*...
gi 9506367 679 -----THEELLLK----PNGLYrKLMNK 697
Cdd:PRK13645 235 pfeifSNQELLTKieidPPKLY-QLMYK 261
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
457-695 |
1.47e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP--------EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPNSGTVSLDGHDIRQLNP 528
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 ---VWLRSKIGTVSQEPvlFSC-----SVAENIAYGAD-NLSSVTAQQVERA-----AEVANAAEFIRSFPQGFdtvvge 594
Cdd:PRK15134 355 rqlLPVRHRIQVVFQDP--NSSlnprlNVLQIIEEGLRvHQPTLSAAQREQQviavmEEVGLDPETRHRYPAEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 595 kgillSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRTV--LIIAHRLSTIKN-ANFVAVLDH 671
Cdd:PRK15134 427 -----SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQ 501
|
250 260
....*....|....*....|....*
gi 9506367 672 GKICEHGTHEELLLKPNGLY-RKLM 695
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYtRQLL 526
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
457-655 |
1.49e-20 |
|
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: 88.27 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlrskig 536
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 tvsqepvlfscsvAENIAYgadnlssvtaqqveraaevanaaefirsFPQgfdtvvgekgilLSGGQKQRIAIARALLKN 616
Cdd:cd03221 62 -------------TVKIGY----------------------------FEQ------------LSGGEKMRLALAKLLLEN 88
|
170 180 190
....*....|....*....|....*....|....*....
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLmeGRTVLIIAH 655
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
457-707 |
1.61e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.82 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTY------PARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH--------- 521
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyky 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 522 ---DIR---Q-----LNPvwlRSKIGTVSQEPVLFScsvaeniaygadnlSSVTAQqvERAAEVANA----------AEF 580
Cdd:COG4167 85 rckHIRmifQdpntsLNP---RLNIGQILEEPLRLN--------------TDLTAE--EREERIFATlrlvgllpehANF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 581 irsFPQgfdtvvgekgiLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE------NEHL-VQEALdrlmeGRTVLII 653
Cdd:COG4167 146 ---YPH-----------MLSSGQKQRVALARALILQPKIIIADEALAALDMSvrsqiiNLMLeLQEKL-----GISYIYV 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 654 AHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKP-NGLYRKLMNKQsFLSYNGAE 707
Cdd:COG4167 207 SQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANPqHEVTKRLIESH-FGEALTAD 261
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
476-655 |
2.35e-20 |
|
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: 90.60 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLrskigTVSQEPVLFS-CSVAENIA 554
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 555 YGADNLSSvTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 634
Cdd:TIGR01184 77 LAVDRVLP-DLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 9506367 635 HLVQEALDRLME--GRTVLIIAH 655
Cdd:TIGR01184 151 GNLQEELMQIWEehRVTVLMVTH 173
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
473-684 |
2.63e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.20 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 473 SVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVL-FSCSVAE 551
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIA---YGADNLSSVTAQQVERAAEVANAAEFIRSFP-QGFDTvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:PRK10253 101 LVArgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 628 ALDAENEHLVQEALDRL--MEGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK10253 173 WLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
463-674 |
5.53e-20 |
|
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: 89.70 E-value: 5.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 463 HFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHD--IRQLNpvwLRSKIGTV-- 538
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKK---FLRRIGVVfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 539 SQEPVLFSCSVAENIAYGAD--NLSSVTAQQ-VERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLK 615
Cdd:cd03267 102 QKTQLWWDLPVIDSFYLLAAiyDLPPARFKKrLDELSELLDLEELL-------DTPVRQ----LSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTI-KNANFVAVLDHGKI 674
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRL 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
457-683 |
8.06e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.92 E-value: 8.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP--EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL---DGHDIRQLNPVW- 530
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 --------------------LRSKIGTVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAAE----VANAAEFIRSF 584
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKyielVGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 585 PqgFDtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENehlVQEALDRL----MEGRTVLIIAHRL-ST 659
Cdd:PRK13651 163 P--FE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFdnlnKQGKTIILVTHDLdNV 228
|
250 260
....*....|....*....|....*
gi 9506367 660 IKNANFVAVLDHGKICEHG-THEEL 683
Cdd:PRK13651 229 LEWTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
474-684 |
9.02e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.18 E-value: 9.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSK--IGTVSQEPVLFS-CSVA 550
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARARrgIGYLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENIAYGADNLSSVTAQQVERAAEvanaaEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALD 630
Cdd:PRK10895 97 DNLMAVLQIRDDLSAEQREDRAN-----ELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 631 AENEHLVQEALDRLME-GRTVLIIAHRL-STIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK10895 170 PISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
474-658 |
1.74e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 87.95 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQL---NPVWLRS-KIGTVSQ-EPVLFSCS 548
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 549 VAENIAYGADNLSSVTAQQVERAAEVANAAefirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSA 628
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|..
gi 9506367 629 LDAENEHLVQEALDRL--MEGRTVLIIAHRLS 658
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
457-674 |
2.87e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.20 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsLDG----HDIRQlnpvwlr 532
Cdd:PRK11247 13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEARE------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 sKIGTVSQEPVLFSC-SVAENIAYGadnLSSVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIAR 611
Cdd:PRK11247 82 -DTRLMFQDARLLPWkKVIDNVGLG---LKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKI 674
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
464-684 |
3.88e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.14 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 464 FTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH--DIRQLNPVWLRSKIGTVSQE 541
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 542 P--VLFSCSVAENIAYGADNL---SSVTAQQVERAAEVANAAEFIRSFPQgfdtvvgekgiLLSGGQKQRIAIARALLKN 616
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLgvpEAEITRRVDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 617 PKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
479-695 |
6.73e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 88.61 E-value: 6.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WL--RSKIGTVSQEPvLFSC----SVAE 551
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDeWRavRSDIQMIFQDP-LASLnprmTIGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIAygaDNLSS----VTAQQVE---RA--AEVANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLL 622
Cdd:PRK15079 120 IIA---EPLRTyhpkLSRQEVKdrvKAmmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 623 DEATSALD----AENEHLVQEaLDRLMeGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPNGLYRK-LM 695
Cdd:PRK15079 186 DEPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYTKaLM 262
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
196-426 |
7.41e-19 |
|
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: 88.10 E-value: 7.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 196 IRVYLMQSSGQSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFV 275
Cdd:cd18558 78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 276 SPSLATFVLSVVPPISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQK 355
Cdd:cd18558 158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 356 EALARAGFFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELMKGLGA 426
Cdd:cd18558 238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGA 308
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
456-631 |
8.41e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 88.75 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVHFTYPARpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLR----LYDPNSGTVSLDGHDIRQLNPVwL 531
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRmvagLERITSGEIWIGGRVVNELEPA-D 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSkIGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQVERAAEVANAAEfIRSFPQgfdtvvgEKGILLSGGQKQRIAIA 610
Cdd:PRK11650 76 RD-IAMVFQNYALYPhMSVRENMAYGLKIRGMPKAEIEERVAEAARILE-LEPLLD-------RKPRELSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 9506367 611 RALLKNPKILLLDEATSALDA 631
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
454-660 |
1.28e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 454 QGALEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLR 532
Cdd:PRK11288 2 SPYLSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQE----PVLfscSVAENIAYGAdnLSSvTAQQVERAAEVANAAEFIRSFPQGFD--TVVGEkgilLSGGQKQR 606
Cdd:PRK11288 79 AGVAIIYQElhlvPEM---TVAENLYLGQ--LPH-KGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQM 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 607 IAIARALLKNPKILLLDEATSALDA-ENEHLVQeALDRLM-EGRTVLIIAHRLSTI 660
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRaEGRVILYVSHRMEEI 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
470-661 |
6.62e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.53 E-value: 6.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 470 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSKIGTVSQE-PVLFSC 547
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHkLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 548 SVAENIAYGADNLSSVTAQQV-------ERAAEVANAAEFIRSfpqgFDTVVGEkgilLSGGQKQRIAIARALLKNPKIL 620
Cdd:PRK09700 96 TVLENLYIGRHLTKKVCGVNIidwremrVRAAMMLLRVGLKVD----LDEKVAN----LSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9506367 621 LLDEATSAL-DAENEHLVQeALDRLM-EGRTVLIIAHRLSTIK 661
Cdd:PRK09700 168 IMDEPTSSLtNKEVDYLFL-IMNQLRkEGTAIVYISHKLAEIR 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
457-683 |
6.82e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.41 E-value: 6.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIG 536
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 T--VSQEPVLF-SCSVAENIAYG----ADNLSSVTAQQVERAAEV---ANAAefirsfpqgfdtvvgekgiLLSGGQKQR 606
Cdd:PRK15439 88 IylVPQEPLLFpNLSVKENILFGlpkrQASMQKMKQLLAALGCQLdldSSAG-------------------SLEVADRQI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 607 IAIARALLKNPKILLLDEATSALD-AENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 683
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
149-403 |
9.92e-18 |
|
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: 84.39 E-value: 9.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 149 ITMSAPFFLGRIIDVIYTNPSEGYGDSLTRLCAVLTCVFLCGA----AANGIRVYLMQSSGQSIVNRLRTSLFSSILRQE 224
Cdd:cd18554 14 IPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLilrpPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 225 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLaTFVLSVVPPISVLAV--IYGRyLR 302
Cdd:cd18554 94 LRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKL-TFVSLVIFPFYILAVkyFFGR-LR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 303 KLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLYKG 382
Cdd:cd18554 172 KLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFA 251
|
250 260
....*....|....*....|.
gi 9506367 383 GLLMGSAHMTVGELSSFLMYA 403
Cdd:cd18554 252 AYLVIEGNLTVGTLVAFVGYM 272
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
457-687 |
1.15e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFtYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN----SGTVSLDGhdiRQLNPVWLR 532
Cdd:PRK10418 5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDG---KPVAPCALR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SK-IGTVSQEPVLFSCSVAENIAYGADNLSSV-------TAQQVERAAEVANAAEFIRSFPqgFDtvvgekgilLSGGQK 604
Cdd:PRK10418 78 GRkIATIMQNPRSAFNPLHTMHTHARETCLALgkpaddaTLTAALEAVGLENAARVLKLYP--FE---------MSGGML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 605 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRT--VLIIAHRLSTI-KNANFVAVLDHGKICEHGTHE 681
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVE 226
|
....*.
gi 9506367 682 ELLLKP 687
Cdd:PRK10418 227 TLFNAP 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
474-674 |
1.19e-17 |
|
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: 81.32 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP-VWLRSKIGTVSQEP----VLFSCS 548
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 549 VAENIAYGadnlssvtaqqveraaevanaaefirsfpqgfdtvvgekgILLSGGQKQRIAIARALLKNPKILLLDEATSA 628
Cdd:cd03215 95 VAENIALS----------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 629 LDAENEHLVQEALDRL-MEGRTVLIIahrlST-----IKNANFVAVLDHGKI 674
Cdd:cd03215 135 VDVGAKAEIYRLIRELaDAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
133-420 |
1.27e-17 |
|
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: 84.07 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 133 RGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRL 212
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTL---DGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 213 RTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISV 292
Cdd:cd18540 78 RKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 293 LAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGN 372
Cdd:cd18540 158 VSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9506367 373 LIVLSVLYKGGLLMGSAHMTVGELSSFLMYA---FWvglSIGGLSSFYSEL 420
Cdd:cd18540 238 IATALVLWYGGILVLAGAITIGTLVAFISYAtqfFE---PIQQLARVLAEL 285
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
460-683 |
1.31e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 460 RNVHFTYPARP--------EVS------VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQ 525
Cdd:COG1129 239 RELEDLFPKRAaapgevvlEVEglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 526 LNPV-WLRSKIGTVS----QEPVLFSCSVAENIAYGadNLSSVT-AQQVERAAEVANAAEFIRSF---PQGFDTVVGEkg 596
Cdd:COG1129 319 RSPRdAIRAGIAYVPedrkGEGLVLDLSIRENITLA--SLDRLSrGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 597 ilLSGGQKQRIAIARALLKNPKILLLDEATSALD--AENE--HLVQEALDrlmEGRTVLII----------AHRlstikn 662
Cdd:COG1129 395 --LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRELAA---EGKAVIVIsselpellglSDR------ 463
|
250 260
....*....|....*....|.
gi 9506367 663 anfVAVLDHGKICEHGTHEEL 683
Cdd:COG1129 464 ---ILVMREGRIVGELDREEA 481
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
450-684 |
1.46e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.30 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 450 EKTFQgaleFRNVHFTYPARpevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV 529
Cdd:PRK10575 9 DTTFA----LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 530 WLRSKIGTVSQE-PVLFSCSVAENIAYGA-------DNLSSVTAQQVERAAevanaaefirsfpqgfdTVVGEKGIL--- 598
Cdd:PRK10575 82 AFARKVAYLPQQlPAAEGMTVRELVAIGRypwhgalGRFGAADREKVEEAI-----------------SLVGLKPLAhrl 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 ---LSGGQKQRIAIARALLKNPKILLLDEATSALDAenEHLVQealdrlmegrtVLIIAHRLSTIKNANFVAVL------ 669
Cdd:PRK10575 145 vdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI--AHQVD-----------VLALVHRLSQERGLTVIAVLhdinma 211
|
250 260
....*....|....*....|....*
gi 9506367 670 ----DH------GKICEHGTHEELL 684
Cdd:PRK10575 212 arycDYlvalrgGEMIAQGTPAELM 236
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
133-421 |
1.65e-17 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 83.80 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 133 RGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGygdSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRL 212
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLA---TLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 213 RTSLFSSILRQEVAFFDKTRTGELINRLSS-DTA---LLGRSVTENLSdglraGAQASVGVGMMFFVSPSLATFVLSVVP 288
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRISElDTIrgfLTGTALTTLLD-----VLFSVIYIAVLFSYSPLLTLVVLATVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 289 PISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAG 368
Cdd:cd18782 153 LQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 9506367 369 LSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELM 421
Cdd:cd18782 233 FLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQ 285
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
475-680 |
1.73e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.84 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV---WLRSKIGTVSQEP-VLFSCSVA 550
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENIAY-----GADnlSSVTAQQVERAAEVANAAEFIRSFPqgfdtvvgekgILLSGGQKQRIAIARALLKNPKILLLDEA 625
Cdd:PRK10908 98 DNVAIpliiaGAS--GDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 626 TSALDAEnehlVQEALDRLME-----GRTVLIIAHRLSTIKNANF-VAVLDHGKIceHGTH 680
Cdd:PRK10908 165 TGNLDDA----LSEGILRLFEefnrvGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
468-655 |
1.76e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 468 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQ-EPVLfs 546
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 547 cSVAENIAYGADNLSSvtaqqveRAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEAT 626
Cdd:PRK13539 89 -TVAENLEFWAAFLGG-------EELDIAAALEAV-----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 9506367 627 SALDAENEHLVQEAL-DRLMEGRTVLIIAH 655
Cdd:PRK13539 156 AALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
457-695 |
3.19e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.68 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP--------EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI----- 523
Cdd:PRK10261 314 LQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 524 RQLNPvwLRSKIGTVSQEPVLfSCSVAENIAYG------------ADNLSSVTAQQVERaaeVANAAEFIRSFPQGFdtv 591
Cdd:PRK10261 394 GKLQA--LRRDIQFIFQDPYA-SLDPRQTVGDSimeplrvhgllpGKAAAARVAWLLER---VGLLPEHAWRYPHEF--- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 592 vgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDAE-NEHLVQEALDRLME-GRTVLIIAHRLSTIKN-ANFVAV 668
Cdd:PRK10261 465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAV 536
|
250 260
....*....|....*....|....*...
gi 9506367 669 LDHGKICEHGTHEELLLKPNGLY-RKLM 695
Cdd:PRK10261 537 MYLGQIVEIGPRRAVFENPQHPYtRKLM 564
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
474-696 |
7.79e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKS-TVVSLLLRLYDPN----SGTVSLDGHDIRQLNPVWLR----SKIGTVSQEPV- 543
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 544 -LFSCSVAENIAYGADNLSSVTAQQVERAAEVA--------NAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALL 614
Cdd:PRK15134 104 sLNPLHTLEKQLYEVLSLHRGMRREAARGEILNcldrvgirQAAKRLTDYPHQ-----------LSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 615 KNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPNGLY 691
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
....*.
gi 9506367 692 -RKLMN 696
Cdd:PRK15134 253 tQKLLN 258
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
480-657 |
1.64e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.06 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 480 LSIPSGSVTALVGPSGSGKSTVVSLLLRLY--DPNSGT-VSLDGH----------DIRQLnpvwlRSKIGTVSQEPVLFS 546
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRtvqregrlarDIRKS-----RANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 547 -CSVAENIAYGA--------DNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTvvgekgilLSGGQKQRIAIARALLKNP 617
Cdd:PRK09984 100 rLSVLENVLIGAlgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQQA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9506367 618 KILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRL 657
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQV 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
457-683 |
1.72e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTypaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL---RS 533
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEPVLFS-CSVAENIAY--------GADNLSSVTAQQVErAAEVANAAEFIRSfpqgfdtvvgekgiLLSGGQK 604
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYplrehtqlPAPLLHSTVMMKLE-AVGLRGAAKLMPS--------------ELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 605 QRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHE 681
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQ 229
|
..
gi 9506367 682 EL 683
Cdd:PRK11831 230 AL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
457-671 |
2.10e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.19 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPA-RPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdirqlnpvwlrSKI 535
Cdd:cd03223 1 IELENLSLATPDgRVLLK---DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GTVSQEPVLFSCSVAENIAYgadnlssvtaqqveraaevanaaefirsfPqgFDTVvgekgilLSGGQKQRIAIARALLK 615
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIY-----------------------------P--WDDV-------LSGGEQQRLAFARLLLH 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 616 NPKILLLDEATSALDAENEHLVQEALDRlmEGRTVLIIAHRLSTIKNANFVAVLDH 671
Cdd:cd03223 109 KPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
474-656 |
2.83e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.46 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLY--DPNSGTVSLDGHDIrqlnpvwlrskigtvSQEpvlfsCSVAE 551
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIAYGADnlssvTAQQVER--AAEVANAAEFIRSFPQgfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSAL 629
Cdd:COG2401 105 AIGRKGD-----FKDAVELlnAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|.
gi 9506367 630 DAENEHLV----QEALDRLmeGRTVLIIAHR 656
Cdd:COG2401 168 DRQTAKRVarnlQKLARRA--GITLVVATHH 196
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
469-684 |
5.49e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 469 RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIrqlNPVWLRSKIGTVSQEPVLF 545
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 -SCSVAENIAYGA-----DNLSSVtaQQVERAAEV------ANAAefirsfpqgfDTVVGEKGIL--LSGGQKQRIAIAR 611
Cdd:TIGR00955 112 pTLTVREHLMFQAhlrmpRRVTKK--EKRERVDEVlqalglRKCA----------NTRIGVPGRVkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 612 ALLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLSTIKNANF--VAVLDHGKICEHGTHEELL 684
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSELFELFdkIILMAEGRVAYLGSPDQAV 255
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
464-699 |
6.07e-16 |
|
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: 82.37 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 464 FTYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIrQLNPVWLRSKIGTVSQEPV 543
Cdd:TIGR01257 938 FEPSGRPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 544 LFS-CSVAENIAYGAD-NLSSVTAQQVERAAEVANAaefirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILL 621
Cdd:TIGR01257 1014 LFHhLTVAEHILFYAQlKGRSWEEAQLEMEAMLEDT---------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 622 LDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTheELLLKP---NGLY----RK 693
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT--PLFLKNcfgTGFYltlvRK 1162
|
....*.
gi 9506367 694 LMNKQS 699
Cdd:TIGR01257 1163 MKNIQS 1168
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
476-666 |
1.21e-15 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 77.27 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVV------SLLLRLYdpNSGTVSLDGHDIRQLNPVwlrSKIGTVSQEPV------ 543
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLH--LKKEQPGNHDRIEGLEHI---DKVIVIDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 544 --------------LFsCSVAE---------NIAYGADNLSSVTAQQVERAAE----VANAAEFIRSFPQ-GFDTV-VGE 594
Cdd:cd03271 87 npatytgvfdeireLF-CEVCKgkrynretlEVRYKGKSIADVLDMTVEEALEffenIPKIARKLQTLCDvGLGYIkLGQ 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 595 KGILLSGGQKQRIAIARALLK---NPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFV 666
Cdd:cd03271 166 PATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
457-684 |
2.84e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnpvW-----L 531
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD----WqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQEPVLFS-CSVAENIAYGADNLSSVTAQQ-VERAAEVanaaefirsFPQGFDTVVGEKGILlSGGQKQRIAI 609
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQErIKWVYEL---------FPRLHERRIQRAGTM-SGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 610 ARALLKNPKILLLDEATSALDAEnehLVQEALDRLM----EGRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPI---IIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
138-403 |
4.05e-15 |
|
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: 76.35 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 138 AAVGFLAVSS-VITMSAPFFLGRIID-VIytnpSEGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18567 5 LQILLLSLALeLFALASPLYLQLVIDeVI----VSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSS-DT--ALLGRSVTENLSDGLragaQASVGVGMMFFVSPSLATFVLSVVppisv 292
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFGSlDEiqQTLTTGFVEALLDGL----MAILTLVMMFLYSPKLALIVLAAV----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 293 laVIYG--RYL--RKLSKATQDSL-AEATQLAE--ERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFG 365
Cdd:cd18567 152 --ALYAllRLAlyPPLRRATEEQIvASAKEQSHflETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSA 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 9506367 366 AAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 403
Cdd:cd18567 230 ANGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYK 267
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
456-674 |
4.58e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.53 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRNVhfTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLR-SK 534
Cdd:COG3845 257 VLEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEP-----VLfSCSVAENIA---YGADNLSSvtAQQVERAAEVANAAEFIRSF---PQGFDTVVGekgiLLSGGQ 603
Cdd:COG3845 335 VAYIPEDRlgrglVP-DMSVAENLIlgrYRRPPFSR--GGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 604 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLII----------AHRlstiknanfVAVLDHG 672
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLIsedldeilalSDR---------IAVMYEG 478
|
..
gi 9506367 673 KI 674
Cdd:COG3845 479 RI 480
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
479-683 |
5.00e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 75.41 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLnPVWLRSKIGTVS--QEPVLF-SCSVAENI-- 553
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRtfQHVRLFrEMTVIENLlv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 554 --------AYGADNLSSVTAQQVERAAeVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEA 625
Cdd:PRK11300 104 aqhqqlktGLFSGLLKTPAFRRAESEA-LDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 626 TSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEEL 683
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
457-673 |
9.07e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.52 E-value: 9.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPN---SGTVSLDG-----HDIRQLNp 528
Cdd:NF040905 2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRDSE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 vwlRSKIGTVSQE----PVLfscSVAENI-------AYGADNLSSVTAQQVERAAEVAnaaefIRSFPqgfDTVVGEKGI 597
Cdd:NF040905 77 ---ALGIVIIHQElaliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKVG-----LDESP---DTLVTDIGV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 598 llsgGQKQRIAIARALLKNPKILLLDEATSAL-DAENEHLvqeaLDRLME----GRTVLIIAHRLSTI-KNANFVAVLDH 671
Cdd:NF040905 143 ----GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAAL----LDLLLElkaqGITSIIISHKLNEIrRVADSITVLRD 214
|
..
gi 9506367 672 GK 673
Cdd:NF040905 215 GR 216
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
136-355 |
9.75e-15 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 75.23 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 136 LSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNS---SSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPslatFVLSVVPPISVLAV 295
Cdd:cd18580 78 LLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYY 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 296 IYGRYLRKLSKATQ--DSLAEA---TQLAEErIGNIRTIRAFGKEmtevEKYTGRVDQLLQLAQK 355
Cdd:cd18580 154 LLQRYYLRTSRQLRrlESESRSplySHFSET-LSGLSTIRAFGWQ----ERFIEENLRLLDASQR 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
478-684 |
1.16e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.11 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 478 FSLSIPSGSVTALVGPSGSGKSTvvsLLLRLYD--PNSGTVSLDGHDIRQLNPVWLRSKIGTVSQE-PVLFSCSVAENIA 554
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST---LLARMAGllPGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 555 -YGADNLSSVTAQQVerAAEVANAAEFI----RSFPQgfdtvvgekgilLSGGQKQRIAIARALLK-----NP--KILLL 622
Cdd:COG4138 92 lHQPAGASSEAVEQL--LAQLAEALGLEdklsRPLTQ------------LSGGEWQRVRLAAVLLQvwptiNPegQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 623 DEATSALD-AEnehlvQEALDRLME-----GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELL 684
Cdd:COG4138 158 DEPMNSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
468-641 |
1.46e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.91 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 468 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSC 547
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 548 SVAENIAYGADNLSSvtaQQVERAAEVANAAEFirsfpqgFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:cd03231 89 SVLENLRFWHADHSD---EQVEEALARVGLNGF-------EDRPVAQ----LSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 9506367 628 ALDAENEHLVQEAL 641
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
457-681 |
1.57e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 73.91 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYParpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--RLYDPNSGTVSLDGHDIRQLNPVwLRSK 534
Cdd:CHL00131 8 LEIKNLHASVN---ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPE-ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGT------------VSQEPVLFSCSVAENIAYGADNLSSVTAQQV--ERAAEVANAAEFI-RSFPQGFdtvvgekgill 599
Cdd:CHL00131 84 LGIflafqypieipgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIinEKLKLVGMDPSFLsRNVNEGF----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 600 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH--RLSTIKNANFVAVLDHGKICE 676
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
....*
gi 9506367 677 HGTHE 681
Cdd:CHL00131 233 TGDAE 237
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
472-687 |
2.00e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.94 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 472 VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN----SGTVSLDGHDIRQLNPV----WLRSKIGTVSQEPV 543
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRerrkIIGREIAMIFQEPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 544 lfSC-----SVAENIAYGADNlSSVTA-------QQVERAAE------VANAAEFIRSFPQGfdtvvgekgilLSGGQKQ 605
Cdd:COG4170 100 --SCldpsaKIGDQLIEAIPS-WTFKGkwwqrfkWRKKRAIEllhrvgIKDHKDIMNSYPHE-----------LTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL--MEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEE 682
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQ 245
|
....*
gi 9506367 683 LLLKP 687
Cdd:COG4170 246 ILKSP 250
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
468-655 |
2.75e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.01 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 468 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQEPVLFSC 547
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 548 SVAENIAYGADNLSSVtaqqvERAAEVANAAEFIRSFPqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:TIGR01189 89 SALENLHFWAAIHGGA-----QRTIEDALAAVGLTGFE---DLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 9506367 628 ALDAENEHLVQEAL-DRLMEGRTVLIIAH 655
Cdd:TIGR01189 157 ALDKAGVALLAGLLrAHLARGGIVLLTTH 185
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
484-671 |
3.32e-14 |
|
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: 70.48 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 484 SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTV-SLDGHDIRQLNPVWLRskigtvsqepvlfscsvaeniaygadnlss 562
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 563 vtaqqveraaevanaaefirsfpqgfDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALD 642
Cdd:smart00382 51 --------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
170 180 190
....*....|....*....|....*....|....*.
gi 9506367 643 RLM-------EGRTVLIIAHRLSTIKNANFVAVLDH 671
Cdd:smart00382 105 LRLllllkseKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
477-702 |
6.39e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 72.06 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGS-----VTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIrQLNPVWLRSKI-GTVSqepvlfscsva 550
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYeGTVR----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 eniaygaDNLSSVTAQQVERA---AEVANaaefirsfPQGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:cd03237 80 -------DLLSSITKDFYTHPyfkTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 628 ALDAENEHLVQEALDRLMEG--RTVLIIAHRLSTIKN-ANFVAVLDhGKICEHGTheelLLKPNGLyRKLMNKqsFLS 702
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV----ANPPQSL-RSGMNR--FLK 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
471-630 |
1.01e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.96 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 471 EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP---VWLRSK-IGTVSQEPVLF- 545
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKhVGFVFQSFMLIp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 SCSVAENIAYGADNLSSVTAQQVERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLL 622
Cdd:PRK10584 102 TLNALENVELPALLRGESSRQSRNGAKALLEQlglGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDVLFA 170
|
....*...
gi 9506367 623 DEATSALD 630
Cdd:PRK10584 171 DEPTGNLD 178
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
476-684 |
1.03e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRsKIGTV----SQ----EPVLFSC 547
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlwwdLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 548 SVAENIaYGADNlsSVTAQQVERAAEVANAAEFIrsfpqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:COG4586 118 RLLKAI-YRIPD--AEYKKRLDELVELLDLGELL-------DTPVRQ----LSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 628 ALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELK 243
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
153-403 |
1.39e-13 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 71.76 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 153 APFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQEVAFFDKTR 232
Cdd:cd18588 21 TPLFFQVIIDKVLVHRSL---STLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 233 TGELINRL------------SSDTALLgrsvtenlsDGLRAGaqasVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRY 300
Cdd:cd18588 98 VGDTVARVrelesirqfltgSALTLVL---------DLVFSV----VFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 301 LRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLSGNLIVLSVLY 380
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILW 244
|
250 260
....*....|....*....|...
gi 9506367 381 KGGLLMGSAHMTVGELSSFLMYA 403
Cdd:cd18588 245 FGAYLVMDGELTIGQLIAFNMLA 267
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
457-673 |
1.41e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPN---SGTVSLDG-----HDIRQLNp 528
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGeelqaSNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 vwlRSKIGTVSQEPVLFS-CSVAENIAYGADnlsSVTAQQVERAAEVANAAEFIRSFPQGFD--TVVGEkgilLSGGQKQ 605
Cdd:PRK13549 81 ---RAGIAIIHQELALVKeLSVLENIFLGNE---ITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGN----LGLGQQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 606 RIAIARALLKNPKILLLDEATSAL-DAENEHLVQEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGK 673
Cdd:PRK13549 151 LVEIAKALNKQARLLILDEPTASLtESETAVLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
477-630 |
2.31e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPV-WLRSKIGTVSQEP----VLFSCSVAE 551
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NIAYGADNLSSVTAQQVERAAEVANAAEFIRSF----PqGFDTVVGekgiLLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:PRK10762 350 NMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
...
gi 9506367 628 ALD 630
Cdd:PRK10762 425 GVD 427
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
457-696 |
2.89e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARP------EVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHD-------- 522
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPlhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 523 ----IR--------QLNPvwlRSKIGTVSQEPVLFSCSVAENIAYGADNLssvTAQQVERAAEVANaaefirSFPQgfdt 590
Cdd:PRK15112 85 rsqrIRmifqdpstSLNP---RQRISQILDFPLRLNTDLEPEQREKQIIE---TLRQVGLLPDHAS------YYPH---- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 591 vvgekgiLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVA 667
Cdd:PRK15112 149 -------MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVL 221
|
250 260 270
....*....|....*....|....*....|
gi 9506367 668 VLDHGKICEHGTHEELLLKP-NGLYRKLMN 696
Cdd:PRK15112 222 VMHQGEVVERGSTADVLASPlHELTKRLIA 251
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
461-691 |
3.22e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.29 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 461 NVHFTYPaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDI-----RQLNPvwLR 532
Cdd:PRK09473 19 RVTFSTP-DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELNK--LR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 S-KIGTVSQEPVlfsCSVAENIAYGaDNLSSV--------TAQQVER------AAEVANAAEFIRSFPQGFdtvvgekgi 597
Cdd:PRK09473 96 AeQISMIFQDPM---TSLNPYMRVG-EQLMEVlmlhkgmsKAEAFEEsvrmldAVKMPEARKRMKMYPHEF--------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 598 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLI-IAHRLSTIKN-ANFVAVLDHGKI 674
Cdd:PRK09473 163 --SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDLGVVAGiCDKVLVMYAGRT 240
|
250
....*....|....*..
gi 9506367 675 CEHGTHEELLLKPNGLY 691
Cdd:PRK09473 241 MEYGNARDVFYQPSHPY 257
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
475-695 |
3.44e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDiRQLNPVW----------LRSKIGTVSQEP-- 542
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYalseaerrrlLRTEWGFVHQHPrd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 543 -VLFSCSVAENI-----AYGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKN 616
Cdd:PRK11701 101 gLRMQVSAGGNIgerlmAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTF-----------SGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 617 PKILLLDEATSALDAEnehlVQEALDRLMEGRT------VLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPNG 689
Cdd:PRK11701 170 PRLVFMDEPTGGLDVS----VQARLLDLLRGLVrelglaVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
....*.
gi 9506367 690 LYRKLM 695
Cdd:PRK11701 246 PYTQLL 251
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
142-421 |
3.72e-13 |
|
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: 70.67 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 142 FLA--VSSVITMSAPFFLGRIID-VIYTNPSegygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSsgqsIVNRLRTSLFS 218
Cdd:cd18568 8 LLAslLLQLLGLALPLFTQIILDrVLVHKNI----SLLNLILIGLLIVGIFQILLSAVRQYLLDY----FANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 219 S----ILRQEVAFFDKTRTGELINRLSSD---TALLGRSVTENLSDGLragaQASVGVGMMFFVSPSLATFVLSVVPPIS 291
Cdd:cd18568 80 DfykhLLSLPLSFFASRKVGDIITRFQENqkiRRFLTRSALTTILDLL----MVFIYLGLMFYYNLQLTLIVLAFIPLYV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 292 VLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKE-------------MTEVEKYTGRVDQLLQLAqkeal 358
Cdd:cd18568 156 LLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAErpirwrwenkfakALNTRFRGQKLSIVLQLI----- 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 359 arAGFFGAAGLsgnlivLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSELM 421
Cdd:cd18568 231 --SSLINHLGT------IAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQ 285
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
478-688 |
6.35e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 478 FSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPNSGTVSLDGHDIRQLNPVWLRSKIGTVSQE-PVLFSCSVAENIA-Y 555
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 556 GADNL-SSVTAQQVERAAEVANAAEFI-RSFPQgfdtvvgekgilLSGGQKQRIAIARALLK-----NP--KILLLDEAT 626
Cdd:PRK03695 94 QPDKTrTEAVASALNEVAEALGLDDKLgRSVNQ------------LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 627 SALDAENehlvQEALDRLME-----GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHGTHEELLLKPN 688
Cdd:PRK03695 162 NSLDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
472-686 |
7.09e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 472 VSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLL--LRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTvsqepvlfSCSV 549
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALCEKCGYVERPSKVGE--------PCPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 550 AENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFP-QGFDTVV-------------GEKGIL----------------- 598
Cdd:TIGR03269 85 CGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlYGDDTVLdnvlealeeigyeGKEAVGravdliemvqlshrith 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 ----LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTIKNANFVAV-LDH 671
Cdd:TIGR03269 165 iardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDLSDKAIwLEN 244
|
250
....*....|....*
gi 9506367 672 GKICEHGTHEELLLK 686
Cdd:TIGR03269 245 GEIKEEGTPDEVVAV 259
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
148-420 |
9.17e-13 |
|
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: 69.46 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 148 VITMSAPFFLGRIIDVIYTNPSEGYgdsLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQEVAF 227
Cdd:cd18555 16 LLTLLIPILTQYVIDNVIVPGNLNL---LNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 228 FDKTRTGELINRLSSDTA---LLGRSVTENLSDGLRAGaqasVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRYLRKL 304
Cdd:cd18555 93 FENRSSGDLLFRANSNVYirqILSNQVISLIIDLLLLV----IYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 305 skaTQDSLAEATQLAE---ERIGNIRTIRAFGKEMTEVEKYTGRVDQLLqLAQKEALARAGFFGAA----GLSGNLIVLS 377
Cdd:cd18555 169 ---NQEEIVAQTKVQSyltETLYGIETIKSLGSEKNIYKKWENLFKKQL-KAFKKKERLSNILNSIsssiQFIAPLLILW 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 9506367 378 VlykGGLLMGSAHMTVGELSSFLMYAFWVGLSIGGLSSFYSEL 420
Cdd:cd18555 245 I---GAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQF 284
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
465-673 |
9.47e-13 |
|
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: 71.12 E-value: 9.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 465 TYParPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTvvslLLRLydpnsgtvsLDGHDIRQLNPVWLRS--KIGTVSQEP 542
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST----LLRI---------MAGVDKDFNGEARPQPgiKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 543 VL-FSCSVAENIAYGA-------DNLSSVTAQ----------------------------QVERAAEVAnaAEFIRsFPQ 586
Cdd:TIGR03719 78 QLdPTKTVRENVEEGVaeikdalDRFNEISAKyaepdadfdklaaeqaelqeiidaadawDLDSQLEIA--MDALR-CPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 587 GfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN----EHLVQEaldrlMEGrTVLIIAHRLSTIKN 662
Cdd:TIGR03719 155 W-DADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVTHDRYFLDN 223
|
250
....*....|..
gi 9506367 663 -ANFVAVLDHGK 673
Cdd:TIGR03719 224 vAGWILELDRGR 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
474-708 |
9.98e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlRSKIGTVSQ----EPVL-FSCS 548
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVPQklylDTTLpLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 549 VAENIAYGadnlssVTAQQVERAAEVANAAEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSA 628
Cdd:PRK09544 88 RFLRLRPG------TKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 629 LDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNANFVAVLDHgKICEHGTHEELLLKPNGLyrklmnkqSFLSYNG 705
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCLNH-HICCSGTPEVVSLHPEFI--------SMFGPRG 221
|
...
gi 9506367 706 AEQ 708
Cdd:PRK09544 222 AEQ 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
461-693 |
1.02e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 461 NVHFtYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP--VWLRSK---- 534
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 --------IGTVSQEPV-----LFScsVAENIAygadnlSSVTAQQ----VERAAEVANAAEFIRsFPQGfDTVVGEKGI 597
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMtslnpVFT--VGEQIA------ESIRLHQgasrEEAMVEAKRMLDQVR-IPEA-QTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 598 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEGRT--VLIIAHRLSTIKN-ANFVAVLDHGKI 674
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEA 247
|
250
....*....|....*....
gi 9506367 675 CEHGTHEELLLKPNGLYRK 693
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTR 266
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
454-660 |
1.04e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 454 QGALEFRNVHFTYpaRPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlnpVWLRS 533
Cdd:PRK15056 4 QAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQ-EPVLFSCSV-AENIA----YGADNL----SSVTAQQVERAAEVANAAEFIRSfpqgfdtVVGEkgilLSGGQ 603
Cdd:PRK15056 79 LVAYVPQsEEVDWSFPVlVEDVVmmgrYGHMGWlrraKKRDRQIVTAALARVDMVEFRHR-------QIGE----LSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 604 KQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTI 660
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
461-684 |
1.17e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 461 NVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL-RLYDPN-------SGTVSLDGHDIRQLNPVWLR 532
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 533 SKIGTVSQ--EPVlFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIrsfpQGFDTVVGEKGILLSGGQKQRIAIA 610
Cdd:PRK13547 83 RLRAVLPQaaQPA-FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALAL----AGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 611 RALLK---------NPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLS-TIKNANFVAVLDHGKICEHG 678
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
....*.
gi 9506367 679 THEELL 684
Cdd:PRK13547 238 APADVL 243
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
457-659 |
1.27e-12 |
|
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: 66.88 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN--SGTVSLDGhdiRQLNPVWLRS 533
Cdd:cd03232 4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING---RPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 kIGTVSQEPVLFSCS-VAENIAYGADNlssvtaqqveRAaevanaaefirsfpqgfdtvvgekgilLSGGQKQRIAIARA 612
Cdd:cd03232 81 -TGYVEQQDVHSPNLtVREALRFSALL----------RG---------------------------LSVEQRKRLTIGVE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9506367 613 LLKNPKILLLDEATSALDAENEHLVQEALDRL-MEGRTVLIIAHRLST 659
Cdd:cd03232 123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSA 170
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
457-665 |
1.81e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.90 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI--------RQLNP 528
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctyqKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 VWLRSKIgtvsqEPVLfscSVAENIAYgaDNLSSVTAQQVERAAEVANAAEFIrSFPQGfdtvvgekgiLLSGGQKQRIA 608
Cdd:PRK13540 79 VGHRSGI-----NPYL---TLRENCLY--DIHFSPGAVGITELCRLFSLEHLI-DYPCG----------LLSSGQKRQVA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 609 IARALLKNPKILLLDEATSALDAEN-EHLVQEALDRLMEGRTVLIIAHRLSTIKNANF 665
Cdd:PRK13540 138 LLRLWMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKADY 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
446-655 |
4.99e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 446 MVLDEKTFQGAL--EFRNVHFTYPARPEVSvfqDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdi 523
Cdd:PRK11147 307 MQVEEASRSGKIvfEMENVNYQIDGKQLVK---DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 524 rqlnpvwlrsKIGTvSQEPVLFSC---------SVAENIAYGAdnlSSVTAQQVERaaevanaaeFIRSFPQGF------ 588
Cdd:PRK11147 377 ----------HCGT-KLEVAYFDQhraeldpekTVMDNLAEGK---QEVMVNGRPR---------HVLGYLQDFlfhpkr 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 589 -DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRlMEGrTVLIIAH 655
Cdd:PRK11147 434 aMTPVKA----LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
470-660 |
5.77e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 470 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPvwlRSK----IGTVSQE---- 541
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP---KSSqeagIGIIHQElnli 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 542 PVLfscSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILL 621
Cdd:PRK10762 92 PQL---TIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9506367 622 LDEATSAL-DAENEHLVQEALDRLMEGRTVLIIAHRLSTI 660
Cdd:PRK10762 165 MDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEI 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
459-631 |
9.95e-12 |
|
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: 64.59 E-value: 9.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 459 FRNVHFTYP-ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPVWlRSK 534
Cdd:cd03233 6 WRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY-PGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQEPVLFScsvaeniaygadnlsSVTAQQVERAAEVANAAEFIRsfpqgfdtvvgekGIllSGGQKQRIAIARALL 614
Cdd:cd03233 85 IIYVSEEDVHFP---------------TLTVRETLDFALRCKGNEFVR-------------GI--SGGERKRVSIAEALV 134
|
170
....*....|....*..
gi 9506367 615 KNPKILLLDEATSALDA 631
Cdd:cd03233 135 SRASVLCWDNSTRGLDS 151
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
479-684 |
1.84e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 67.13 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL----DGHDIRQLNPVwLRSK----IGTVSQEPVLFSCSVA 550
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 eniaygADNLSSvtAQQVERAAEVANAAEFIRSFPQGFDTVVGEKgIL------LSGGQKQRIAIARALLKNPKILLLDE 624
Cdd:TIGR03269 383 ------LDNLTE--AIGLELPDELARMKAVITLKMVGFDEEKAEE-ILdkypdeLSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 625 ATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
457-691 |
1.87e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.98 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRN--VHFTYPARPeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN----SGTVSLDGHDIRQLNPVW 530
Cdd:PRK15093 4 LDIRNltIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 LRSKIG-TVS---QEPVlfSC-SVAENIayGADNLSSVTA--------QQV----ERAAE------VANAAEFIRSFPQG 587
Cdd:PRK15093 83 RRKLVGhNVSmifQEPQ--SClDPSERV--GRQLMQNIPGwtykgrwwQRFgwrkRRAIEllhrvgIKDHKDAMRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 588 fdtvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME--GRTVLIIAHRLSTI-KNAN 664
Cdd:PRK15093 159 -----------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWAD 227
|
250 260
....*....|....*....|....*..
gi 9506367 665 FVAVLDHGKICEHGTHEELLLKPNGLY 691
Cdd:PRK15093 228 KINVLYCGQTVETAPSKELVTTPHHPY 254
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
457-676 |
2.46e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArpevsvfQDFS-----LSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWL 531
Cdd:PRK10522 323 LELRNVTFAYQD-------NGFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTVSQEPVLFscsvaeniaygaDNLSSVTAQQVERAAeVANAAEFIRSfpQGFDTVVGEK--GILLSGGQKQRIAI 609
Cdd:PRK10522 396 RKLFSAVFTDFHLF------------DQLLGPEGKPANPAL-VEKWLERLKM--AHKLELEDGRisNLKLSKGQKKRLAL 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 610 ARALLKNPKILLLDEATSALDAE-NEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFVAVLDHGKICE 676
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
485-673 |
2.88e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 485 GSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRskIGTVSQEPVLFS-CSVAENIAYGA--DNLS 561
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR--TGFVTQDDILYPhLTVRETLVFCSllRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 562 SVTAQQVERAAEvANAAEFirSFPQGFDTVVGEKGIL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEH-LVQE 639
Cdd:PLN03211 172 SLTKQEKILVAE-SVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLVLT 248
|
170 180 190
....*....|....*....|....*....|....*.
gi 9506367 640 ALDRLMEGRTVLIIAHRLSTIKNANF--VAVLDHGK 673
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQPSSRVYQMFdsVLVLSEGR 284
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
477-660 |
5.94e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.60 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGS-----VTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghdIR-QLNPVWLRSKI-GTVSQepVLFSCsv 549
Cdd:PRK13409 352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKPDYdGTVED--LLRSI-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 550 aeniaygADNLSSVTAQQveraaevanaaEFIRSF--PQGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:PRK13409 425 -------TDDLGSSYYKS-----------EIIKPLqlERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
170 180 190
....*....|....*....|....*....|....*
gi 9506367 628 ALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTI 660
Cdd:PRK13409 483 HLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
475-660 |
6.01e-11 |
|
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: 65.58 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIPSGS-----VTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghdirqLN----PVWLRSKI-GTVSQepVL 544
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKisykPQYISPDYdGTVEE--FL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 545 FSCSvaeniaygADNLSSVTAQqveraaevanaAEFIRsfPQG----FDTVVGEkgilLSGGQKQRIAIARALLKNPKIL 620
Cdd:COG1245 423 RSAN--------TDDFGSSYYK-----------TEIIK--PLGleklLDKNVKD----LSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9506367 621 LLDEATSALDAENEHLVQEALDRLMEGR--TVLIIAHRLSTI 660
Cdd:COG1245 478 LLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
457-680 |
6.58e-11 |
|
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: 65.23 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPArpeVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYdPN---SGTVSLDGHDIRQLNPVWLRS 533
Cdd:TIGR02633 2 LEMKGIVKTFGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 K-IGTVSQEPVLF-SCSVAENIAYGadNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTV---VGEKGillsGGQKQRIA 608
Cdd:TIGR02633 78 AgIVIIHQELTLVpELSVAENIFLG--NEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtrpVGDYG----GGQQQLVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 609 IARALLKNPKILLLDEATSAL-DAENEHLVQEALDRLMEGRTVLIIAHRLSTIKnanfvAVLDHGKICEHGTH 680
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQH 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
470-660 |
6.89e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 470 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIR-QLNPVWLRSKIGTVSQE-PVLFSC 547
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 548 SVAENIAYGADNLSSVTAQQVERAAEVANAAEFIrsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATS 627
Cdd:PRK10982 89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190
....*....|....*....|....*....|....*
gi 9506367 628 AL-DAENEHLVQeALDRLME-GRTVLIIAHRLSTI 660
Cdd:PRK10982 164 SLtEKEVNHLFT-IIRKLKErGCGIVYISHKMEEI 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
457-659 |
7.02e-11 |
|
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: 65.34 E-value: 7.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLdGHDIrqlnpvwlrsKIG 536
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQ--EPVLFSCSVAENIAYGADNLSSVTAQQVERAaevanaaeFIRSFpqGFDTVVGEKGI-LLSGGQKQRIAIARAL 613
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGLDIIKLGKREIPSRA--------YVGRF--NFKGSDQQKKVgQLSGGERNRVHLAKTL 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9506367 614 LKNPKILLLDEATSALDAENEHLVQEALDRLmeGRTVLIIAH------RLST 659
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
457-675 |
8.33e-11 |
|
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: 64.85 E-value: 8.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN-SGTVSLDGHDIRQLNPV-WLRSK 534
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 535 IGTVSQE-------PVLfscSVAENIAYGADNlSSVTAQQVERAAEVANAAEFIR------SFPqgfDTVVGEkgilLSG 601
Cdd:TIGR02633 338 IAMVPEDrkrhgivPIL---GVGKNITLSVLK-SFCFKMRIDAAAELQIIGSAIQrlkvktASP---FLPIGR----LSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 602 GQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKIC 675
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
469-694 |
1.03e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.74 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 469 RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRS--KIGTVSQ-EPVLf 545
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQPGiKTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 scSVAENIAYGADNLSSVTAQQVERAAEVANAAefirsfpqGF-DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDE 624
Cdd:PRK13538 90 --TALENLRFYQRLHGPGDDEALWEALAQVGLA--------GFeDVPVRQ----LSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 625 ATSALDAenehlvqEALDRLmegrTVLIIAHrlstiknanfvavldhgkiCEHG------THEELLLKPNGlYRKL 694
Cdd:PRK13538 156 PFTAIDK-------QGVARL----EALLAQH-------------------AEQGgmviltTHQDLPVASDK-VRKL 200
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
409-661 |
1.22e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 64.77 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 409 SIGGLSSFYSELMKGLGAGGRLWEL---LERQPRLPFNEGMVLD--------------------EKTFQGaLEFRNVHFT 465
Cdd:TIGR00954 382 ALGRLMLAGRDMTRLAGFTARVDTLlqvLDDVKSGNFKRPRVEEiesgreggrnsnlvpgrgivEYQDNG-IKFENIPLV 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 466 YPARpEVsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGhdirqlnpvwlRSKIGTVSQEPVLF 545
Cdd:TIGR00954 461 TPNG-DV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMT 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 SCSVAENIAY--GADNL--SSVTAQQVERAAEVANAaEFIRSFPQGFDTVVGEKGiLLSGGQKQRIAIARALLKNPKILL 621
Cdd:TIGR00954 528 LGTLRDQIIYpdSSEDMkrRGLSDKDLEQILDNVQL-THILEREGGWSAVQDWMD-VLSGGEKQRIAMARLFYHKPQFAI 605
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 9506367 622 LDEATSALDAENEHLVQEALDRLmeGRTVLIIAHRLSTIK 661
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWK 643
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
475-670 |
1.30e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIPS-GSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdirQLNPVW---LRSKIGTVSQEpvLFSCSVA 550
Cdd:PRK13409 88 FKLYGLPIPKeGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--------EEEPSWdevLKRFRGTELQN--YFKKLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENIAygadnlSSVTAQQVERAAEV--ANAAEFIRSFPQG--FDTVVGEKGIL---------LSGGQKQRIAIARALLKNP 617
Cdd:PRK13409 158 GEIK------VVHKPQYVDLIPKVfkGKVRELLKKVDERgkLDEVVERLGLEnildrdiseLSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9506367 618 KILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLstiknanfvAVLD 670
Cdd:PRK13409 232 DFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL---------AVLD 275
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
457-680 |
1.42e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.12 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLL--RLYDPNSGTVSLDGHDIRQLNP------ 528
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 529 -VWLR----SKIGTVSQEPVLFSCSVAENIAYGADNLSSVTAQQ-VERAAEVANAAE--FIRSFPQGFdtvvgekgillS 600
Cdd:PRK09580 79 gIFMAfqypVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDlMEEKIALLKMPEdlLTRSVNVGF-----------S 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 601 GGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLMEG-RTVLIIAHR---LSTIKnANFVAVLDHGKICE 676
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYqriLDYIK-PDYVHVLYQGRIVK 226
|
....
gi 9506367 677 HGTH 680
Cdd:PRK09580 227 SGDF 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
428-630 |
2.28e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 428 GRlwELLERQPRLPFNEGMVLdektfqgaLEFRNVHFTYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLR 507
Cdd:PRK13549 241 GR--ELTALYPREPHTIGEVI--------LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 508 LYdP--NSGTVSLDGHDIRQLNPV-WLRSKIGTVSQE-------PVLfscSVAENIAYGAdnLSSVT-AQQVERAAEVAN 576
Cdd:PRK13549 311 AY-PgrWEGEIFIDGKPVKIRNPQqAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAA--LDRFTgGSRIDDAAELKT 384
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 577 AAEFIR------SFPqgfDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALD 630
Cdd:PRK13549 385 ILESIQrlkvktASP---ELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
139-424 |
2.70e-10 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 62.13 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIytnpSEGYGDSLTRLCAVLTCVFLC---GAAANGIRVYLMQSSGQSIVNRLRTS 215
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL----SAPASALLAVPLLLLLAYGLArilSSLFNELRDALFARVSQRAVRRLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 216 LFSSILRQEVAFFDKTRTGEL---INRLSsdtallgRSVTENLSdglragaqasvgvGMMFFVSPSLATFVLSVVppisV 292
Cdd:cd18582 77 VFRHLHSLSLRFHLSRKTGALsraIERGT-------RGIEFLLR-------------FLLFNILPTILELLLVCG----I 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 293 LAVIYG----------------------RYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYtgrvDQLL 350
Cdd:cd18582 133 LWYLYGwsyalitlvtvalyvaftikvtEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERY----DKAL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 351 QLAQKEALARAGFFGAAGLSGNLIV----LSVLYKGGLLMGSAHMTVGEL---SSFLMyAFWVGLSIggLSSFYSELMKG 423
Cdd:cd18582 209 AKYEKAAVKSQTSLALLNIGQALIIslglTAIMLLAAQGVVAGTLTVGDFvlvNTYLL-QLYQPLNF--LGFVYREIRQS 285
|
.
gi 9506367 424 L 424
Cdd:cd18582 286 L 286
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
474-655 |
4.32e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 474 VFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL-DGHdirqlnpvwlrsKIGTVSQEPVL-FSCSVAE 551
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI------------KVGYLPQEPQLdPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 552 NI-------------------------------------------AYGADNLSSvtaqQVERAAEVanaaefIRSfPQGf 588
Cdd:PRK11819 90 NVeegvaevkaaldrfneiyaayaepdadfdalaaeqgelqeiidAADAWDLDS----QLEIAMDA------LRC-PPW- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 589 DTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EHLVQealdrlMEGrTVLIIAH 655
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawleQFLHD------YPG-TVVAVTH 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
475-670 |
6.30e-10 |
|
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: 62.49 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIP-SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDghdirqlnPVW---LRSKIGTVSQEpvLFScSVA 550
Cdd:COG1245 88 FRLYGLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEE--------PSWdevLKRFRGTELQD--YFK-KLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENiaygadNLS-SVTAQQVERAAEV--ANAAEFIRSfpqgfdtvVGEKGIL-------------------LSGGQKQRIA 608
Cdd:COG1245 157 NG------EIKvAHKPQYVDLIPKVfkGTVRELLEK--------VDERGKLdelaeklglenildrdiseLSGGELQRVA 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 609 IARALLKNPKILLLDEATSALD-------AEnehLVQEALDrlmEGRTVLIIAHRLstiknanfvAVLD 670
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDiyqrlnvAR---LIRELAE---EGKYVLVVEHDL---------AILD 276
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
476-683 |
1.68e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 61.18 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLL------RLYdpNSGTVSLDGHDIRQLNPVwlrSKIGTVSQEPV------ 543
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanRLN--GAKTVPGRYTSIEGLEHL---DKVIHIDQSPIgrtprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 544 --------------LFS----------------------------------------------CSVAE---------NIA 554
Cdd:TIGR00630 700 npatytgvfdeireLFAetpeakvrgytpgrfsfnvkggrceacqgdgvikiemhflpdvyvpCEVCKgkrynretlEVK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 555 YGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTV------VGEKGILLSGGQKQRIAIARALLK---NPKILLLDEA 625
Cdd:TIGR00630 780 YKGKNIADVLDMTVEEAYEFFEAVPSISRKLQTLCDVglgyirLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEP 859
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 626 TSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFVAVL-----DH-GKICEHGTHEEL 683
Cdd:TIGR00630 860 TTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYIIDLgpeggDGgGTVVASGTPEEV 924
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
457-682 |
2.81e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.26 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNVHFTYPARPevSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVsldghdirqlnpvwLRS--- 533
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV--------------FRSakv 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 534 KIGTVSQEPVLFSCSVAENIAYGADNLSSVTAQQVeRAaevanaaeFIRSFpqgfdtvvGEKGIL-------LSGGQKQR 606
Cdd:PLN03073 573 RMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKL-RA--------HLGSF--------GVTGNLalqpmytLSGGQKSR 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 607 IAIARALLKNPKILLLDEATSALDAEN-EHLVQEALdrLMEGrTVLIIAHRLSTIKNA-NFVAVLDHGKICE-HGTHEE 682
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQG-GVLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFHD 711
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
436-684 |
2.95e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.91 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 436 RQ-PRLPFNEgmvlDEKTFQGALEFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSG 514
Cdd:PRK15064 302 RQnPFIRFEQ----DKKLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 515 TVSldghdirqlnpvWlrskigtvsqepvlfscsvAENIAYGadnlssVTAQqvERAAEVAN---AAEFIRSF--PQGFD 589
Cdd:PRK15064 375 TVK------------W-------------------SENANIG------YYAQ--DHAYDFENdltLFDWMSQWrqEGDDE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 590 TVVgeKGIL----------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDrLMEGrTVLII 653
Cdd:PRK15064 416 QAV--RGTLgrllfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFV 491
|
250 260 270
....*....|....*....|....*....|....*....
gi 9506367 654 AHrlstikNANFVAVL--------DHGKICEHGTHEELL 684
Cdd:PRK15064 492 SH------DREFVSSLatriieitPDGVVDFSGTYEEYL 524
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
458-662 |
3.19e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 458 EFRNVHFTYPARPevsVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLL-----------LRLYDPNSGTvsldGHDIrql 526
Cdd:PRK10938 262 VLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRRGS----GETI--- 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 527 npvW-LRSKIGTVSQEPVL---FSCSVAENIAYG-----------ADNLSSVTAQQVER---AAEVANAAefIRSfpqgf 588
Cdd:PRK10938 332 ---WdIKKHIGYVSSSLHLdyrVSTSVRNVILSGffdsigiyqavSDRQQKLAQQWLDIlgiDKRTADAP--FHS----- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 589 dtvvgekgilLSGGQkQRIA-IARALLKNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLI------------IA 654
Cdd:PRK10938 402 ----------LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacIT 470
|
....*...
gi 9506367 655 HRLSTIKN 662
Cdd:PRK10938 471 HRLEFVPD 478
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
443-665 |
4.28e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 443 NEGMVLDEKTFQGALEFRNVHFTYPARPEVSVFQD-FSLSIPSGSVTALVGPSGSGKSTvvsLLLRLYDPNSGTVSLDGH 521
Cdd:TIGR00956 746 NDEKDMEKESGEDIFHWRNLTYEVKIKKEKRVILNnVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGD 822
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 522 DI---RQLNPVWLRSkIGTVSQEPV-LFSCSVAENIAYGA--DNLSSVT-AQQVERAAEVANAAEfIRSFPqgfDTVVGE 594
Cdd:TIGR00956 823 RLvngRPLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAylRQPKSVSkSEKMEYVEEVIKLLE-MESYA---DAVVGV 897
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 595 KGILLSGGQKQRIAIARALLKNPKILL-LDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANF 665
Cdd:TIGR00956 898 PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILFEEF 970
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
476-672 |
4.73e-09 |
|
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: 56.18 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVslllrlydpnsgtvsLDGhdIRQLNPVWLRSKIGTVSQEPVLFscsvaeniay 555
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEG--LYASGKARLISFLPKFSRNKLIF---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 556 gADNLSSVtaqqveraaeVANAAEFIRsfpqgfdtvVGEKGILLSGGQKQRIAIARALLKNPK--ILLLDEATSALDAEN 633
Cdd:cd03238 65 -IDQLQFL----------IDVGLGYLT---------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9506367 634 EHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFVAVLDHG 672
Cdd:cd03238 125 INQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
476-657 |
6.71e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdirqlnPVWLRSKIGTVSQEPVLfsC-------- 547
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK------PIDIRSPRDAIRAGIML--Cpedrkaeg 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 548 -----SVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFpqGFDTVVGEKGIL-LSGGQKQRIAIARALLKNPKILL 621
Cdd:PRK11288 342 iipvhSVADNINISARRHHLRAGCLINNRWEAENADRFIRSL--NIKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVIL 419
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9506367 622 LDEATSALD--AENE--HLVQEALDRlmeGRTVLIIAHRL 657
Cdd:PRK11288 420 LDEPTRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDL 456
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
479-711 |
8.50e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLRSKIGTVsqepvlfscsvaENIAYGAd 558
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIELKG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 559 NLSSVTAQQVE----RAAEVANAAEFIRsfpQGFDTvvgekgilLSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 634
Cdd:PRK13545 111 LMMGLTKEKIKeiipEIIEFADIGKFIY---QPVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGD---Q 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 635 HLVQEALDRLME----GRTVLIIAHRLSTIKNANFVAV-LDHGKICEHGTHEELLLKpnglYRKLMNKQSFLSYNGAEQF 709
Cdd:PRK13545 177 TFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDH----YDEFLKKYNQMSVEERKDF 252
|
..
gi 9506367 710 LE 711
Cdd:PRK13545 253 RE 254
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
139-379 |
1.01e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 57.11 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTNP----SEGYGdsltrLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRT 214
Cdd:cd18579 2 AGLLKLLEDLLSLAQPLLLGLLISYLSSYPdeplSEGYL-----LALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 215 SLFSSILRQEVAFFDKTRTGELINRLSSDTALLGrSVTENLSDGLRAGAQASVGVGMMFFV--SPSLATFVLSVV--PPI 290
Cdd:cd18579 77 LIYRKALRLSSSARQETSTGEIVNLMSVDVQRIE-DFFLFLHYLWSAPLQIIVALYLLYRLlgWAALAGLGVLLLliPLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 291 SVLAVIYGRYLRKLSKATQdslaEATQLAEERIGNIRTIRAFGKEmtevEKYTGRVDQL----LQLAQKEALARAGFFGA 366
Cdd:cd18579 156 AFLAKLISKLRKKLMKATD----ERVKLTNEILSGIKVIKLYAWE----KPFLKRIEELrkkeLKALRKFGYLRALNSFL 227
|
250
....*....|...
gi 9506367 367 AGLSGNLIVLSVL 379
Cdd:cd18579 228 FFSTPVLVSLATF 240
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
462-691 |
1.21e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 462 VHFTYPARPEVSVfQDFSLSIPSGSVTALVGPSGSGKStVVSL-LLRLYDpNSGTVS-----LDGHDIRQLNPVWLRSKI 535
Cdd:PRK11022 11 VHFGDESAPFRAV-DRISYSVKQGEVVGIVGESGSGKS-VSSLaIMGLID-YPGRVMaekleFNGQDLQRISEKERRNLV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 536 GT----VSQEPVlfscsVAENIAY--GADNLSSVTAQQ-------VERAAE------VANAAEFIRSFPQGfdtvvgekg 596
Cdd:PRK11022 88 GAevamIFQDPM-----TSLNPCYtvGFQIMEAIKVHQggnkktrRQRAIDllnqvgIPDPASRLDVYPHQ--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 597 ilLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLM--EGRTVLIIAHRLSTI-KNANFVAVLDHGK 673
Cdd:PRK11022 154 --LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQ 231
|
250
....*....|....*...
gi 9506367 674 ICEHGTHEELLLKPNGLY 691
Cdd:PRK11022 232 VVETGKAHDIFRAPRHPY 249
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
138-347 |
1.95e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 56.32 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 138 AAVGFLAVSSVITMSAPFFLGRII----DVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSG----QSIV 209
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWAsayeTSSALPPSE---VSVLYYLGIYALISLLSVLLGTLRYLLFFFGSlrasRKLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 210 NRLRTSLFSSILRqevaFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSlatFVLSVVPp 289
Cdd:cd18604 80 ERLLHSVLRAPLR----WLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPA---FLLPAVV- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 290 ISVLAVIYGR-YLRklskaTQDSL--AEATQLA------EERIGNIRTIRAFGKEMTEVEKYTGRVD 347
Cdd:cd18604 152 LAALYVYIGRlYLR-----ASRELkrLESVARSpilshfGETLAGLVTIRAFGAEERFIEEMLRRID 213
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
479-664 |
2.09e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.90 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKSTVvslllrlydpnsgtvsldghdirqlnpvwlrskigtvsqepvLFSCSVAENIAYGAD 558
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTI------------------------------------------LDAIGLALGGAQSAT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 559 NLSSVTAQQVERAAEvanAAEFIRSFPQgfdtvvgekgilLSGGQKQRIAIARAL---LKNPKIL-LLDEATSALDAENE 634
Cdd:cd03227 53 RRRSGVKAGCIVAAV---SAELIFTRLQ------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|.
gi 9506367 635 HLVQEAL-DRLMEGRTVLIIAHRLSTIKNAN 664
Cdd:cd03227 118 QALAEAIlEHLVKGAQVIVITHLPELAELAD 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
470-631 |
2.50e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 470 PEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVV-SLLLRLYD---PNSGTVSLDGHDIRQLNPvWLRSKIGTVSQEPVLF 545
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGfhiGVEGVITYDGITPEEIKK-HYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 -SCSVAENIAYGA---------DNLSsvtaqQVERAAEVANAAEFIRSFPQGFDTVVGE---KGIllSGGQKQRIAIARA 612
Cdd:TIGR00956 151 pHLTVGETLDFAArcktpqnrpDGVS-----REEYAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEA 223
|
170
....*....|....*....
gi 9506367 613 LLKNPKILLLDEATSALDA 631
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDS 242
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
475-658 |
2.58e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.45 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIP-SGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTvsldghdiRQLNPVW---LRSKIGTVSQEpvLFSCSVA 550
Cdd:cd03236 15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDWdeiLDEFRGSELQN--YFTKLLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 551 ENIAygadnlSSVTAQQVERAAEVA--NAAEFIRSFPQ--GFDTVV---GEKGIL------LSGGQKQRIAIARALLKNP 617
Cdd:cd03236 85 GDVK------VIVKPQYVDLIPKAVkgKVGELLKKKDErgKLDELVdqlELRHVLdrnidqLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9506367 618 KILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLS 658
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
482-660 |
3.51e-08 |
|
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: 53.73 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 482 IPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHdirqlnpvwlrskigTVSQEPvlfscsvaeniaygadnls 561
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI---------------TPVYKP------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 562 svtaqqveraaevanaaefirsfpqgfdtvvgeKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEAL 641
Cdd:cd03222 68 ---------------------------------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180
....*....|....*....|.
gi 9506367 642 DRLME--GRTVLIIAHRLSTI 660
Cdd:cd03222 115 RRLSEegKKTALVVEHDLAVL 135
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
487-671 |
4.99e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 53.77 E-value: 4.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 487 VTALVGPSGSGKSTVVSLLLrlydpnsgtVSLDGHDIRQLNPVWLRSKIgtvsqepvlfsCSVAENIAYGADNLSSVTAQ 566
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK---------YALTGELPPNSKGGAHDPKL-----------IREGEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 567 Q--VERAAEVANAAEFIRsfpQG-FDTVVGEKGILLSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENehlV 637
Cdd:cd03240 84 KytITRSLAILENVIFCH---QGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---I 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 9506367 638 QEALDRLME------GRTVLIIAHrlstikNANFVAVLDH 671
Cdd:cd03240 158 EESLAEIIEerksqkNFQLIVITH------DEELVDAADH 191
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
468-641 |
5.00e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.08 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 468 ARPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNpvwlRSK-IGTVSQEPVLFS 546
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 547 -CSVAENIAYgadnlssVTAQQVERAAEVANAAEFIRSFPQGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEA 625
Cdd:PRK13543 96 dLSTLENLHF-------LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170
....*....|....*.
gi 9506367 626 TSALDAENEHLVQEAL 641
Cdd:PRK13543 165 YANLDLEGITLVNRMI 180
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
143-401 |
5.85e-08 |
|
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: 54.90 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 143 LAVSSVITMSA---PFFLGRIIDVIYTNPSEgygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSS 219
Cdd:cd18566 8 LLASLFINILAlatPLFILQVYDRVIPNESI---PTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 220 ILRQEVAFFDKTRTGELINRLSSdtallgrsvTENLSDGLraGAQASVGV----------GMMFFVSPSLATFVLSVVPP 289
Cdd:cd18566 85 LLSLPLSFFEREPSGAHLERLNS---------LEQIREFL--TGQALLALldlpfvliflGLIWYLGGKLVLVPLVLLGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 290 ISVLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYtgrvDQLLQLAQKEALARAGFFGAAGL 369
Cdd:cd18566 154 FVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRY----ERLQANAAYAGFKVAKINAVAQT 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 9506367 370 SGNLI----VLSVLYKGGLLMGSAHMTVGELSSFLM 401
Cdd:cd18566 230 LGQLFsqvsMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
478-663 |
1.28e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.57 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 478 FSLSI---PSgSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVWLrSKIGtvSQEPVLFSCSVAENIA 554
Cdd:PRK13541 17 FDLSItflPS-AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 555 YGadnlssvtaqqveraAEVANAAEFIRSFPQGF--DTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 632
Cdd:PRK13541 93 FW---------------SEIYNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180 190
....*....|....*....|....*....|..
gi 9506367 633 NEHLVQEALD-RLMEGRTVLIIAHRLSTIKNA 663
Cdd:PRK13541 158 NRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
475-630 |
1.93e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNPVwLRSKIGTV-----SQEPVLF-SCS 548
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 549 VAENI-AYGADNLSSVTAQQVERAA-EVANAAEFIRsFPQGFDTVVGekgilLSGGQKQRIAIARALLKNPKILLLDEAT 626
Cdd:PRK15439 358 LAWNVcALTHNRRGFWIKPARENAVlERYRRALNIK-FNHAEQAART-----LSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
....
gi 9506367 627 SALD 630
Cdd:PRK15439 432 RGVD 435
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
139-424 |
3.97e-07 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 52.23 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYGDSLTRLcaVLTCVFLCGAAANG-IRVYLMQSSGQSIVNRLRTSLF 217
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVTLI--LLYALLRFSSKLLKeLRSLLYRRVQQNAYRELSLKTF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 218 SSILRQEVAFFDKTRTGELI---NRLSSDTALLGRSVTENLSDGLragaqASVGVGMMFFV---SPSLATFVLSVVPPIS 291
Cdd:cd18560 79 AHLHSLSLDWHLSKKTGEVVrimDRGTESANTLLSYLVFYLVPTL-----LELIVVSVVFAfhfGAWLALIVFLSVLLYG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 292 VLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKeALARagfFGAAGLSG 371
Cdd:cd18560 154 VFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVK-VQAS---LSLLNVGQ 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 372 NLIVLSVLYkGGLLMGS-----AHMTVGELSSFLMYAF--WVGLSIggLSSFYSELMKGL 424
Cdd:cd18560 230 QLIIQLGLT-LGLLLAGyrvvdGGLSVGDFVAVNTYIFqlFQPLNF--LGTIYRMIIQSL 286
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
476-708 |
7.73e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 7.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGH-DIRQLNpVWLRSKIGTVsqEPVLFSCSVaenIA 554
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAIS-AGLSGQLTGI--ENIEFKMLC---MG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 555 YGADNLSSVTAQQVEraaeVANAAEFIRSFPQGFdtvvgekgillSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 634
Cdd:PRK13546 115 FKRKEIKAMTPKIIE----FSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---Q 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9506367 635 HLVQEALDRLME----GRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKpnglYRKLMNkqSFLSYNGAEQ 708
Cdd:PRK13546 177 TFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLN--DFKKKSKAEQ 249
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
589-658 |
1.02e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 589 DTVVGEKGIL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLS 658
Cdd:PLN03140 1009 DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPS 1080
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
137-426 |
1.73e-06 |
|
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: 50.36 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 137 SAAVGFLAVSSVITMSapFFLGRIIDVIYTNpseGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSL 216
Cdd:cd18561 1 SVLLGLLITALYIAQA--WLLARALARIFAG---GPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 217 FSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVI 296
Cdd:cd18561 76 FAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 297 YGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKE---ALARAGFFGAAGLSGNL 373
Cdd:cd18561 156 WDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVlavSLLSSGIMGLATALGTA 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 9506367 374 IVLSVLyKGGLLMGSAHMTVGELSSFLMYAFWVGLsiGGLSSFYSELMKGLGA 426
Cdd:cd18561 236 LALGVG-ALRVLGGQLTLSSLLLILFLSREFFRPL--RDLGAYWHAGYQGISA 285
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
599-674 |
2.56e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 2.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 599 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EHLVQEALDrlMEGrTVLIIAHRLSTIKN-ANFVAVLDHGKI 674
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWLEGFLKT--FQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
133-396 |
3.07e-06 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 49.52 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 133 RGRLSAAVGFLAVSSVITMSAPFFLGRIID-VIytnPSEGyGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNR 211
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDrVL---PSGS-LSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 212 LRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLragaQASVGVGMMFFVSPSLATFVLSVVPPIS 291
Cdd:cd18586 77 LGRRVFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLP----WAPLFLAVIFLIHPPLGWVALVGAPVLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 292 VLAVIYGRYLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLaQKEALARAGFFGAAGLS- 370
Cdd:cd18586 153 GLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLEL-QIRASDLAGAISAIGKTl 231
|
250 260
....*....|....*....|....*.
gi 9506367 371 GNLIVLSVLYKGGLLMGSAHMTVGEL 396
Cdd:cd18586 232 RMALQSLILGVGAYLVIDGELTIGAL 257
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
147-403 |
3.47e-06 |
|
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: 49.44 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 147 SVITMSAPFFLGRIIDVIYTNPSEGygdSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSILRQEVA 226
Cdd:cd18783 15 HVLALAPPIFFQIVIDKVLVHQSYS---TLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 227 FFDKTRTGELINRLSSDTALlgRS-VTENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSVVPPISVLAVIYGRYLRKLS 305
Cdd:cd18783 92 FFERTPAGVLTKHMQQIERI--RQfLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 306 KATQDslAEATQLA--EERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLaqKEALARAGFFGAAGLSG--NLIVLSVLYK 381
Cdd:cd18783 170 QALYR--AEGERQAflVETVHGIRTVKSLALEPRQRREWDERVARAIRA--RFAVGRLSNWPQTLTGPleKLMTVGVIWV 245
|
250 260
....*....|....*....|..
gi 9506367 382 GGLLMGSAHMTVGELSSFLMYA 403
Cdd:cd18783 246 GAYLVFAGSLTVGALIAFNMLA 267
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
469-652 |
3.82e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 469 RPEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPN---SGTVSLDGHDIRQLNPvwlRSKIGTVSQEPV-L 544
Cdd:PLN03140 175 KTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP---RKTSAYISQNDVhV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 545 FSCSVAENIAYGA---------DNLSSVTAQQVERA----AEV-----ANAAEFIRS------------FPQGFDTVVGE 594
Cdd:PLN03140 252 GVMTVKETLDFSArcqgvgtryDLLSELARREKDAGifpeAEVdlfmkATAMEGVKSslitdytlkilgLDICKDTIVGD 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9506367 595 ---KGIllSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALD---RLMEGrTVLI 652
Cdd:PLN03140 332 emiRGI--SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQqivHLTEA-TVLM 392
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
479-684 |
4.63e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 479 SLSIPSGSVTALVGPSGSGKStvvSLLLRLydpnSGTVSL-DGHDIRQLNPVWLRS-----KIgtVSQEpvlFSCSVAEN 552
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKS---ALARAL----AGELPLlSGERQSQFSHITRLSfeqlqKL--VSDE---WQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 553 IAYGADNLSSVTAQQV-------ERAAEVAnaAEFirsfpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEA 625
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIqdevkdpARCEQLA--QQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 626 TSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELL 684
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
454-689 |
4.97e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.35 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 454 QGALEFRNV--HFTyparpEVSVFQDFSLSIPSGSVTALVGPSGSGKSTVvSLLLRLYDPNSGTVSLDgHDIRQLNPVWL 531
Cdd:NF000106 11 RNAVEVRGLvkHFG-----EVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWR-F*TWCANRRAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 RSKIGTvsQEPVlfSCSVAENIAyGADNLSSVTAQ-QVERAAEVANAAEFIRSFpqGFDTVVGEKGILLSGGQKQRIAIA 610
Cdd:NF000106 84 RRTIG*--HRPV--R*GRRESFS-GRENLYMIGR*lDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 611 RALLKNPKILLLDEATSALDAENEHLV-QEALDRLMEGRTVLIIAHRLSTIKN-ANFVAVLDHGKICEHGTHEELLLKPN 688
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
|
.
gi 9506367 689 G 689
Cdd:NF000106 237 G 237
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
599-683 |
6.85e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 49.64 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 LSGGQKQRIAIARALLK--NPKIL-LLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNAnfvavlDH--- 671
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTA------DWiid 900
|
90 100
....*....|....*....|.
gi 9506367 672 ---------GKICEHGTHEEL 683
Cdd:COG0178 901 lgpeggdggGEIVAEGTPEEV 921
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
485-657 |
7.96e-06 |
|
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: 49.63 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 485 GSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQlNPVWLRSKIGTVSQEPVLFSCSVAENIAYGADNLSSVT 564
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 565 AQQVERaaeVANAAefIRSFpqGFDTVVGEKGILLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEHLVQEALDRL 644
Cdd:TIGR01257 2044 AEEIEK---VANWS--IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI 2116
|
170
....*....|....
gi 9506367 645 M-EGRTVLIIAHRL 657
Cdd:TIGR01257 2117 IrEGRAVVLTSHSM 2130
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
490-655 |
9.03e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.73 E-value: 9.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 490 LVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDirqlnpvwlrsKIGTVSQEPVLF-SCSVAENIAYGADNLSSVTAqqv 568
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKLRQDQFAFeEFTVLDTVIMGHTELWEVKQ--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 569 ERAAEVAN----------AAEFIRSFPQgFDTVVGEK--GILLSG-----------------GQKQRIAIARALLKNPKI 619
Cdd:PRK15064 98 ERDRIYALpemseedgmkVADLEVKFAE-MDGYTAEAraGELLLGvgipeeqhyglmsevapGWKLRVLLAQALFSNPDI 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 9506367 620 LLLDEATSALDAENEHLVQEALDrlmeGR--TVLIIAH 655
Cdd:PRK15064 177 LLLDEPTNNLDINTIRWLEDVLN----ERnsTMIIISH 210
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
139-335 |
9.58e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 47.98 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGYGDSLTRLCAV-------------LTCVFLCGAAangirVYLMQSSG 205
Cdd:cd18602 4 VLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDevsyyisvyaglsLGAVILSLVT-----NLAGELAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 206 QSIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGVGMMFFVSPslaTFVLS 285
Cdd:cd18602 79 LRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTP---YFLIA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9506367 286 VVpPISVLAVIYGRYLRKLSKATQ--DSLAEATQLAE--ERIGNIRTIRAFGKE 335
Cdd:cd18602 156 LI-PIIIVYYFLQKFYRASSRELQrlDNITKSPVFSHfsETLGGLTTIRAFRQQ 208
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
599-666 |
1.33e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 1.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 599 LSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFV 666
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYV 881
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
211-335 |
1.73e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 47.14 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 211 RLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTAllgrSVTENLSDGL-RAGAQASVGVGMMFFVSPSLATFVLSVVPp 289
Cdd:cd18605 76 RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVY----TIDDSLPFILnILLAQLFGLLGYLVVICYQLPWLLLLLLP- 150
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 9506367 290 isvLAVIYGRY----------LRKLSKATQDSLaeATQLAEErIGNIRTIRAFGKE 335
Cdd:cd18605 151 ---LAFIYYRIqryyratsreLKRLNSVNLSPL--YTHFSET-LKGLVTIRAFRKQ 200
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
181-306 |
1.75e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 47.32 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 181 AVLTCVFLCGAAANGIRV-YLMQSSGQSIVNRLrtslFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGL 259
Cdd:cd18601 66 AGLTAATFVFGFLRSLLFfHVAVSASKNLHNKM----FASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFL 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 9506367 260 RAGAQAsVGVgmmFFVSPSLATFVLSVVPPISVLAVIYGRYLRKLSK 306
Cdd:cd18601 142 QLLLQV-VGV---VLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSR 184
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
457-655 |
1.75e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 46.49 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 457 LEFRNvhFTYPARPEVSVFQDFSLSipsgSVTALVGPSGSGKSTvvslllrLYDpnSGTVSLDGHDIRQLNPVWLRSKIG 536
Cdd:cd03279 6 LELKN--FGPFREEQVIDFTGLDNN----GLFLICGPTGAGKST-------ILD--AITYALYGKTPRYGRQENLRSVFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 537 TVSQE-PVLFSCSvAENIAYgadnlssvtaqQVERAAEVaNAAEFIRSF--PQG-FDTVVGEKGILLSGGQKQRIAIARA 612
Cdd:cd03279 71 PGEDTaEVSFTFQ-LGGKKY-----------RVERSRGL-DYDQFTRIVllPQGeFDRFLARPVSTLSGGETFLASLSLA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9506367 613 L-----LKNPK-----ILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAH 655
Cdd:cd03279 138 LalsevLQNRGgarleALFIDEGFGTLDPEALEAVATALELIRtENRMVGVISH 191
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
211-410 |
1.83e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 47.09 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 211 RLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsvgVGMMFFVSPSLATFVLSVVPpi 290
Cdd:cd18603 75 NLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQV---ISTLVVISISTPIFLVVIIP-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 291 svLAVIYG----------RYLRKLSKAT--------QDSLAEATqlaeerignirTIRAFGKEMTEVEKYTGRVDQLLql 352
Cdd:cd18603 150 --LAILYFfiqrfyvatsRQLKRLESVSrspiyshfSETLQGAS-----------TIRAYGVQERFIRESDRRVDENQ-- 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9506367 353 aqkealaRAGFFGAAG---LS------GNLIVLS-----VLYKGgllmgsaHMTVGelssflmyafWVGLSI 410
Cdd:cd18603 215 -------RAYYPSIVSnrwLAvrleflGNLIVLFaalfaVLSRD-------SLSPG----------LVGLSI 262
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
599-712 |
2.05e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 599 LSGGQKQRIAIARALLKNP--KIL-LLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNAnfvavlDH--- 671
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTA------DWiid 904
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 9506367 672 ---------GKICEHGTHEELLLKPNglyrklmnkqsflSYNGaeQFLEP 712
Cdd:PRK00349 905 lgpeggdggGEIVATGTPEEVAKVEA-------------SYTG--RYLKP 939
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
477-630 |
2.64e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 477 DFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDI------RQLNPvwlrsKIGTVSQ------EPVL 544
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhrRAVCP-----RIAYMPQglgknlYPTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 545 fscSVAENIA-----YGADnlssvTAQQVERAAEVANA---AEFiRSFPQGfdtvvgeKgilLSGGQKQRIAIARALLKN 616
Cdd:NF033858 94 ---SVFENLDffgrlFGQD-----AAERRRRIDELLRAtglAPF-ADRPAG-------K---LSGGMKQKLGLCCALIHD 154
|
170
....*....|....
gi 9506367 617 PKILLLDEATSALD 630
Cdd:NF033858 155 PDLLILDEPTTGVD 168
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
176-335 |
3.81e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 46.31 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 176 LTRLCAVLTCVFLCGAAANGIRvylmqSSgqsivNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTallgRSVTENL 255
Cdd:cd18606 44 LGVLQAIFLFLFGLLLAYLGIR-----AS-----KRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDT----DVLDNEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 256 SDGLRagaqasvgvgmMFFVSPS--LATFVLSVV---------PPISVLAVIYGRYLRKLSK------ATQDSLAEAtQL 318
Cdd:cd18606 110 PDSLR-----------MFLYTLSsiIGTFILIIIylpwfaialPPLLVLYYFIANYYRASSRelkrleSILRSFVYA-NF 177
|
170
....*....|....*..
gi 9506367 319 AEERIGnIRTIRAFGKE 335
Cdd:cd18606 178 SESLSG-LSTIRAYGAQ 193
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
133-403 |
4.69e-05 |
|
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: 46.00 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 133 RGRLSAAVGFLAVSSVITMSAPFFLGRIIDVIYTNpseGYGDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRL 212
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPR---GDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 213 RTSLFSSILRQEVAFFDKTRTGELINRLSSDTALlgRSV-TENLSDGLRAGAQASVGVGMMFFVSPSLATFVLSV-VPPI 290
Cdd:cd18779 78 TLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATI--RELlTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLaALQV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 291 SVLAVIYGRyLRKLSKATQDSLAEATQLAEERIGNIRTIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAGFFGAAGLS 370
Cdd:cd18779 156 ALLLATRRR-VRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATL 234
|
250 260 270
....*....|....*....|....*....|...
gi 9506367 371 GNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 403
Cdd:cd18779 235 RLAAPLVLLWVGAWQVLDGQLSLGTMLALNALA 267
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
210-348 |
9.12e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 45.25 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 210 NRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRagaQASVGVGMMFFVSPSLATFVLSVVPp 289
Cdd:cd18599 91 SRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQ---NVLLVVFSLIIIAIVFPWFLIALIP- 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9506367 290 isvLAVIYGrYLRKLSKATQDSLaeatqlaeERIGNIR----------------TIRAFGKEMTEVEKYTGRVDQ 348
Cdd:cd18599 167 ---LAIIFV-FLSKIFRRAIREL--------KRLENISrsplfshltatiqglsTIHAFNKEKEFLSKFKKLLDQ 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
475-630 |
9.73e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 9.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDF------SLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNSGTVSL-----DGHDIRqlnpvwLRSKIGTVSQEpv 543
Cdd:NF033858 276 FGDFtavdhvSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIA------TRRRVGYMSQA-- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 544 lFSC----SVAENIAYGADnLSSVTAQQV-ERAAEVANA---AEFIRSFPQGfdtvvgekgilLSGGQKQRIAIARALLK 615
Cdd:NF033858 348 -FSLygelTVRQNLELHAR-LFHLPAAEIaARVAEMLERfdlADVADALPDS-----------LPLGIRQRLSLAVAVIH 414
|
170
....*....|....*
gi 9506367 616 NPKILLLDEATSALD 630
Cdd:NF033858 415 KPELLILDEPTSGVD 429
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
484-655 |
2.70e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.69 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 484 SGSVTALVGPSGSGKSTVV-SLLLRLYDPNSGTVSLDGHDIR--------------------------------QLNPVW 530
Cdd:COG0419 22 DDGLNLIVGPNGAGKSTILeAIRYALYGKARSRSKLRSDLINvgseeasvelefehggkryrierrqgefaeflEAKPSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 531 LRSKIGTvsqepvLFSCSVAENIAYGADNLSSVTAQQVERAAEVANAAEFIRSFPQGFDTVVgekgiLLSGGQKQRIAIA 610
Cdd:COG0419 102 RKEALKR------LLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQLSGLDPIE-----TLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9506367 611 RALLknpkiLLLDeaTSALDAENEHLVQEALDRLMegrtvlIIAH 655
Cdd:COG0419 171 DLLS-----LILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
456-653 |
3.60e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 456 ALEFRN--VHftYPARPEVSVFQDFSLSIPSGSVTALVGPSGSGKS-TVVSLLLRLYDPN-SGTVSLDGHDIRqlnpvwl 531
Cdd:NF040905 257 VFEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVD------- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 532 rskIGTVSQepvlfscSVAENIAY--------------------GADNLSSVTAQQV-ERAAEVANAAEF-----IRSfp 585
Cdd:NF040905 328 ---VSTVSD-------AIDAGLAYvtedrkgyglnliddikrniTLANLGKVSRRGViDENEEIKVAEEYrkkmnIKT-- 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 586 QGFDTVVGEkgilLSGGQKQRIAIARALLKNPKILLLDEATSALD--AENEhlVQEALDRLM-EGRTVLII 653
Cdd:NF040905 396 PSVFQKVGN----LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYE--IYTIINELAaEGKGVIVI 460
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
592-672 |
4.03e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 592 VGEKGILLSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEHLVQEALDRLM-EGRTVLIIAHRLSTIKNANFVA 667
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVsLGHSVIYIDHDPALLKQADYLI 1772
|
....*
gi 9506367 668 VLDHG 672
Cdd:PRK00635 1773 EMGPG 1777
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
600-630 |
4.59e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 4.59e-04
10 20 30
....*....|....*....|....*....|.
gi 9506367 600 SGGQKQRIAIARALLKNPKILLLDEATSALD 630
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
599-630 |
4.87e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 4.87e-04
10 20 30
....*....|....*....|....*....|..
gi 9506367 599 LSGGQKQRIAIARALLKNPKILLLDEATSALD 630
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
142-312 |
5.19e-04 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 42.63 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 142 FLAVSSVITMS-APFFLGRIIDVIYTNPSEGYgDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFSSI 220
Cdd:cd18556 9 FISLLSSILISiSPVILAKITDLLTSSSSDSY-NYIVVLAALYVITISATKLLGFLSLYLQSSLRVELIISISSSYFRYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 221 LRQEVAFFDKTRTGEL---INRLSSDTALLGRSVTENLSDGLragAQASVGVgmmFFVSPSLATFVLSVvppISVLAVIY 297
Cdd:cd18556 88 YEQPKTFFVKENSGDItqrLNQASNDLYTLVRNLSTNILPPL---LQLIIAI---VVILSSGDYFVAAL---FLLYAVLF 158
|
170
....*....|....*....
gi 9506367 298 ----GRYLRKLSKATQDSL 312
Cdd:cd18556 159 vinnTIFTKKIVSLRNDLM 177
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
475-513 |
5.64e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.74 E-value: 5.64e-04
10 20 30
....*....|....*....|....*....|....*....
gi 9506367 475 FQDFSLSIPSGSVTALVGPSGSGKSTVVSLLLRLYDPNS 513
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
476-666 |
9.34e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 9.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 476 QDFSLSIPSGSVTALVGPSGSGKST--------------VVSL-------LLRLYDPN-------SGTVSLDGHDIRQlN 527
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSlafdtiyaegqrryVESLsayarqfLGQMDKPDvdsieglSPAIAIDQKTTSR-N 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 528 PvwlRSKIGTVSQ----EPVLFS-CSVAENIAY----GADNLSsvtaqqVERAAEVanaaefirsfpqgfdtvvgekgil 598
Cdd:cd03270 91 P---RSTVGTVTEiydyLRLLFArVGIRERLGFlvdvGLGYLT------LSRSAPT------------------------ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 599 LSGGQKQRIAIARALLKNPK--ILLLDEATSALDAENEHLVQEALDRLME-GRTVLIIAHRLSTIKNANFV 666
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHV 208
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
214-436 |
1.45e-03 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 41.31 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 214 TSLFSSILRQEVAFFDKTRTGELINRLSSDtallgRSVTENLSDGLragAQASVGVGM-------MFFVSPSLATFVLSV 286
Cdd:cd18569 79 SRFFWHVLRLPVEFFSQRYAGDIASRVQSN-----DRVANLLSGQL---ATTVLNLVMavfyallMLQYDVPLTLIGIAI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 287 VppisVLAVIYGRYL-RKLSKATQDSLAEATQLAEERIGNIR---TIRAFGKEMTEVEKYTGRVDQLLQLAQKEALARAG 362
Cdd:cd18569 151 A----LLNLLVLRLVsRKRVDLNRRLLQDSGKLTGTTMSGLQmieTLKASGAESDFFSRWAGYQAKVLNAQQELGRTNQL 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9506367 363 FFGAAGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYafwvglsiggLSSFYSELMKGLGAGGRLWEL---LER 436
Cdd:cd18569 227 LGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSL----------MASFLAPVNSLVGLGGTLQEMrgdMER 293
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
139-335 |
1.79e-03 |
|
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: 40.86 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 139 AVGFLAVSSVITMSAPFFLGRIIDVIYTNPSEGygDSLTRLCAVLTCVFLCGAAANGIRVYLMQSSGQSIVNRLRTSLFS 218
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGL--AALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 219 SILRQEVAFFDKTRTGELinrlssdTALLGRSVtENL----SDGLRAGAQASVG----VGMMFFVSPSLATFVLSVVPPI 290
Cdd:cd18584 79 RLLALGPALLRRQSSGEL-------ATLLTEGV-DALdgyfARYLPQLVLAAIVplliLVAVFPLDWVSALILLVTAPLI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9506367 291 SVLAVIYGRYLRKLSKATQDSLAE-ATQLAeERIGNIRTIRAFGKE 335
Cdd:cd18584 151 PLFMILIGKAAQAASRRQWAALSRlSGHFL-DRLRGLPTLKLFGRA 195
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
485-526 |
1.99e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 39.04 E-value: 1.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 9506367 485 GSVTALVGPSGSGKSTvvslLLRLYDPNSGTVSLDghDIRQL 526
Cdd:COG4639 2 LSLVVLIGLPGSGKST----FARRLFAPTEVVSSD--DIRAL 37
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
598-664 |
2.87e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 2.87e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 598 LLSGGQKQRIAIA--RALLK-NPK-ILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNAN 664
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKAD 1147
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
490-516 |
3.26e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 38.28 E-value: 3.26e-03
10 20
....*....|....*....|....*..
gi 9506367 490 LVGPSGSGKSTVVSLLLRLYDPNSGTV 516
Cdd:cd00071 4 LSGPSGVGKSTLLKRLLEEFDPNFGFS 30
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
475-675 |
5.05e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 475 FQDFSLSIPSGsVTALVGPSGSGKSTVVSLLLRLYDPNSGTvSLDGHDIRQLNP---------VWLRSKIGTVSQEpvLF 545
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSR-KFDEEDFYLGDDpdlpeieieLTFGSLLSRLLRL--LL 89
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9506367 546 SCSVAENIAYGADNLSSVTAQQVERAAE--------VANAAEF-IRSFPQGFDTVVGEKGILLSGGQK----------QR 606
Cdd:COG3593 90 KEEDKEELEEALEELNEELKEALKALNEllseylkeLLDGLDLeLELSLDELEDLLKSLSLRIEDGKElpldrlgsgfQR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9506367 607 ---IAIARALL-----KNPKILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIA-HrlSTiknaNFVAVLDHGKIC 675
Cdd:COG3593 170 lilLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITtH--SP----HLLSEVPLENIR 241
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| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
576-632 |
5.45e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 5.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9506367 576 NAAEFIRSFPQGFDTvvgekgilLSGGQKQ------RIAIARALLKNPKILLLDEATSALDAE 632
Cdd:PRK01156 787 NITVSRGGMVEGIDS--------LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDED 841
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|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
490-528 |
7.27e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.11 E-value: 7.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 9506367 490 LVGPSGSGKSTVVSLLLRLYDPNSGTVSLDGHDIRQLNP 528
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
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|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
598-664 |
8.59e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.21 E-value: 8.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9506367 598 LLSGGQKQRIAIAR--ALLK-NPK-ILLLDEATSALDAENEHLVQEALDRLMEGRTVLIIAHRLSTIKNAN 664
Cdd:cd03278 113 LLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
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