|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
99-685 |
0e+00 |
|
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: 881.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 99 LSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDslnqmsgnmlNLSDAPNTVATMATAVLIGYGVSRAGAA 178
Cdd:COG5265 23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 179 FFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGV 258
Cdd:COG5265 93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 259 LYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYE 338
Cdd:COG5265 173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 339 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 418
Cdd:COG5265 253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 419 FTLLKVDTQIKDKVMASPLQITPqtATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 498
Cdd:COG5265 333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 499 QKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGE 578
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 579 RGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 658
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
570 580
....*....|....*....|....*..
gi 411147367 659 AERGTHHGLLANpHSIYSEMWHTQSSR 685
Cdd:COG5265 571 VERGTHAELLAQ-GGLYAQMWARQQEE 596
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
90-684 |
1.38e-180 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 527.43 E-value: 1.38e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 90 DTRKIIKAMLSYVWPkdrpdLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIG 169
Cdd:COG1132 4 SPRKLLRRLLRYLRP-----YRGLLILALLLLLLSALLELLLPLLLGRIIDAL---------LAGGDLSALLLLLLLLLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 170 YGVSRAGAAFFnevRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIM 249
Cdd:COG1132 70 LALLRALLSYL---QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 250 FEVMLVSGVLYYKcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQR 329
Cdd:COG1132 147 VTLIGALVVLFVI-DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELER 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 330 YDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETR 409
Cdd:COG1132 226 FREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 410 QALIDMNTLFTLLKVDTQIKDKvmASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIV 489
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDP--PGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 490 RLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMP 569
Cdd:COG1132 384 NLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 570 HGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADE 649
Cdd:COG1132 464 DGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543
|
570 580 590
....*....|....*....|....*....|....*
gi 411147367 650 IIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQSS 684
Cdd:COG1132 544 ILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQFG 577
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
117-418 |
3.97e-167 |
|
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: 482.00 E-value: 3.97e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 117 SLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSI 196
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLG 276
Cdd:cd18582 71 RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 277 TYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS 356
Cdd:cd18582 151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 357 AIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 418
Cdd:cd18582 231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
446-682 |
7.39e-144 |
|
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: 420.10 E-value: 7.39e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 525
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVIL 605
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 606 YDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAnPHSIYSEMWHTQ 682
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEMWKAQ 236
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
59-682 |
3.48e-139 |
|
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: 425.40 E-value: 3.48e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 59 QVWPLIEKRTCWHGHAgggLHTDPKEGLKDVDTRKI-IKAMLSYVWPkDRPDLRArvAISLGFLGGAkaMNIVVPFMFKY 137
Cdd:COG2274 110 RKLSLEEFAESWTGVA---LLLEPTPEFDKRGEKPFgLRWFLRLLRR-YRRLLLQ--VLLASLLINL--LALATPLFTQV 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 138 AVDSLnqMSGNMLNlsdapnTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLS 217
Cdd:COG2274 182 VIDRV--LPNQDLS------TLWVLAIGLLLALLFE----GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFES 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 218 RQTGALSKAIdRGTRGI-SFVLSALVFNLLPIMFevMLVSGVL--YYkcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRI 294
Cdd:COG2274 250 RSVGDLASRF-RDVESIrEFLTGSLLTALLDLLF--VLIFLIVlfFY--SPPLALVVLLLIPLYVLLGLLFQPRLRRLSR 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 295 EMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGI 374
Cdd:COG2274 325 EESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 375 VAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLkvDTQIKDKVMASPLQITPQTATVAFDNVHFE 454
Cdd:COG2274 405 IDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL--DLPPEREEGRSKLSLPRLKGDIELENVSFR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 455 YIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFH 533
Cdd:COG2274 483 YPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFS 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 534 NTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 613
Cdd:COG2274 563 GTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 614 DSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 682
Cdd:COG2274 643 DAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
102-669 |
5.90e-102 |
|
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: 324.36 E-value: 5.90e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 102 VWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMfKYAVDSLnqmsgnmLNLSDaPNTVATMAtAVLIGYGVSRAGAAFFN 181
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALL-KPLLDDG-------FGGRD-RSVLWWVP-LVVIGLAVLRGICSFVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 182 evrNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYY 261
Cdd:TIGR02203 75 ---TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTL---LSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 262 KCGAQFALvTLGTLGTYTAFTVAVTRWRTRFR---IEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYE 338
Cdd:TIGR02203 149 LLYYSWQL-TLIVVVMLPVLSILMRRVSKRLRrisKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 339 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 418
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 419 FTLLkvDTQikDKVMASPLQITPQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE 497
Cdd:TIGR02203 308 FTLL--DSP--PEKDTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 498 PQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNIS-ASPEEVYAVAKLAGLHDAILRMPHGYDTQV 576
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 577 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQG 656
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
570
....*....|...
gi 411147367 657 KVAERGTHHGLLA 669
Cdd:TIGR02203 544 RIVERGTHNELLA 556
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
446-679 |
7.44e-102 |
|
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: 311.86 E-value: 7.44e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 524
Cdd:cd03251 1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 604
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMW 679
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKLH 234
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
99-669 |
1.06e-101 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 323.58 E-value: 1.06e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 99 LSYVWPKDRPdLRARVAISLGFLGGAKAMNIVVPFMFKYAVD-SLNQMSGNMLNLSDAPNTVATMATAVLIG---YGVSR 174
Cdd:TIGR02204 6 LAALWPFVRP-YRGRVLAALVALLITAAATLSLPYAVRLMIDhGFSKDSSGLLNRYFAFLLVVALVLALGTAarfYLVTW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 175 AGAAFFNEVRNAVFGkvaqnsirriaknvflHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNL-LPIMFEVM 253
Cdd:TIGR02204 85 LGERVVADIRRAVFA----------------HLISLSPSFFDKNRSGEV---VSRLTTDTTLLQSVIGSSLsMALRNALM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 254 LVSGV-LYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDG 332
Cdd:TIGR02204 146 CIGGLiMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 333 FLKTYETASLKSTSTLAMLNfgQSAIFSV--GLTAIMVLASQGIVAGTLTVGDL-------VMVNGLLFQLSlplnflgT 403
Cdd:TIGR02204 226 AVEKAYEAARQRIRTRALLT--AIVIVLVfgAIVGVLWVGAHDVIAGKMSAGTLgqfvfyaVMVAGSIGTLS-------E 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 404 VYRETRQALIDMNTLFTLLKVDTQIKdkVMASPLQI-TPQTATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGG 480
Cdd:TIGR02204 297 VWGELQRAAGAAERLIELLQAEPDIK--APAHPKTLpVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 481 SGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAG 560
Cdd:TIGR02204 375 SGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAH 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 561 LHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHR 640
Cdd:TIGR02204 455 AHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHR 534
|
570 580
....*....|....*....|....*....
gi 411147367 641 LSTVVDADEIIVLDQGKVAERGTHHGLLA 669
Cdd:TIGR02204 535 LATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
308-670 |
1.31e-100 |
|
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: 320.55 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 308 IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKstsTLAMlNFGQSA----IFSVGLTAIMVLASQGIVAGTLTVGD 383
Cdd:COG4988 201 LDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMK---VLRV-AFLSSAvlefFASLSIALVAVYIGFRLLGGSLTLFA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 384 LVMVngLLfqLS----LPLNFLGTVYRETRQALIDMNTLFTLLkvDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQ 459
Cdd:COG4988 277 ALFV--LL--LApeffLPLRDLGSFYHARANGIAAAEKIFALL--DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYN 539
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREN 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 LLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 619
Cdd:COG4988 431 LRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEA 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 411147367 620 TILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 670
Cdd:COG4988 511 EILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
444-669 |
5.25e-100 |
|
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: 306.84 E-value: 5.25e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 444 ATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 523
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 603
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 604 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 669
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
446-682 |
8.32e-99 |
|
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: 304.08 E-value: 8.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 523
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 603
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 604 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 682
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
117-418 |
1.13e-98 |
|
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: 306.07 E-value: 1.13e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 117 SLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSI 196
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNAL----------TLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLG 276
Cdd:cd18560 71 RELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 277 TYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS 356
Cdd:cd18560 151 LYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQ 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 357 AIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 418
Cdd:cd18560 231 LIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
197-669 |
5.10e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 306.50 E-value: 5.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLLPIMFEVmlvsgvlyykcG 264
Cdd:PRK13657 87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFM-----------N 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 265 AQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKS 344
Cdd:PRK13657 156 WRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 345 TSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNTLFT 420
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEEFFE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 421 LLKVDTQIKDKVMASPLQITpqTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK 500
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRV--KGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 501 GSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERG 580
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 581 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAE 660
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
....*....
gi 411147367 661 RGTHHGLLA 669
Cdd:PRK13657 550 SGSFDELVA 558
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
233-680 |
1.31e-91 |
|
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: 297.06 E-value: 1.31e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 233 GISFVLSALVFNLLPIMFEVMLVSGVLyykcgaqfalVTLGTLGTYTAFTVAVTRWRTRFRIemnkadndagnAAIDSLL 312
Cdd:COG4987 145 AAVAFLAFFSPALALVLALGLLLAGLL----------LPLLAARLGRRAGRRLAAARAALRA-----------RLTDLLQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 313 NYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVngLLF 392
Cdd:COG4987 204 GAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL--VLA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 393 QLSL--PLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLqitPQTATVAFDNVHFEY-IEGQKVLSGISFEV 469
Cdd:COG4987 282 ALALfeALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPA---PGGPSLELEDVSFRYpGAGRPVLDGLSLTL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 470 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASP 549
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 550 EEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVV 629
Cdd:COG4987 439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL 518
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 411147367 630 KHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWH 680
Cdd:COG4987 519 AGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ-NGRYRQLYQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
187-682 |
4.85e-87 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 285.37 E-value: 4.85e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 187 VFGKVAQNsIRRiakNVFLHLHNLDLGFHLSRQTGAL-------SKAIDRGTRG--ISFVL-SALVFNLLPIMFevmlvs 256
Cdd:PRK11176 92 VSGKVVMT-MRR---RLFGHMMGMPVSFFDKQSTGTLlsritydSEQVASSSSGalITVVReGASIIGLFIMMF------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 257 gvlYYKCgaQFALVtLGTLGTYTAFTVAVTRwrTRFRIEMNKADNDAG---NAAIDSLLNYETVKYFNNERYEAQRYDGF 333
Cdd:PRK11176 162 ---YYSW--QLSLI-LIVIAPIVSIAIRVVS--KRFRNISKNMQNTMGqvtTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 334 LKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALI 413
Cdd:PRK11176 234 SNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 414 DMNTLFTLLKVDTQiKDKvmaSPLQITPQTATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL 492
Cdd:PRK11176 314 ACQTLFAILDLEQE-KDE---GKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 493 FRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYG-NISASPEEVYAVAKLAGLHDAILRMPHG 571
Cdd:PRK11176 390 TRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDNG 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 572 YDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEII 651
Cdd:PRK11176 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIL 549
|
490 500 510
....*....|....*....|....*....|.
gi 411147367 652 VLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 682
Cdd:PRK11176 550 VVEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
118-415 |
1.04e-82 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 264.49 E-value: 1.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 118 LGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGY-------GVSRAGAAFFNEVRNAVFGK 190
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSL---------TPDSADSPLAFPWALILLYvflkflqGGGSGSVGLLSNLRSFLWIP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 191 VAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALV 270
Cdd:cd18581 73 VQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 271 TLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAM 350
Cdd:cd18581 153 VFVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 351 LNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 415
Cdd:cd18581 233 LNTAQNLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDM 297
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
197-678 |
2.90e-79 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 267.74 E-value: 2.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGT----RGISFVLSALVFNLlpimfeVMLVsGVLYYKC--GAQFALV 270
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTqtmsRSLSLNVNVLLRNL------VMLL-GLLGFMLwlSPRLTMV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 271 TLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKtyETASLKSTSTLA- 349
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALE--ETLQLNKRKALAy 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 350 MLNFGQSAIFSVGL-TAIMVLASQGIVAGTLTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQALIDMNTLFTLLKVDT 426
Cdd:TIGR00958 385 AGYLWTTSVLGMLIqVLVLYYGGQLVLTGKVSSGNLVSF--LLYQEQLgeAVRVLSYVYSGMMQAVGASEKVFEYLDRKP 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 427 QIKDKVMASPLqitPQTATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIY 504
Cdd:TIGR00958 463 NIPLTGTLAPL---NLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 505 LAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLS 584
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 585 GGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKdvVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTH 664
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697
|
490
....*....|....
gi 411147367 665 HGLLANPhSIYSEM 678
Cdd:TIGR00958 698 KQLMEDQ-GCYKHL 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
446-657 |
2.44e-78 |
|
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: 248.07 E-value: 2.44e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 524
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIYYNLlygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 604
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 657
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
446-682 |
1.59e-77 |
|
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: 248.56 E-value: 1.59e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEY-IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 524
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 604
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 682
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
446-663 |
8.24e-72 |
|
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: 232.77 E-value: 8.24e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 524
Cdd:cd03244 3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIYYNL-LYGniSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 603
Cdd:cd03244 83 IPQDPVLFSGTIRSNLdPFG--EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 604 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 663
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
156-680 |
1.03e-70 |
|
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: 244.65 E-value: 1.03e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 156 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGIS 235
Cdd:TIGR01193 188 PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEI---VSRFTDASS 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 236 FV--LSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLN 313
Cdd:TIGR01193 265 IIdaLASTILSLFLDMWILVIVGLFLVRQ-NMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNG 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 314 YETVKYFNNERYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIFSV-GLTAIMVL---ASQGIVAGTLTVGDLVMVNG 389
Cdd:TIGR01193 344 IETIKSLTSEAERYSKIDSEFGDY----LNKSFKYQKADQGQQAIKAVtKLILNVVIlwtGAYLVMRGKLTLGQLITFNA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 390 LLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLqiTPQTATVAFDNVHFEYIEGQKVLSGISFEV 469
Cdd:TIGR01193 420 LLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTEL--NNLNGDIVINDVSYSYGYGSNILSDISLTI 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 470 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI-SAS 548
Cdd:TIGR01193 498 KMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNVS 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 549 PEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDv 628
Cdd:TIGR01193 578 QDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN- 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 411147367 629 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLaNPHSIYSEMWH 680
Cdd:TIGR01193 657 LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLIH 707
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
197-669 |
1.19e-70 |
|
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: 244.47 E-value: 1.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAI---DRGTRGISFVLSALVFNLLPIMFEVMLVsgVLYykcGAQFALVTLG 273
Cdd:TIGR03796 227 VGMSARFLWHILRLPVRFFAQRHAGDIASRVqlnDQVAEFLSGQLATTALDAVMLVFYALLM--LLY---DPVLTLIGIA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 274 TlgtyTAFTVAVTRWRTRFRIEMN-KADNDAG---NAAIDSLLNYETVKYFNNERYEAQRYDGflktYETASLKSTSTLA 349
Cdd:TIGR03796 302 F----AAINVLALQLVSRRRVDANrRLQQDAGkltGVAISGLQSIETLKASGLESDFFSRWAG----YQAKLLNAQQELG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 350 MLNfgqsAIFSV------GLTAIMVLASQG--IVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTL 421
Cdd:TIGR03796 374 VLT----QILGVlptlltSLNSALILVVGGlrVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDV 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 422 LK--VDTQIKDKVMASPLQITPQ--TATVAFDNVHFEY-IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFY 496
Cdd:TIGR03796 450 LRnpVDPLLEEPEGSAATSEPPRrlSGYVELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLY 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 497 EPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQV 576
Cdd:TIGR03796 530 QPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAEL 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 577 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILgamkDVVKHR--TSIFIAHRLSTVVDADEIIVLD 654
Cdd:TIGR03796 610 AEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIID----DNLRRRgcTCIIVAHRLSTIRDCDEIIVLE 685
|
490
....*....|....*
gi 411147367 655 QGKVAERGTHHGLLA 669
Cdd:TIGR03796 686 RGKVVQRGTHEELWA 700
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
446-658 |
1.66e-69 |
|
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: 226.70 E-value: 1.66e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 524
Cdd:cd03245 3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 604
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 658
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
121-418 |
8.14e-67 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 222.02 E-value: 8.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 121 LGGAKAMNIVVPFMFKYAVDSLNQMSGNMlnlsdapntvatMATAVLIgYGVSR--AGAAFFNEVRNAVFGKVAQNSIRR 198
Cdd:cd18583 5 LLAERVLNVLVPRQLGIIVDSLSGGSGKS------------PWKEIGL-YVLLRflQSGGGLGLLRSWLWIPVEQYSYRA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 199 IAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTrGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTY 278
Cdd:cd18583 72 LSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 279 TAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAI 358
Cdd:cd18583 151 VWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 359 FSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 418
Cdd:cd18583 231 LTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
360-667 |
2.36e-66 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 229.78 E-value: 2.36e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 360 SVGLTAIMVLASQGIVAGTLTVGDLVMVNG----LLFQLSLPLNFLGTVYrETRQALIDmntlFTLLKVDTQIKDKVMAS 435
Cdd:TIGR01192 251 TISMMCILVIGTVLVIKGELSVGEVIAFIGfanlLIGRLDQMSGFITQIF-EARAKLED----FFDLEDSVFQREEPADA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 436 PlQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL 515
Cdd:TIGR01192 326 P-ELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 516 ESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIAR 595
Cdd:TIGR01192 405 ESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGL 667
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
439-658 |
2.34e-65 |
|
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: 216.18 E-value: 2.34e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 439 ITPQT--ATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS 514
Cdd:cd03248 3 LAPDHlkGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 515 LESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIA 594
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 595 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 658
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
374-682 |
2.15e-61 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 216.12 E-value: 2.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 374 IVAGTLTVGDL---VMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVdtqIKDKVMASPlqitPQTATVAFDN 450
Cdd:PRK10789 246 VVNGSLTLGQLtsfVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV---VKDGSEPVP----EGRGELDVNI 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 451 VHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDA 529
Cdd:PRK10789 319 RQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 530 VLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 610 TSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPhSIYSEMWHTQ 682
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
113-653 |
1.72e-60 |
|
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: 212.53 E-value: 1.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 113 RVAISLGFLGGAkaMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATA-VLIGYG----VSRAGAAFFNEVRNAV 187
Cdd:TIGR02857 6 ALLALLGVLGAL--LIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLrALLGWLqeraAARAAAAVKSQLRERL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 188 FGKVAQNSIRRIAKnvflhlhnldlgfhlsRQTGALSKAIDRGTRGisfvLSALVFNLLPIMFEVMLVSGVLYYKCGAQ- 266
Cdd:TIGR02857 84 LEAVAALGPRWLQG----------------RPSGELATLALEGVEA----LDGYFARYLPQLVLAVIVPLAILAAVFPQd 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 267 --FALVTLGTLGTYTAFtVAVTRWRTRFRIEMN-KADNDAGNAAIDSLLNYETVKYFNNERYEAQRydgfLKTYETASLK 343
Cdd:TIGR02857 144 wiSGLILLLTAPLIPIF-MILIGWAAQAAARKQwAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA----IRRSSEEYRE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 344 ST-STLAMlNFGQSAIF------SVGLTAIMVlasqGIvagTLTVGDLVMVNGLLFQL-----SLPLNFLGTVYRETRQA 411
Cdd:TIGR02857 219 RTmRVLRI-AFLSSAVLelfatlSVALVAVYI----GF---RLLAGDLDLATGLFVLLlapefYLPLRQLGAQYHARADG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 412 LIDMNTLFTLLKVDTQI----KDKVMASPLQITpqtatvaFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKST 487
Cdd:TIGR02857 291 VAAAEALFAVLDAAPRPlagkAPVTAAPASSLE-------FSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKST 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 488 IVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILR 567
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 568 MPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA 647
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523
|
....*.
gi 411147367 648 DEIIVL 653
Cdd:TIGR02857 524 DRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
438-670 |
4.93e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 212.38 E-value: 4.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 438 QITPQTATVAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE 516
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLhDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARA 596
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 670
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
324-682 |
3.40e-59 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 210.34 E-value: 3.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 324 RYEAQRYDGFLkTYETASLKSTSTLA--MLNFGQSAifsvgltaimvlasqgivAGTLTVGDLVMVNGLLFQLSLPLNFL 401
Cdd:PRK10790 241 RMQTLRLDGFL-LRPLLSLFSALILCglLMLFGFSA------------------SGTIEVGVLYAFISYLGRLNEPLIEL 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 402 GTVYRETRQALIDMNTLFTLlkvdtqikdkvMASPLQ------ITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKV 475
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFEL-----------MDGPRQqygnddRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFV 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 476 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYG-NISAspEEVYA 554
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGrDISE--EQVWQ 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 555 VAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS 634
Cdd:PRK10790 449 ALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL 528
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 411147367 635 IFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 682
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQLQ 575
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
267-659 |
9.07e-55 |
|
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: 197.28 E-value: 9.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 267 FALVTLGTLGTYTAFTVAVTRwrtRFRIEMNKADNDAGNAAIDSLLNYETVkyfnneryEA------------QRYDGFL 334
Cdd:COG4618 160 LALVGALVLVALALLNERLTR---KPLKEANEAAIRANAFAEAALRNAEVI--------EAmgmlpalrrrwqRANARAL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 335 KTYETASLKSTSTLAML----NFGQSAIFSVGltAIMVLASQ----GIVAGTLTVG------DLVMVNGLLFQlslplnf 400
Cdd:COG4618 229 ALQARASDRAGGFSALSkflrLLLQSAVLGLG--AYLVIQGEitpgAMIAASILMGralapiEQAIGGWKQFV------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 401 lgtvyrETRQALIDMNTLFTLLKVDtqikDKVMASPlqiTPQtATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVG 479
Cdd:COG4618 300 ------SARQAYRRLNELLAAVPAE----PERMPLP---RPK-GRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIG 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 480 GSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYynllyGNIS----ASPEEVYAV 555
Cdd:COG4618 366 PSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIA-----ENIArfgdADPEKVVAA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 556 AKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSI 635
Cdd:COG4618 441 AKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATV 520
|
410 420
....*....|....*....|....*
gi 411147367 636 F-IAHRLSTVVDADEIIVLDQGKVA 659
Cdd:COG4618 521 VvITHRPSLLAAVDKLLVLRDGRVQ 545
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
329-641 |
1.10e-54 |
|
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: 196.43 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 329 RYDGFLKTYETASLKST----STLAMLNFGQSA-IFSVGLTAIMVL--ASQGIVAGTLTVGDLVMVngLLFQLSL--PLN 399
Cdd:TIGR02868 211 ALPAALAQVEEADRELTraerRAAAATALGAALtLLAAGLAVLGALwaGGPAVADGRLAPVTLAVL--VLLPLAAfeAFA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 400 FLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVG 479
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILG 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 480 GSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLA 559
Cdd:TIGR02868 369 PSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERV 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 560 GLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH 639
Cdd:TIGR02868 449 GLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
..
gi 411147367 640 RL 641
Cdd:TIGR02868 529 HL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
441-663 |
1.16e-53 |
|
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: 183.77 E-value: 1.16e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 441 PQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLR 519
Cdd:cd03369 2 PEHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 520 RAVGVVPQDAVLFHNTIYYNL-LYGNIsaSPEEVYAVAKlaglhdailrmphgydtqVGERGLKLSGGEKQRVAIARAIL 598
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 663
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
392-671 |
2.41e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 191.21 E-value: 2.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 392 FQlslPLNFLGTVYRETRQALIDMNTLFTLLKVDTQikdkvmasplqiTPQTATVAFDNVHFEYIEGQ---------KVL 462
Cdd:PRK11174 301 YQ---PLRDLGTFYHAKAQAVGAAESLVTFLETPLA------------HPQQGEKELASNDPVTIEAEdleilspdgKTL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 463 SG-ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLL 541
Cdd:PRK11174 366 AGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 542 YGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETI 621
Cdd:PRK11174 445 LGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 411147367 622 LGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
446-671 |
2.57e-51 |
|
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: 178.29 E-value: 2.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 525
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAV--LFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAI 597
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpeNLGLPREEirerVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 598 LKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
446-662 |
2.06e-49 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 170.96 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV 524
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIYYNLlygnisaspeevyavaklaglhdailrmphgydtqvgerGLKLSGGEKQRVAIARAILKDPPVI 604
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERG 662
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
448-672 |
7.90e-48 |
|
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: 168.83 E-value: 7.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGV 524
Cdd:cd03261 3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLF-HNTIYYNL---LYGNISASPEEVYAVA--KLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 596
Cdd:cd03261 82 LFQSGALFdSLTVFENVafpLREHTRLSEEEIREIVleKLEavGLRGAEDLYPA-----------ELSGGMKKRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 597 ILKDPPVILYDEATSSLDSIT----EETILgAMKDVVKHrTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIAsgviDDLIR-SLKKELGL-TSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228
|
.
gi 411147367 672 H 672
Cdd:cd03261 229 D 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
446-675 |
1.14e-47 |
|
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: 176.25 E-value: 1.14e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEY----IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESL 518
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 519 RRAVGVVPQD--AVLF-HNTIYYNL-----LYGNISAS--PEEVYAVAKLAGLHDAIL-RMPHGydtqvgerglkLSGGE 587
Cdd:COG1123 341 RRRVQMVFQDpySSLNpRMTVGDIIaeplrLHGLLSRAerRERVAELLERVGLPPDLAdRYPHE-----------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 588 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTH 664
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
250
....*....|.
gi 411147367 665 HGLLANPHSIY 675
Cdd:COG1123 490 EEVFANPQHPY 500
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
448-658 |
2.33e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.53 E-value: 2.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 527
Cdd:COG4619 3 LEGLSFR-VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLFHNTIYYNLL----YGNISASPEEVYAVAKLAGLHDAILrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPV 603
Cdd:COG4619 82 EPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 604 ILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH------RLstvvdADEIIVLDQGKV 658
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
446-672 |
5.03e-47 |
|
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: 166.69 E-value: 5.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 522
Cdd:COG1127 6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDAVLFHN-TIYYNLLYG---NISASPEEVYAVA--KLA--GLHDAILRMPhgydtqvGErglkLSGGEKQRVAIA 594
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleKLElvGLPGAADKMP-------SE----LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 595 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASD 233
|
.
gi 411147367 672 H 672
Cdd:COG1127 234 D 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
446-660 |
3.68e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.99 E-value: 3.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 522
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDA-VLFHNTIYYNLLY-----GnisASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVA 592
Cdd:COG2884 82 GVVFQDFrLLPDRTVYENVALplrvtG---KSRKEirrrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 593 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVvdaDE----IIVLDQGKVAE 660
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELV---DRmpkrVLELEDGRLVR 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
449-676 |
6.97e-45 |
|
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: 161.12 E-value: 6.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEY---IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 525
Cdd:COG1124 5 RNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVL-FH--NTIYYNL-----LYGnISASPEEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARA 596
Cdd:COG1124 85 FQDPYAsLHprHTVDRILaeplrIHG-LPDREERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANPH 672
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLAGPK 231
|
....
gi 411147367 673 SIYS 676
Cdd:COG1124 232 HPYT 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
389-713 |
7.88e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 174.16 E-value: 7.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 389 GLLfqLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIkDKVMASPLQIT--------PQTATVAFDNVHFEY-IEGQ 459
Cdd:PLN03130 1176 GLL--LSYALNITSLLTAVLRLASLAENSLNAVERVGTYI-DLPSEAPLVIEnnrpppgwPSSGSIKFEDVVLRYrPELP 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYN 539
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 LLYGNiSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 619
Cdd:PLN03130 1333 LDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 620 TILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMwhTQSSRVQNHDNPKWEA--K 697
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM--VQSTGAANAQYLRSLVfgG 1489
|
330
....*....|....*.
gi 411147367 698 KENISKEEERKKLQEE 713
Cdd:PLN03130 1490 DEDRLAREESKALDGQ 1505
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
448-657 |
2.67e-44 |
|
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: 158.01 E-value: 2.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 526
Cdd:cd03225 2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 527 QDA--VLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 598
Cdd:cd03225 82 QNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGK 657
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
345-702 |
3.08e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 172.08 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 345 TSTLAMLNFGQSAiFSVGLTAIMVLasqgIVAGTLTVGDLVmvNGLLFQLSLPLNFLGTVYRETRqaLIDMNTLFTLLKV 424
Cdd:PLN03232 1151 TATFAVLRNGNAE-NQAGFASTMGL----LLSYTLNITTLL--SGVLRQASKAENSLNSVERVGN--YIDLPSEATAIIE 1221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 425 DTQikdkvmasPLQITPQTATVAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI 503
Cdd:PLN03232 1222 NNR--------PVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 504 YLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLlygnisaSPEEVYAVAKL------AGLHDAILRMPHGYDTQVG 577
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-------DPFSEHNDADLwealerAHIKDVIDRNPFGLDAEVS 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 578 ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 657
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 411147367 658 VAERGTHHGLLANPHSIYSEMWH-TQSSRVQNHDNPKWEAKKENIS 702
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSAFFRMVHsTGPANAQYLSNLVFERRENGMS 1492
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
450-662 |
1.92e-43 |
|
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: 156.51 E-value: 1.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHF-EYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVV 525
Cdd:cd03257 8 SVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLFHN---TIYYNL---LYGNISASPEEVYAVAKLA-----GLHDAILRM-PHgydtqvgerglKLSGGEKQRVAI 593
Cdd:cd03257 88 FQDPMSSLNprmTIGEQIaepLRIHGKLSKKEARKEAVLLllvgvGLPEEVLNRyPH-----------ELSGGQRQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
449-658 |
6.88e-43 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 152.76 E-value: 6.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 527
Cdd:cd03246 4 ENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLFHNTIyynllYGNIsaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:cd03246 84 DDELFSGSI-----AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 411147367 608 EATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVDADEIIVLDQGKV 658
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
458-662 |
1.07e-42 |
|
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: 153.83 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTI 536
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFpHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 YYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEAT 610
Cdd:cd03259 90 AENIAFGlKLRGVPKAeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 611 SSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03259 159 SALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
446-673 |
1.07e-42 |
|
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: 154.77 E-value: 1.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 525
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLF-HNTIYYNL-LYGNISASPEE-----VYAVAKLAGLHDAIL--RMPHgydtqvgerglKLSGGEKQRVAIARA 596
Cdd:cd03295 81 IQQIGLFpHMTVEENIaLVPKLLKWPKEkirerADELLALVGLDPAEFadRYPH-----------ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLDQGKVAERGTHHGLLANPHS 673
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
434-678 |
1.50e-42 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 166.88 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 434 ASPLQITP---QTATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQN 509
Cdd:PTZ00243 1294 ASPTSAAPhpvQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 510 IQDVSLESLRRAVGVVPQDAVLFHNTIYYNlLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQ 589
Cdd:PTZ00243 1374 IGAYGLRELRRQFSMIPQDPVLFDGTVRQN-VDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQ 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 590 RVAIARAILK-DPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLL 668
Cdd:PTZ00243 1453 LMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
250
....*....|
gi 411147367 669 ANPHSIYSEM 678
Cdd:PTZ00243 1533 MNRQSIFHSM 1542
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
462-611 |
2.79e-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: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLF-HNTIYYNL 540
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 541 LYGnisASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATS 611
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
446-662 |
3.86e-42 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 152.72 E-value: 3.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESL 518
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 519 RRAVGVVPQDAVLFHNTIYYNLLYG-------NISASPEEVYAVAKLAGLHDAILRMPHGydtqvgergLKLSGGEKQRV 591
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHA---------LGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH------RLstvvdADEIIVLDQGKVAERG 662
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
446-663 |
2.47e-41 |
|
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: 151.81 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVG 523
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 595
Cdd:TIGR04520 81 MVFQnpDNQFVGATVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 663
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
446-669 |
2.62e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.60 E-value: 2.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEsLRRAVGVV 525
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLFHN-TIYYNL-----LYG-NISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAIL 598
Cdd:COG1131 79 PQEPALYPDlTVRENLrffarLYGlPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLA 669
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
446-671 |
3.10e-41 |
|
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: 150.42 E-value: 3.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 519
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 520 RAVGVVPQdavlfhntiYYNLL-----YGNI-----------SASPEEVYAVAKLAGLHDAIlrmpHGYDTQvgerglkL 583
Cdd:cd03258 82 RRIGMIFQ---------HFNLLssrtvFENValpleiagvpkAEIEERVLELLELVGLEDKA----DAYPAQ-------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 584 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 660
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
250
....*....|.
gi 411147367 661 RGTHHGLLANP 671
Cdd:cd03258 222 EGTVEEVFANP 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
446-671 |
5.71e-41 |
|
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: 157.37 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 521
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQD--AVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 593
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLAN 670
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
.
gi 411147367 671 P 671
Cdd:COG1123 234 P 234
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
392-676 |
6.95e-41 |
|
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: 161.65 E-value: 6.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 392 FQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMAS-PLQITPQTATVAFDNVHFEYIEGQK-VLSGISFEV 469
Cdd:TIGR00957 1230 LQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETaPPSGWPPRGRVEFRNYCLRYREDLDlVLRHINVTI 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 470 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL-LYGniSAS 548
Cdd:TIGR00957 1310 HGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS--QYS 1387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 549 PEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDV 628
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 411147367 629 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYS 676
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
446-673 |
1.06e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.99 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAVG 523
Cdd:COG1126 2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQDAVLF-HNTIYYNLLYGNISA---SPEEVYAVAK--LA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 595
Cdd:COG1126 81 MVFQQFNLFpHLTVLENVTLAPIKVkkmSKAEAEERAMelLErvGLADKADAYPA-----------QLSGGQQQRVAIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 596 AILKDPPVILYDEATSSLD--SITEetILGAMKDVVK-HRTSIFIAHRLS---TVvdADEIIVLDQGKVAERGTHHGLLA 669
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDpeLVGE--VLDVMRDLAKeGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFFE 225
|
....
gi 411147367 670 NPHS 673
Cdd:COG1126 226 NPQH 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
448-657 |
1.42e-40 |
|
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: 146.56 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES--LRRAVGVV 525
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLF-HNTIYYNLLYGnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 604
Cdd:cd03229 82 FQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGK 657
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
151-677 |
5.77e-40 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 159.04 E-value: 5.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 151 NLSDAPNTVATMATAVLIGYGVSRAGAAFFNevrNAVFGKVAQNSIRRIAKNVFLHlhnlDLGF--HLSRQTGALSKAID 228
Cdd:PTZ00265 860 NLEANSNKYSLYILVIAIAMFISETLKNYYN---NVIGEKVEKTMKRRLFENILYQ----EISFfdQDKHAPGLLSAHIN 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 229 RGtrgISFVLSALVFNLLPIMFEVML--VSGVL-YYKCGAQFALVTlgtlGTYTAFT-VAVTRWRTRFRIEMNKAD-NDA 303
Cdd:PTZ00265 933 RD---VHLLKTGLVNNIVIFTHFIVLflVSMVMsFYFCPIVAAVLT----GTYFIFMrVFAIRARLTANKDVEKKEiNQP 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 304 GNAAI----------------DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAML-NFGQSAIFSVGLTAI 366
Cdd:PTZ00265 1006 GTVFAynsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLwGFSQSAQLFINSFAY 1085
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 367 MvLASQGIVAGTLTVGDLVMVnglLFQLSLPLNFLGTVYR---ETRQALIDMNTLFTLL--KVDTQIKDKVMASPLQITP 441
Cdd:PTZ00265 1086 W-FGSFLIRRGTILVDDFMKS---LFTFLFTGSYAGKLMSlkgDSENAKLSFEKYYPLIirKSNIDVRDNGGIRIKNKND 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 442 QTATVAFDNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE---------------------- 497
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 498 --------------------------------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI 545
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 546 SASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 625
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 626 KDVVKH--RTSIFIAHRLSTVVDADEIIVLDQGK-----VAERGTHHGLLANPHSIYSE 677
Cdd:PTZ00265 1402 VDIKDKadKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKK 1460
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
446-660 |
6.24e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 6.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 519
Cdd:COG1136 5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 520 R-AVGVVPQdavlFHN-----TIYYN----LLYGNISAS--PEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 587
Cdd:COG1136 85 RrHIGFVFQ----FFNllpelTALENvalpLLLAGVSRKerRERARELLERVGLGDRLDHRPS-----------QLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 588 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAE 660
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
443-663 |
1.01e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.44 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 443 TATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 521
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 593
Cdd:PRK13632 85 IGIIFQnpDNQFIGATVEDDIAFGleNKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 663
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
441-707 |
1.22e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 157.88 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 441 PQTATVAFDNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA-GQNIQDVSLES 517
Cdd:PTZ00265 378 KDIKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKW 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 518 LRRAVGVVPQDAVLFHNTIYYNLLYG----------------NISASPE------------------------------- 550
Cdd:PTZ00265 458 WRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliem 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 551 ----------EVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 620
Cdd:PTZ00265 538 rknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 621 ILGAMKDVV--KHRTSIFIAHRLSTVVDADEIIVL------------------------------DQGK----------- 657
Cdd:PTZ00265 618 VQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDDNnnnnnnnnnki 697
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 658 ------VAERGTHHGLLANPHSIYSEMWHTQ---SSRVQNHDNPKWEAKKENISKEEER 707
Cdd:PTZ00265 698 nnagsyIIEQGTHDALMKNKNGIYYTMINNQkvsSKKSSNNDNDKDSDMKSSAYKDSER 756
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
448-657 |
4.77e-39 |
|
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: 141.61 E-value: 4.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 527
Cdd:cd00267 2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 davlfhntiyynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 411147367 608 EATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDA-DEIIVLDQGK 657
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
446-658 |
1.63e-38 |
|
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: 142.24 E-value: 1.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEG---QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 519
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 520 RA-VGVVPQdavlFHN-----TIYYN-----LLYGNISASPEE-VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 587
Cdd:cd03255 81 RRhIGFVFQ----SFNllpdlTALENvelplLLAGVPKKERRErAEELLERVGLGDRLNHYPS-----------ELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 588 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKV 658
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
446-657 |
2.91e-38 |
|
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: 141.07 E-value: 2.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrra 521
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQDAVLFHNTIYYNLLYGnisaSP--EEVY-AVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 598
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG----KPfdEERYeKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 599 KDPPVILYDEATSSLDS-----ITEETILGAMKDvvkHRTSIFIAHRLSTVVDADEIIVLDQGK 657
Cdd:cd03250 144 SDADIYLLDDPLSAVDAhvgrhIFENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
461-673 |
5.83e-37 |
|
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: 138.62 E-value: 5.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 539
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 LLYG------NISASPEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 613
Cdd:cd03299 92 IAYGlkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 614 DSITEETILGAMKDVVKHR--TSIFIAHRLSTV-VDADEIIVLDQGKVAERGTHHGLLANPHS 673
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
449-662 |
1.67e-36 |
|
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: 135.26 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQd 528
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 avlfhntiyynllygnisaspeevyaVAKLAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDE 608
Cdd:cd03214 81 --------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 609 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
442-677 |
2.06e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.23 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 442 QTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRA 521
Cdd:COG3842 2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRV 591
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlrmrgvpkaEIRARVAELLELVGLEGLAD---RYPH-----------QLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHrlstvvD-------ADEIIVLDQGKVAERG 662
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH------DqeealalADRIAVMNDGRIEQVG 218
|
250
....*....|....*
gi 411147367 663 ThhgllanPHSIYSE 677
Cdd:COG3842 219 T-------PEEIYER 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
446-661 |
2.13e-36 |
|
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: 136.45 E-value: 2.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrRAV 522
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDAVLF-HNTIYYNLLYG----NISASP--EEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 595
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALGlelqGVPKAEarERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQ--GKVAER 661
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
446-658 |
2.67e-36 |
|
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: 135.74 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--QDVSLESLRRAVG 523
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQDAVLF-HNTIYYNLLYGNISA---SPEEVYAVA----KLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 595
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLAPIKVkgmSKAEAEERAlellEKVGLADKADAYPA-----------QLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
450-671 |
4.09e-36 |
|
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: 138.65 E-value: 4.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYIEGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLR----RA 521
Cdd:COG0444 8 KVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQD-----------------AVLFHNtiyynllygniSASPEEVYAVA----KLAGLHDAILRM---PHgydtQvg 577
Cdd:COG0444 88 IQMIFQDpmtslnpvmtvgdqiaePLRIHG-----------GLSKAEARERAiellERVGLPDPERRLdryPH----E-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 578 erglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTS-IFIAHRLSTVVD-ADEIIVLD 654
Cdd:COG0444 151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAiLFITHDLGVVAEiADRVAVMY 225
|
250
....*....|....*..
gi 411147367 655 QGKVAERGTHHGLLANP 671
Cdd:COG0444 226 AGRIVEEGPVEELFENP 242
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
449-663 |
5.89e-36 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 136.33 E-value: 5.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ- 527
Cdd:COG1120 5 ENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 ----------DAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDaiLRmphgyDTQVGErglkLSGGEKQRVAIARAI 597
Cdd:COG1120 84 ppapfgltvrELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEH--LA-----DRPVDE----LSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 598 LKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 663
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
446-658 |
2.12e-35 |
|
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: 133.30 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLESLRRAV 522
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDA-VLFHNTIYYNLLYGN--ISASPEE----VYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIAR 595
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFALevTGVPPREirkrVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA--DEIIVLDQGKV 658
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
441-660 |
2.41e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.06 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 441 PQTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRR 520
Cdd:COG1121 2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 521 AVGVVPQdavlfHNTIYYNL-----------LYGNISASP-------EEVYAVAKLAGLHDaiLRmphgyDTQVGErglk 582
Cdd:COG1121 76 RIGYVPQ-----RAEVDWDFpitvrdvvlmgRYGRRGLFRrpsradrEAVDEALERVGLED--LA-----DRPIGE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 583 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAE 660
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
458-658 |
2.69e-35 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 131.75 E-value: 2.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLfhntiY 537
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSL-----Y 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLlygnisaSPEEVyavaklaglhdailrmphgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 617
Cdd:cd03230 86 ENL-------TVREN----------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 411147367 618 EETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKV 658
Cdd:cd03230 131 RREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
446-658 |
2.76e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.03 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 522
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDavlfHN-----TIYYNLLYGNISA-----------SPEEV-YAVAKLA--GLHDAILRmphgydtqvgeRGLKL 583
Cdd:COG3638 83 GMIFQQ----FNlvprlSVLTNVLAGRLGRtstwrsllglfPPEDReRALEALErvGLADKAYQ-----------RADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 584 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRV 225
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
114-398 |
3.86e-35 |
|
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: 134.69 E-value: 3.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQmsgnmlNLSDAPNTVATMATAVLIGYgvsrAGAAFFNEVRNAVFGKVAQ 193
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLP------DGDPETQALNVYSLALLLLG----LAQFILSFLQSYLLNHTGE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLG 273
Cdd:pfam00664 71 RLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 274 TLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNF 353
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 411147367 354 GQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPL 398
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
446-673 |
1.21e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 134.82 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 519
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 520 RAVGVVPQdavlfHntiyYNLL-----YGNIsASPEEVYAVAK---------------LAGLHDAilrmphgYDTQvger 579
Cdd:COG1135 82 RKIGMIFQ-----H----FNLLssrtvAENV-ALPLEIAGVPKaeirkrvaellelvgLSDKADA-------YPSQ---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 580 glkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQG 656
Cdd:COG1135 141 ---LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRiCDRVAVLENG 217
|
250
....*....|....*..
gi 411147367 657 KVAERGTHHGLLANPHS 673
Cdd:COG1135 218 RIVEQGPVLDVFANPQS 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
446-676 |
4.14e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.41 E-value: 4.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 524
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLAgLHDAILRMPHGYDTQvgerglKLSGGEKQRVAIARAILKD 600
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 601 PPVILYDEATSSLDSITEETILGAMKDV--VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGThhgllanPHSIYS 676
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT-------PTEIFD 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
465-671 |
4.57e-34 |
|
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: 133.70 E-value: 4.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 539
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 LLYGNISASPEEVYAVaklaglHDAILRMpHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 619
Cdd:TIGR02142 96 LRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 620 TILGAMKDVVKHRT--SIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:TIGR02142 169 EILPYLERLHAEFGipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
114-415 |
1.00e-33 |
|
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: 131.13 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFFnevRNAVFGKVAQ 193
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV---------IPAGDLSLLLWIALLLLLLALLRALLSYL---RRYLAARLGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLG 273
Cdd:cd07346 69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL-NWKLTLVALL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 274 TLgtytAFTVAVTRW-----RTRFRIEMNKADNDAGNAAiDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTL 348
Cdd:cd07346 148 LL----PLYVLILRYfrrriRKASREVRESLAELSAFLQ-ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLS 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 349 AMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 415
Cdd:cd07346 223 ALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
448-663 |
3.09e-33 |
|
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: 128.07 E-value: 3.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAVGV 524
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDavlfHN-----TIYYNLLYGNISASPeevyavaklagLHDAILRMPHGYDTQ--------VG------ERGLKLSG 585
Cdd:cd03256 83 IFQQ----FNlierlSVLENVLSGRLGRRS-----------TWRSLFGLFPKEEKQralaalerVGlldkayQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 586 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227
|
.
gi 411147367 663 T 663
Cdd:cd03256 228 P 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
440-660 |
4.51e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.28 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 440 TPQTATVAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvslE 516
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----T 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRAVGVVPQDAVLF-HNTIYYNLLYG--NISASPEEVYAVA----KLAGLHDAILRMPHgydtQvgerglkLSGGEKQ 589
Cdd:COG1116 77 GPGPDRGVVFQEPALLpWLTVLDNVALGleLRGVPKAERRERArellELVGLAGFEDAYPH----Q-------LSGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 590 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAH------RLstvvdADEIIVLDQ--GKVA 659
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220
|
.
gi 411147367 660 E 660
Cdd:COG1116 221 E 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
449-663 |
4.76e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 4.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 527
Cdd:PRK13635 9 EHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 --DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 599
Cdd:PRK13635 89 npDNQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 600 DPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 663
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
449-658 |
4.77e-33 |
|
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: 126.22 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvSLESLRRAVGVVPQD 528
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 A--VLFHNTIYYNLLYGN--ISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI 604
Cdd:cd03226 80 VdyQLFTDSVREELLLGLkeLDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKHRTSIF-IAHR---LSTVvdADEIIVLDQGKV 658
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIvITHDyefLAKV--CDRVLLLANGAI 204
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
458-671 |
6.85e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.56 E-value: 6.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--------QDVSLESLRRAVGVVPQDA 529
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 530 VLF-HNTIYYNLLYGNISASPE----------EVYAVAKLAGLHDAILRmphgydtqvgerglKLSGGEKQRVAIARAIL 598
Cdd:PRK11264 95 NLFpHRTVLENIIEGPVIVKGEpkeeatararELLAKVGLAGKETSYPR--------------RLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
448-659 |
1.61e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 124.95 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRRAVGVVPQ 527
Cdd:cd03235 2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 -------------DAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRmphgydtQVGErglkLSGGEKQRVAIA 594
Cdd:cd03235 76 rrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 595 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 659
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
446-677 |
1.65e-32 |
|
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: 125.81 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVV 525
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLF-HNTIYYNLLYG------NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 598
Cdd:cd03300 78 FQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVvkHR----TSIFIAHRLS-TVVDADEIIVLDQGKVAERGThhgllanPHS 673
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRL--QKelgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT-------PEE 217
|
....
gi 411147367 674 IYSE 677
Cdd:cd03300 218 IYEE 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
465-675 |
2.08e-32 |
|
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: 126.60 E-value: 2.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQDAVLF-HNTIYYN 539
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 LLYG-NISASPEEV-YAVA----KLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSL 613
Cdd:cd03294 123 VAFGlEVQGVPRAErEERAaealELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 614 DSiteeTILGAMKDVV------KHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 675
Cdd:cd03294 192 DP----LIRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
449-663 |
5.82e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.93 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAV 522
Cdd:PRK13637 6 ENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHdailrmphgYDTQVGERGLKLSGGEKQRVAIA 594
Cdd:PRK13637 86 GLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEienrVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 595 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 663
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
460-675 |
1.55e-31 |
|
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: 129.80 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKST----IVRLLfrfyePQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD---- 528
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfgs 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 ---------------AVLFhntiyynllygnISASPEEVYA-VAKL---AGLH-DAILRMPHgydtqvgerglKLSGGEK 588
Cdd:COG4172 375 lsprmtvgqiiaeglRVHG------------PGLSAAERRArVAEAleeVGLDpAARHRYPH-----------EFSGGQR 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 589 QRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLStVVDA--DEIIVLDQGKVAERGTH 664
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPT 510
|
250
....*....|.
gi 411147367 665 HGLLANPHSIY 675
Cdd:COG4172 511 EQVFDAPQHPY 521
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
465-662 |
1.62e-31 |
|
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: 122.40 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 539
Cdd:cd03297 17 IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 LLYGNISASPEE----VYAVAKLAGLhdailrmphgydTQVGERG-LKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:cd03297 96 LAFGLKRKRNREdrisVDELLDLLGL------------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 411147367 615 SITEETILGAMKDVVK--HRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
460-677 |
2.05e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 125.23 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLfhN 534
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDpyASL--N 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 ---TIyynllyGNISASPEEVYAVAKLAGLHDAILRM--------------PHgydtqvgerglKLSGGEKQRVAIARAI 597
Cdd:COG4608 110 prmTV------GDIIAEPLRIHGLASKAERRERVAELlelvglrpehadryPH-----------EFSGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 598 LKDPPVILYDEATSSLD-SItEETILGAMKDVVKHR--TSIFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANPH 672
Cdd:COG4608 173 ALNPKLIVCDEPVSALDvSI-QAQVLNLLEDLQDELglTYLFISHDLS-VVRhiSDRVAVMYLGKIVEIAPRDELYARPL 250
|
....*
gi 411147367 673 SIYSE 677
Cdd:COG4608 251 HPYTQ 255
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
460-675 |
3.04e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.26 E-value: 3.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAVGVVPQDAVLF-HNTIYY 538
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQHYALFpHMTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 539 NLLYG--NISASPEEVYAVA-------KLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:COG1118 95 NIAFGlrVRPPSKAEIRARVeellelvQLEGLAD---RYPS-----------QLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 610 TSSLDSITEETILGAMKDVVK--HRTSIFIAH------RLstvvdADEIIVLDQGKVAERGTHHGLLANPHSIY 675
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRPATPF 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
433-622 |
3.99e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.45 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 433 MASPLQITPQTATVafDNVHFEYieGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLA 506
Cdd:COG1117 1 MTAPASTLEPKIEV--RNLNVYY--GDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 507 GQNI--QDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGnisaspeevyavAKLAGLH-----DAI----LRmphgydtQ 575
Cdd:COG1117 77 GEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYG------------LRLHGIKskselDEIveesLR-------K 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 576 VG----------ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT----EETIL 622
Cdd:COG1117 138 AAlwdevkdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELIL 198
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
448-673 |
8.41e-31 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.76 E-value: 8.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRA 521
Cdd:PRK11153 4 LKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQdavlfHntiyYNLL-----YGNIsASPEEVYAVAK------------LAGL---HDAilrmphgYDTQvgergl 581
Cdd:PRK11153 84 IGMIFQ-----H----FNLLssrtvFDNV-ALPLELAGTPKaeikarvtelleLVGLsdkADR-------YPAQ------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 582 kLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLStVVD--ADEIIVLDQGK 657
Cdd:PRK11153 141 -LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMD-VVKriCDRVAVIDAGR 218
|
250
....*....|....*.
gi 411147367 658 VAERGTHHGLLANPHS 673
Cdd:PRK11153 219 LVEQGTVSEVFSHPKH 234
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
461-676 |
1.83e-30 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 120.78 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 540
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 541 lYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 620
Cdd:cd03288 116 -DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 621 ILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYS 676
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
444-662 |
2.02e-30 |
|
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: 118.42 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 444 ATVAFDNV-----HFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSIYLAGQNIqdvSLE 516
Cdd:cd03213 2 VTLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRAVGVVPQDAVLF-HNTIYYNLLYgnisaspeevyaVAKLAGLhdailrmphgydtqvgerglklSGGEKQRVAIAR 595
Cdd:cd03213 79 SFRKIIGYVPQDDILHpTLTVRETLMF------------AAKLRGL----------------------SGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIAHRLSTVV--DADEIIVLDQGKVAERG 662
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
449-670 |
5.87e-30 |
|
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: 117.92 E-value: 5.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES-LRRAVGVVPQ 527
Cdd:cd03224 4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLFHN-TIYYNLLYG-------NISASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRV 591
Cdd:cd03224 83 GRRIFPElTVEENLLLGayarrraKRKARLERVYELfprlkerrKQLAGT---------------------LSGGEQQML 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI----AHRLSTVvdADEIIVLDQGKVAERGTHHGL 667
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219
|
...
gi 411147367 668 LAN 670
Cdd:cd03224 220 LAD 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
394-704 |
9.45e-30 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 126.98 E-value: 9.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 394 LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTAtVAFDNVHFEYIEGQK-VLSGISFEVPAG 472
Cdd:TIGR00957 586 LRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNS-ITVHNATFTWARDLPpTLNGITFSIPEG 664
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 473 KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslrrAVGVVPQDAVLFHNTIYYNLLYGNiSASPEEV 552
Cdd:TIGR00957 665 ALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK-ALNEKYY 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 553 YAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE----ETILGAMkDV 628
Cdd:TIGR00957 731 QQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhifEHVIGPE-GV 809
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 629 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKE 704
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKE 885
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
450-712 |
1.22e-29 |
|
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: 118.80 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQD 528
Cdd:cd03289 7 DLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 AVLFHNTIYYNL-LYGniSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:cd03289 86 VFIFSGTFRKNLdPYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 608 EATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRV- 686
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLf 243
|
250 260
....*....|....*....|....*....
gi 411147367 687 -QNHDNPKWEAKKENIS--KEEERKKLQE 712
Cdd:cd03289 244 pRRNSSKSKRKPRPQIQalQEETEEEVQD 272
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
444-663 |
1.92e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.18 E-value: 1.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 444 ATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVG 523
Cdd:COG3839 2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQDAVLF-HNTIYYNLLYG--NISASPEE----VYAVAKLAGLhDAIL-RMPhgydtqvgergLKLSGGEKQRVAIAR 595
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEidrrVREAAELLGL-EDLLdRKP-----------KQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVvkHR----TSIFIAHrlstvvD-------ADEIIVLDQGKVAERGT 663
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL--HRrlgtTTIYVTH------DqveamtlADRIAVMNDGRIQQVGT 217
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
446-673 |
2.58e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.73 E-value: 2.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNV--HFeyieGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRR 520
Cdd:PRK09493 2 IEFKNVskHF----GPtQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 521 AVGVVPQDAVLF-HNTIYYNLLYGNI---SASPEEVYAVAK--LA--GLHDailRMPHgYDTQvgerglkLSGGEKQRVA 592
Cdd:PRK09493 78 EAGMVFQQFYLFpHLTALENVMFGPLrvrGASKEEAEKQARelLAkvGLAE---RAHH-YPSE-------LSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 593 IARAILKDPPVILYDEATSSLDSITEETILGAMKD---------VVKHRtsIFIAHRLSTvvdadEIIVLDQGKVAERGT 663
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlaeegmtmvIVTHE--IGFAEKVAS-----RLIFIDKGRIAEDGD 219
|
250
....*....|
gi 411147367 664 HHGLLANPHS 673
Cdd:PRK09493 220 PQVLIKNPPS 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
465-671 |
4.22e-29 |
|
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: 119.44 E-value: 4.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRL---LFRfyePQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTI 536
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFpHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 YYNLLYG----NISASPEEVYAVAKLAGLhDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATS 611
Cdd:COG4148 95 RGNLLYGrkraPRAERRISFDEVVELLGI-GHLLdRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 612 SLDSITEETILGAMKDvVKHRTSI---FIAH------RLstvvdADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:COG4148 163 ALDLARKAEILPYLER-LRDELDIpilYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
460-671 |
7.92e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.76 E-value: 7.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVpqdavlFHNTi 536
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIV------FQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 yYNLL-----YGNISASP-------------EEVYAVAKLAGL---HDAilRMPHGYdtqvgerglklSGGEKQRVAIAR 595
Cdd:PRK11308 102 -YGSLnprkkVGQILEEPllintslsaaerrEKALAMMAKVGLrpeHYD--RYPHMF-----------SGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTS-IFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
449-671 |
8.53e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.37 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 528
Cdd:PRK13647 8 EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 A--VLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 600
Cdd:PRK13647 88 PddQVFSSTVWDDVAFGpvNMGLDKDEverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 601 PPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHgLLANP 671
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTDE 228
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
462-673 |
8.83e-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: 115.13 E-value: 8.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNL 540
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 541 LYG-------------NISASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:cd03296 96 AFGlrvkprserppeaEIRAKVHELLKLVQLDWLAD---RYPA-----------QLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 608 EATSSLDS-ITEE--TILGAMKDVVkHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHS 673
Cdd:cd03296 162 EPFGALDAkVRKElrRWLRRLHDEL-HVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
458-659 |
1.06e-28 |
|
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: 112.52 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQdavlfhnti 536
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 yynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSI 616
Cdd:cd03216 83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 411147367 617 TEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 659
Cdd:cd03216 117 EVERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
469-662 |
1.08e-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: 114.13 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 469 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQDAVLF-HNTIYYNLLYG---N 544
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLFQENNLFaHLTVEQNVGLGlspG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 545 ISASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETI 621
Cdd:cd03298 99 LKLTAEDRQAIEVALarvGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 411147367 622 LGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03298 168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
448-671 |
2.49e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.70 E-value: 2.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYieGQKVLSgISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQ 527
Cdd:COG3840 4 LDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLF-HNTIYYNLLYG---NISASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 600
Cdd:COG3840 79 ENNLFpHLTVAQNIGLGlrpGLKLTAEQRAQVEQALervGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 601 PPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
446-662 |
4.09e-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: 112.35 E-value: 4.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAVGVV 525
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLF-HNTIYYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 598
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlKLRKVPKDeiderVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVLDQGKVAERG 662
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
306-670 |
5.26e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 121.24 E-value: 5.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 306 AAIDSLLNYETVKYFNNeRYEAQRYDGfLKTYETASLKSTSTLAMLNfgqsaifsvGLTAIMVLASQGIVagTLTVGDLV 385
Cdd:PLN03232 487 ASMDTVKCYAWEKSFES-RIQGIRNEE-LSWFRKAQLLSAFNSFILN---------SIPVVVTLVSFGVF--VLLGGDLT 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 386 MVNGL----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDtqikDKVMASPLQITPQTATVAFDNVHFEYIE--G 458
Cdd:PLN03232 554 PARAFtslsLFAvLRSPLNMLPNLLSQVVNANVSLQRIEELLLSE----ERILAQNPPLQPGAPAISIKNGYFSWDSktS 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 459 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkgsiylagqnIQDVSLEsLRRAVGVVPQDAVLFHNTIYY 538
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVV-IRGSVAYVPQVSWIFNATVRE 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 539 NLLYGNISASPEEVYAVAKLAGLHDaiLRMPHGYD-TQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDS-I 616
Cdd:PLN03232 698 NILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhV 775
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 411147367 617 TEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 670
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
356-670 |
5.46e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.38 E-value: 5.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 356 SAIFSVGLTAIMVLA---SQGIVagTLTVGDLVMVNGL----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDtq 427
Cdd:PLN03130 523 SAFNSFILNSIPVLVtvvSFGVF--TLLGGDLTPARAFtslsLFAvLRFPLFMLPNLITQAVNANVSLKRLEELLLAE-- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 428 ikDKVMASPLQITPQTATVAFDNVHFEY-IEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL 505
Cdd:PLN03130 599 --ERVLLPNPPLEPGLPAISIKNGYFSWdSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 506 agqniqdvslesLRRAVGVVPQDAVLFHNTIYYNLLYGNiSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSG 585
Cdd:PLN03130 677 ------------IRGTVAYVPQVSWIFNATVRDNILFGS-PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISG 743
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 586 GEKQRVAIARAILKDPPVILYDEATSSLDS-ITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTH 664
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTY 823
|
....*.
gi 411147367 665 HGLLAN 670
Cdd:PLN03130 824 EELSNN 829
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
308-712 |
5.88e-27 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 118.09 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 308 IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLA------SQGIVAGTLTV 381
Cdd:TIGR01271 1068 ITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAigtnqdGEGEVGIILTL 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 382 GDLVM------------VNGLLFQLSLPLNFLGTVYRETR-QALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVaf 448
Cdd:TIGR01271 1148 AMNILstlqwavnssidVDGLMRSVSRVFKFIDLPQEEPRpSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTA-- 1225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 dnvhfEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQ 527
Cdd:TIGR01271 1226 -----KYTEaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQ 1299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLFHNTIYYNLlYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:TIGR01271 1300 KVFIFSGTFRKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLD 1378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 608 EATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLaNPHSIYSEMWhTQSSRVQ 687
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAM-SAADRLK 1456
|
410 420 430
....*....|....*....|....*....|.
gi 411147367 688 ----NHDNPKWEAKKENIS--KEEERKKLQE 712
Cdd:TIGR01271 1457 lfplHRRNSSKRKPQPKITalREEAEEEVQN 1487
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
429-677 |
1.14e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.35 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 429 KDKVMASPLQITPqtaTVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ 508
Cdd:PRK09452 1 SKKLNKQPSSLSP---LVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 509 NIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAVAKLAGLHDailRMPHgydtqvge 578
Cdd:PRK09452 77 DITHVPAE--NRHVNTVFQSYALFpHMTVFENVAFGlrmqktpaaEITPRVMEALRMVQLEEFAQ---RKPH-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 579 rglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSiteeTILGAMKDVVKH--R----TSIFIAH----RLSTvvdAD 648
Cdd:PRK09452 144 ---QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY----KLRKQMQNELKAlqRklgiTFVFVTHdqeeALTM---SD 213
|
250 260
....*....|....*....|....*....
gi 411147367 649 EIIVLDQGKVAERGThhgllanPHSIYSE 677
Cdd:PRK09452 214 RIVVMRDGRIEQDGT-------PREIYEE 235
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
446-671 |
1.24e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.08 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGV 524
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 596
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRAlaeiGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
461-672 |
1.92e-26 |
|
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: 108.15 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL-RRAVGVVPQDAVLFHN-TIYY 538
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 539 NLLYG--------NISASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPP 602
Cdd:COG0410 98 NLLLGayarrdraEVRADLERVYELfprlkerrRQRAGT---------------------LSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 603 VILYDEATSSLD-SITEEtILGAMKDVVKHRTSIFI----AHRLSTVvdADEIIVLDQGKVAERGTHHGLLANPH 672
Cdd:COG0410 157 LLLLDEPSLGLApLIVEE-IFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
450-673 |
2.18e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.90 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV-------------SLE 516
Cdd:PRK10619 10 DLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRAVGVVPQDAVLF-HNTIYYNLLygnisASPEEVYAVAKLAGLHDAILRMPH-GYDTQV-GERGLKLSGGEKQRVAI 593
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWsHMTVLENVM-----EAPIQVLGLSKQEARERAVKYLAKvGIDERAqGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
..
gi 411147367 672 HS 673
Cdd:PRK10619 244 QS 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
449-677 |
2.26e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQK-----VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAV 522
Cdd:PRK13633 8 KNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQ--DAVLFHNTIYYNLLYG--NISASPEEV-----YAVAKLaGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 593
Cdd:PRK13633 88 GMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIrervdESLKKV-GMYEYRRHAPH-----------LLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAERGThhgllanP 671
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT-------P 228
|
....*.
gi 411147367 672 HSIYSE 677
Cdd:PRK13633 229 KEIFKE 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
445-678 |
3.92e-26 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 113.24 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 445 TVAFDNVHFEyiegQKVLSGISFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRR 520
Cdd:COG4172 13 SVAFGQGGGT----VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 521 ----AVGVVPQDA----------------VLfhntiyynLLYGNISASPEEVYAVAKLA--GLHDAILRM---PHgydtq 575
Cdd:COG4172 89 irgnRIAMIFQEPmtslnplhtigkqiaeVL--------RLHRGLSGAAARARALELLErvGIPDPERRLdayPH----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 576 vgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSI-FIAHRLSTVVD-ADEIIV 652
Cdd:COG4172 156 ------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALlLITHDLGVVRRfADRVAV 229
|
250 260
....*....|....*....|....*.
gi 411147367 653 LDQGKVAERGTHHGLLANPHSIYSEM 678
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAPQHPYTRK 255
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
441-625 |
3.95e-26 |
|
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: 107.52 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 441 PQTATVAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 517
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 518 L----RRAVGVVPQDavlFHntiyynlLYGNISASpEEVYAVAKLAGLHDA------IL-------RMPHgYDTQvgerg 580
Cdd:COG4181 84 RarlrARHVGFVFQS---FQ-------LLPTLTAL-ENVMLPLELAGRRDArararaLLervglghRLDH-YPAQ----- 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 411147367 581 lkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 625
Cdd:COG4181 147 --LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
449-662 |
4.71e-26 |
|
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: 106.51 E-value: 4.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYiEGQKVLSGISFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQD 528
Cdd:cd03264 4 ENLTKRY-GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 AVLFHN-TIYYNLLY----GNISAS--PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDP 601
Cdd:cd03264 81 FGVYPNfTVREFLDYiawlKGIPSKevKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 602 PVILYDEATSSLDSitEETI--LGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03264 150 SILIVDEPTAGLDP--EERIrfRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
458-657 |
5.18e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.02 E-value: 5.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 537
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNL-----LYGnISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSS 612
Cdd:COG4133 94 ENLrfwaaLYG-LRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 411147367 613 LDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 657
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
459-658 |
1.08e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 105.66 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 459 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLFHN-TI- 536
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 ----YYNLLYG-NISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATS 611
Cdd:cd03263 94 ehlrFYARLKGlPKSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 411147367 612 SLDSITEETILGAMKDVVKHRTSIFIAHRLSTV-VDADEIIVLDQGKV 658
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKL 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
458-672 |
1.12e-25 |
|
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: 105.98 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-T 535
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 IYYNLLYGNISASPEEVYAVAKLAGLHDA---------ILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 606
Cdd:cd03219 92 VLENVMVAAQARTGSGLLLARARREEREAreraeelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 607 DEATSSLdSITE-ETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPH 672
Cdd:cd03219 168 DEPAAGL-NPEEtEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
439-662 |
1.48e-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: 105.14 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 439 ITPQTATVAFDNVHFEYiegqKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL 518
Cdd:cd03266 2 ITADALTKRFRDVKKTV----QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 519 RRaVGVVPQDAVLF------HNTIYYNLLYGnisASPEEVYA-VAKLAGLhdaiLRMPHGYDTQVGErglkLSGGEKQRV 591
Cdd:cd03266 78 RR-LGFVSDSTGLYdrltarENLEYFAGLYG---LKGDELTArLEELADR----LGMEELLDRRVGG----FSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILgamkDVVKH-----RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALR----EFIRQlralgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
445-671 |
1.76e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 445 TVAFDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLE 516
Cdd:PRK13641 2 SIKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEvyavAKLAGLhDAILRMphGYDTQVGERG-LKLSGGEKQRV 591
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDE----AKEKAL-KWLKKV--GLSEDLISKSpFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLA 669
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
..
gi 411147367 670 NP 671
Cdd:PRK13641 235 DK 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
450-663 |
2.13e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 2.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-- 527
Cdd:PRK13652 8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLFHNTIYYNLLYGNISASPEE------VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDP 601
Cdd:PRK13652 88 DDQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 602 PVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 663
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
445-673 |
2.64e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.10 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 445 TVAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 518
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 519 RRAVGVVPQDAVLF-HNTIYYNLlygnISAsPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 591
Cdd:PRK11124 81 RRNVGMVFQQYNLWpHLTVQQNL----IEA-PCRVLGLSKDQALARAEkllerLRL-----KPYADRfPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 592 AIARAILKDPPVILYDEATSSLD--------SITEE-TILGAMKDVVKHRTSifIAHRLSTVVdadeiIVLDQGKVAERG 662
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeitaqivSIIRElAETGITQVIVTHEVE--VARKTASRV-----VYMENGHIVEQG 223
|
250
....*....|.
gi 411147367 663 THHGlLANPHS 673
Cdd:PRK11124 224 DASC-FTQPQT 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
351-661 |
4.86e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 110.28 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 351 LNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRE--TRQALIDmnTLFTLLKVDTQI 428
Cdd:COG4178 268 LTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSlaEWRATVD--RLAGFEEALEAA 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 429 KDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVR------------------ 490
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRaiaglwpygsgriarpag 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 491 --LLFRfyePQKgsIYLAgqniqdvsLESLRRAvgvvpqdavlfhntiyynLLYGNI--SASPEEVYAVAKLAGLHDAIL 566
Cdd:COG4178 426 arVLFL---PQR--PYLP--------LGTLREA------------------LLYPATaeAFSDAELREALEAVGLGHLAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 567 RMphgydTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD 646
Cdd:COG4178 475 RL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAF 549
|
330
....*....|....*
gi 411147367 647 ADEIIVLDQGKVAER 661
Cdd:COG4178 550 HDRVLELTGDGSWQL 564
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
442-653 |
6.95e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.64 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 442 QTATVAFDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 521
Cdd:PRK10247 4 NSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQDAVLFHNTIYYNLL--YGNISASPEEVYAVAKLA--GLHDAILRMPhgydtqVGErglkLSGGEKQRVAIARAI 597
Cdd:PRK10247 83 VSYCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLErfALPDTILTKN------IAE----LSGGEKQRISLIRNL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 598 LKDPPVILYDEATSSLDS----ITEETILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVL 653
Cdd:PRK10247 153 QFMPKVLLLDEITSALDEsnkhNVNEIIHRYVRE--QNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
448-671 |
7.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 7.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLESLR 519
Cdd:PRK13634 5 FQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 520 RAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAK----LAGLHDAIL-RMPhgydtqvgergLKLSGGEKQR 590
Cdd:PRK13634 85 KKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEDAKQKARemieLVGLPEELLaRSP-----------FELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 591 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGL 667
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
....
gi 411147367 668 LANP 671
Cdd:PRK13634 234 FADP 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
450-669 |
7.59e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.81 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYIEGQK--VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 527
Cdd:PRK13650 9 NLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 --DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 599
Cdd:PRK13650 89 npDNQFVGATVEDDVAFGleNKGIPHEEmkerVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 600 DPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 669
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
446-656 |
9.73e-25 |
|
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: 102.79 E-value: 9.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRA 521
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQDAVLFHNTIYYNLLYGnisaSP---EEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 598
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFG----SPfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 599 KDPPVILYDEATSSL-----DSITEETILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVLDQG 656
Cdd:cd03290 157 QNTNIVFLDDPFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
450-674 |
1.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRRAVGVVPQ 527
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 --DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 599
Cdd:PRK13639 86 npDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 600 DPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTV-VDADEIIVLDQGKVAERGTHHGLLANPHSI 674
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
446-662 |
1.18e-24 |
|
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: 103.63 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKG-SIYLAGQNIQDVSLESLRRAVGV 524
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDavlFHNTIYYNL---------LYGNI----SASPEEVYAVAKLAglhdAILRMPHGYDTQVGErglkLSGGEKQRV 591
Cdd:COG1119 83 VSPA---LQLRFPRDEtvldvvlsgFFDSIglyrEPTDEQRERARELL----ELLGLAHLADRPFGT----LSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVDA-DEIIVLDQGKVAERG 662
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
445-673 |
1.91e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.78 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 445 TVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 518
Cdd:COG4161 2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 519 RRAVGVVPQDAVLF-HNTIYYNLLygnisASPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 591
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLI-----EAPCKVLGLSKEQAREKAMkllarLRL-----TDKADRfPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 592 AIARAILKDPPVILYDEATSSLDS---------ITEETILGAMKDVVKHRTSifIAHRLstvvdADEIIVLDQGKVAERG 662
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPeitaqvveiIRELSQTGITQVIVTHEVE--FARKV-----ASQVVYMEKGRIIEQG 223
|
250
....*....|.
gi 411147367 663 THHgLLANPHS 673
Cdd:COG4161 224 DAS-HFTQPQT 233
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
449-663 |
1.92e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 103.27 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYieGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL--RRAVgvV 525
Cdd:COG4559 5 ENLSVRL--GGRtLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRAV--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLfhntiyynllygnisASPEEVYAVAKLAglhdailRMPHGYDT------------QVGERGLK------LSGGE 587
Cdd:COG4559 81 PQHSSL---------------AFPFTVEEVVALG-------RAPHGSSAaqdrqivrealaLVGLAHLAgrsyqtLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 588 KQRVAIARAIL-------KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIF-IAHRLS-TVVDADEIIVLDQGKV 658
Cdd:COG4559 139 QQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVaVLHDLNlAAQYADRILLLHQGRL 218
|
....*
gi 411147367 659 AERGT 663
Cdd:COG4559 219 VAQGT 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
466-669 |
2.34e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 102.35 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 466 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG- 543
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFsHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 544 ------NiSASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 617
Cdd:PRK10771 97 npglklN-AAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 618 EETILGAMKDVVKHR--TSIFIAHRLStvvDADEI----IVLDQGKVAERGTHHGLLA 669
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
446-663 |
2.72e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.34 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 521
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 593
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEmikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 663
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
456-663 |
2.76e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.54 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLfhnt 535
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 iyynllygNISASPEEVYAVAklaglhdailRMPHGYD------------TQVGERGLK------LSGGEKQRVAIARAI 597
Cdd:PRK13548 88 --------SFPFTVEEVVAMG----------RAPHGLSraeddalvaaalAQVDLAHLAgrdypqLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 598 L------KDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLS-TVVDADEIIVLDQGKVAERGT 663
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
440-715 |
2.96e-24 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.48 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 440 TPQTATVAFdnvhFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgqniqdvsleslr 519
Cdd:PTZ00243 659 TPKMKTDDF----FE-LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 520 RAVGVVPQDAVLFHNTIYYNLLYGNisaspEEvyavaKLAGLHDAI---------LRMPHGYDTQVGERGLKLSGGEKQR 590
Cdd:PTZ00243 721 RSIAYVPQQAWIMNATVRGNILFFD-----EE-----DAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKAR 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 591 VAIARAILKDPPVILYDEATSSLDS-----ITEETILGAMKDvvkhRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHH 665
Cdd:PTZ00243 791 VSLARAVYANRDVYLLDDPLSALDAhvgerVVEECFLGALAG----KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 411147367 666 GLLANPhsIYSEMwhtqssRVQNHDNPkwEAKKENISKEEERKKLQEEIV 715
Cdd:PTZ00243 867 DFMRTS--LYATL------AAELKENK--DSKEGDADAEVAEVDAAPGGA 906
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
458-658 |
5.87e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 5.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQDAVLFHN-T 535
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 IYYNLLYGNISASP-----EEVYAVAK--LAGLH---DAilrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 605
Cdd:COG1129 96 VAENIFLGREPRRGglidwRAMRRRARelLARLGldiDP--------DTPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 606 YDEATSSLDSiTE-ETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:COG1129 164 LDEPTASLTE-REvERLFRIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
468-658 |
1.06e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 103.03 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 468 EVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLESLRRAVGVVPQDAVLF-HNTIYYNLLY 542
Cdd:PRK11144 20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 543 GNISASPEEVYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETIL 622
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 411147367 623 GAMKDVVKH-RTSI-FIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:PRK11144 169 PYLERLAREiNIPIlYVSHSLDEILRlADRVVVLEQGKV 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
461-676 |
1.35e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN--- 534
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNSSLNprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 ----------TIYYNLLygNISASPEEVYAVAKLAGLhDAILRmpHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVI 604
Cdd:PRK15134 380 nvlqiieeglRVHQPTL--SAAQREQQVIAVMEEVGL-DPETR--HRYPAE-------FSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 605 LYDEATSSLDSITEETILGAMKDV-VKHRTS-IFIAHRLStVVDA--DEIIVLDQGKVAERGTHHGLLANPHSIYS 676
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLqQKHQLAyLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
460-672 |
1.37e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL----AGQNIQDVS------------LESLRRAVG 523
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHElitnpyskkiknFKELRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQ--DAVLFHNTIYYNLLYGNISASPEEVYAvAKLAGLHdaILRMphGYDTQVGERG-LKLSGGEKQRVAIARAILKD 600
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEA-KKLAKFY--LNKM--GLDDSYLERSpFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 601 PPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPH 672
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
465-671 |
1.57e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.68 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------------QNI----QDVSlESL--RRAVGvvp 526
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrcKHIrmifQDPN-TSLnpRLNIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 527 Q--DAVLFHNTiyyNLlygNISASPEEVYAVAKLAGLH-DAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 603
Cdd:COG4167 108 QilEEPLRLNT---DL---TAEEREERIFATLRLVGLLpEHANFYPH-----------MLSSGQKQRVALARALILQPKI 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 604 ILYDEATSSLDSITEETILGAMKDV-VKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:COG4167 171 IIADEALAALDMSVRSQIINLMLELqEKLGISyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANP 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
459-660 |
3.40e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.76 E-value: 3.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 459 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVPQD---AVLF 532
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDsisAVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 533 HNTIyynllyGNISASP-------------EEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARAIL 598
Cdd:PRK10419 105 RKTV------REIIREPlrhllsldkaerlARASEMLRAVDLDDSVLdKRPP-----------QLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDvVKHRTSI---FIAHRLSTVVD-ADEIIVLDQGKVAE 660
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKK-LQQQFGTaclFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
446-666 |
4.36e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.41 E-value: 4.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAV 522
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDA-VLFHNTIYYNLLYGNI--SASPEE----VYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIAR 595
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVDAD-EIIVLDQGKVAerGTHHG 666
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLISRRSyRMLTLSDGHLH--GGVGG 221
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
461-675 |
7.35e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 539
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 LLYG---------NISASPEEVYAVAKLAGLHDAilrmphgYDTQVgerglklSGGEKQRVAIARAILKDPPVILYDEAT 610
Cdd:PRK11432 99 VGYGlkmlgvpkeERKQRVKEALELVDLAGFEDR-------YVDQI-------SGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 611 SSLDSiteeTILGAMKDVVKHR------TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 675
Cdd:PRK11432 165 SNLDA----NLRRSMREKIRELqqqfniTSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
462-668 |
9.35e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 9.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESLRRAVGVVPQDAVLFHN 534
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 TIYYNLLYG-NISASP----EEVYAVAKLAGLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:PRK14243 106 SIYDNIAYGaRINGYKgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 610 TSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLL 668
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL 237
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
446-672 |
1.42e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNIQD--VSLESL 518
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 519 RRAVGVVPQDAVLFHNTIYYNLLYGN--ISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgERGLKLSGGEKQRV 591
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVkiVGWRPKLeiddiVESALKDADLWDEIKHKIH-------KSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVV--KHRTSIFIAHRLSTVVDADEIIVLDQG------KVAERGT 663
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFGL 239
|
....*....
gi 411147367 664 HHGLLANPH 672
Cdd:PRK14258 240 TKKIFNSPH 248
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
460-685 |
1.54e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.77 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqDVSLESLR-RAVGVVPQDAVLF-HNTIY 537
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKVGFVFQHYALFrHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLLYGnISASPE----EVYAV-AKLAGLHDaILRMPH---GYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:PRK10851 93 DNIAFG-LTVLPRrerpNAAAIkAKVTQLLE-MVQLAHladRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 610 TSSLDSITEETI---LGAMKDVVKHrTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGThhgllanPhsiySEMWHTQSSR 685
Cdd:PRK10851 164 FGALDAQVRKELrrwLRQLHEELKF-TSVFVTHDQEEAMEvADRVVVMSQGNIEQAGT-------P----DQVWREPATR 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
445-680 |
3.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.54 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 445 TVAFDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLE 516
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAklaglHDaiLRMPHGYDTQVGERG-LKLSGGEKQRV 591
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HR--LLMDLGFSRDVMSQSpFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 592 AIARAILKDPPVILYDEATSSLDSITEETILGAMKD--VVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLL 668
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234
|
250
....*....|..
gi 411147367 669 ANPHsiYSEMWH 680
Cdd:PRK13646 235 KDKK--KLADWH 244
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
456-614 |
4.39e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.86 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF 532
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 533 -HNTIYYNLLYG-----NISASPEEVYAVAKLAGLHDAILRMPhgyDTqvgerglkLSGGEKQRVAIARAILKDPPVILY 606
Cdd:COG4136 89 pHLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVALLRALLAEPRALLL 157
|
....*...
gi 411147367 607 DEATSSLD 614
Cdd:COG4136 158 DEPFSKLD 165
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-681 |
5.03e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 5.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 438 QITPQTATVAFDNVhfeyiegqKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQD 512
Cdd:PRK14247 3 KIEIRDLKVSFGQV--------EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 513 VSLESLRRAVGVVPQDAVLFHN-TIYYNLLYG----NISASPEEVYAVAKLAgLHDAIL--RMPHGYDTQVGerglKLSG 585
Cdd:PRK14247 75 MDVIELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA-LEKAQLwdEVKDRLDAPAG----KLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 586 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH------RLStvvdaDEIIVLDQGKVA 659
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIV 224
|
250 260
....*....|....*....|..
gi 411147367 660 ERGTHHGLLANPHSIYSEMWHT 681
Cdd:PRK14247 225 EWGPTREVFTNPRHELTEKYVT 246
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
458-662 |
6.69e-22 |
|
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: 94.21 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVVpqdavlfhntIY 537
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGAL----------IE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLLYGNISASpEEVYAVAKLAGL----HDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 613
Cdd:cd03268 80 APGFYPNLTAR-ENLRLLARLLGIrkkrIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 614 D--SITE--ETILgamkDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03268 158 DpdGIKElrELIL----SLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
461-614 |
7.07e-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: 94.81 E-value: 7.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL--AGQNIqDVS-------LESLRRAVGVVPQdavl 531
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAqaspreiLALRRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 532 FHNTIyynllyGNISAspEEVyaVAklaglhDAILRMphGYDTQVG-ERGLKL------------------SGGEKQRVA 592
Cdd:COG4778 101 FLRVI------PRVSA--LDV--VA------EPLLER--GVDREEArARARELlarlnlperlwdlppatfSGGEQQRVN 162
|
170 180
....*....|....*....|..
gi 411147367 593 IARAILKDPPVILYDEATSSLD 614
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLD 184
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
466-675 |
9.64e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.18 E-value: 9.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 466 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQD-AVLFHNTIYYNL 540
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 541 LYG-NISASPEEVYAVAKLAGLHDAILR-MPHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 618
Cdd:PRK10070 128 AFGmELAGINAEERREKALDALRQVGLEnYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 619 ETILGAM-KDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 675
Cdd:PRK10070 201 TEMQDELvKLQAKHqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
443-670 |
1.65e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 443 TATVAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI----YLAGQNIQDV- 513
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 514 SLESLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAvaKLAGLHDaILRMPHGYdtqVGERGLKLSGGEKQ 589
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLK-LVQLPEDY---VKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 590 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHG 666
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
....
gi 411147367 667 LLAN 670
Cdd:PRK13645 238 IFSN 241
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
443-669 |
2.41e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 443 TATVAFDNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAV 522
Cdd:PRK13537 5 VAPIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQdavlFHN-----TIYYNLL----YGNISASPeevyAVAKLAGLHDaILRMPHGYDTQVGErglkLSGGEKQRVAI 593
Cdd:PRK13537 83 GVVPQ----FDNldpdfTVRENLLvfgrYFGLSAAA----ARALVPPLLE-FAKLENKADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-------AHRLstvvdADEIIVLDQG-KVAErGTHH 665
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAE-GAPH 223
|
....
gi 411147367 666 GLLA 669
Cdd:PRK13537 224 ALIE 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
443-658 |
2.83e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 443 TATVAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLE 516
Cdd:PRK10535 2 TALLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRA-VGVVPQDavlfhntiyYNLLYGNISASPEEVYAV-------AKLAGLHDAILRMphGYDTQVGERGLKLSGGEK 588
Cdd:PRK10535 82 QLRREhFGFIFQR---------YHLLSHLTAAQNVEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 589 QRVAIARAILKDPPVILYDEATSSLDSITEE---TILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVLDQGKV 658
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
460-617 |
3.10e-21 |
|
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: 93.10 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK---GSIYLAGQniqDVSLESLRRAVGVVPQ-DAVLFHNT 535
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDQFQKCVAYVRQdDILLPGLT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 IYYNLLYGNISASPEEVYAVAKLAglHDAILRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
...
gi 411147367 615 SIT 617
Cdd:cd03234 176 SFT 178
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
458-663 |
5.18e-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: 93.77 E-value: 5.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 537
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLLYGnISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 617
Cdd:cd03291 116 ENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 411147367 618 EETIL-GAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 663
Cdd:cd03291 195 EKEIFeSCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
450-663 |
5.84e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 5.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVS---LESLRRAVGVVP 526
Cdd:PRK13636 10 ELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 527 Q--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgERGLKLSGGEKQRVAIARAILKDPP 602
Cdd:PRK13636 89 QdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 603 VILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTV-VDADEIIVLDQGKVAERGT 663
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGN 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
449-669 |
6.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.23 E-value: 6.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 526
Cdd:PRK13642 8 ENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 527 Q--DAVLFHNTIYYNLLYG--NISASPEEVyavakLAGLHDAILRMpHGYDTQVGERGlKLSGGEKQRVAIARAILKDPP 602
Cdd:PRK13642 88 QnpDNQFVGATVEDDVAFGmeNQGIPREEM-----IKRVDEALLAV-NMLDFKTREPA-RLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 603 VILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 669
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
449-642 |
1.43e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.42 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES---LR-RA 521
Cdd:PRK11629 9 DNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQdavlFHN---------TIYYNLLYGNISASPEEVYAVAKLAGLhdailrmphGYDTQVGERGLKLSGGEKQRVA 592
Cdd:PRK11629 89 LGFIYQ----FHHllpdftaleNVAMPLLIGKKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 593 IARAILKDPPVILYDEATSSLDSITEETI---LGAMKD-------VVKHrtSIFIAHRLS 642
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIfqlLGELNRlqgtaflVVTH--DLQLAKRMS 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
446-663 |
1.91e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 517
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 518 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVA--KLAGLhdailrmphGYDTQVGERG-LKLSGGEKQR 590
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAreKLALV---------GISESLFEKNpFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 591 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVvkHR---TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 663
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL--HQsgmTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
444-663 |
2.09e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.37 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 444 ATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVG 523
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQDAVLF-HNTIYYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 596
Cdd:PRK11650 80 MVFQNYALYpHMSVRENMAYGlKIRGMPKAeieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 597 ILKDPPVILYDEATSSLDSiteeTILGAMKDVVK--HR----TSIFIAH-RLSTVVDADEIIVLDQGKVAERGT 663
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDA----KLRVQMRLEIQrlHRrlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
427-676 |
2.53e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.75 E-value: 2.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 427 QIKDKVMASPLqITPQTATVAFDnvhfeyieGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA 506
Cdd:PRK11607 9 QAKTRKALTPL-LEIRNLTKSFD--------GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 507 GQNIQDVSleSLRRAVGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAvakLAGLHDAILRMPHgydtqv 576
Cdd:PRK11607 80 GVDLSHVP--PYQRPINMMFQSYALFpHMTVEQNIAFGlkqdklpkaEIASRVNEMLG---LVHMQEFAKRKPH------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 577 gerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVL 653
Cdd:PRK11607 149 -----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIM 223
|
250 260
....*....|....*....|...
gi 411147367 654 DQGKVAERGTHHGLLANPHSIYS 676
Cdd:PRK11607 224 NRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
407-676 |
3.24e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.46 E-value: 3.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 407 ETRQALIDMNTLftllKVDTQIKDKvMASPLQiTPQTAtvafdnvhfeyiegqKVLSGISFEVPAGKKVAIVGGSGSGKS 486
Cdd:PRK15079 3 EGKKVLLEVADL----KVHFDIKDG-KQWFWQ-PPKTL---------------KAVDGVTLRLYEGETLGVVGESGCGKS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 487 TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA---VGVVPQDAVLFHN---TIyynllyGNISASPEEVY------- 553
Cdd:PRK15079 62 TFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNprmTI------GEIIAEPLRTYhpklsrq 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 554 --------AVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 625
Cdd:PRK15079 136 evkdrvkaMMLKVGLLPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 204
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 411147367 626 KDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYS 676
Cdd:PRK15079 205 QQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-679 |
5.37e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 455 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 528
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 AVLF-HNTIYYNLLYGNISASPEEVYAVAKLagLHDAILRMphGYDTQVGER----GLKLSGGEKQRVAIARAILKDPPV 603
Cdd:PRK14246 99 PNPFpHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 604 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSEMW 679
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
459-665 |
5.39e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 5.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 459 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-----DAVLFH 533
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltpEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 534 NTIYY-----NLLYGNISASPEEVYAVAklaglhdailrMPHGYDTQVGERGL-KLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:PRK11231 95 ELVAYgrspwLSLWGRLSAEDNARVNQA-----------MEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 608 EATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHH 665
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPE 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
449-661 |
6.73e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.92 E-value: 6.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEY---IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVV 525
Cdd:COG4525 7 RHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RGV-VF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLFHNTIYYNLLYG----NISASPEEVYAVAKLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 599
Cdd:COG4525 83 QKDALLPWLNVLDNVAFGlrlrGVPKAERRARAEELLAlvGLADFARRRIW-----------QLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 600 DPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLD--QGKVAER 661
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITHSVeEALFLATRLVVMSpgPGRIVER 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
433-658 |
9.66e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 9.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 433 MASPLQITPQTAtVAFDNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQniqd 512
Cdd:PRK11247 1 MMNTARLNQGTP-LLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 513 VSLESLRRAVGVVPQDAVLFH-NTIYYNL---LYGNISASPEEVYAVAKLAglhdailrmphgydTQVGERGLKLSGGEK 588
Cdd:PRK11247 74 APLAEAREDTRLMFQDARLLPwKKVIDNVglgLKGQWRDAALQALAAVGLA--------------DRANEWPAALSGGQK 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 589 QRVAIARAILKDPPVILYDEATSSLDSITE-EtilgaMKDVVK------HRTSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRiE-----MQDLIEslwqqhGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
448-658 |
1.19e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRraVGVVPQ 527
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLF-HNTIYYNLLYGN------------ISASPEEVYAV-AKLAGLHDAILRMpHGY--------------------D 573
Cdd:COG0488 69 EPPLDdDLTVLDTVLDGDaelraleaeleeLEAKLAEPDEDlERLAELQEEFEAL-GGWeaearaeeilsglgfpeedlD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 574 TQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLD--SIT--EETIL---GAMkdvvkhrtsIFIAH-R--LST 643
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDleSIEwlEEFLKnypGTV---------LVVSHdRyfLDR 214
|
250
....*....|....*
gi 411147367 644 VVdaDEIIVLDQGKV 658
Cdd:COG0488 215 VA--TRILELDRGKL 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
460-670 |
1.22e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI------------------YLAGQNIQDV------SL 515
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 516 ESLRRAVGVVPQDA--VLFHNTIYYNLLYGNIS--ASPEEVYAVAK----LAGLHDAIL-RMPHGydtqvgerglkLSGG 586
Cdd:PRK13651 101 KEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAkyieLVGLDESYLqRSPFE-----------LSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 587 EKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTH 664
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDT 249
|
....*.
gi 411147367 665 HGLLAN 670
Cdd:PRK13651 250 YDILSD 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
465-676 |
1.68e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.00 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLF-HNTIYY 538
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyASLDpRQTVGD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 539 ---------NLLYGNisASPEEVYAVAKLAGLH-DAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDE 608
Cdd:PRK10261 423 simeplrvhGLLPGK--AAAARVAWLLERVGLLpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 609 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYS 676
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
115-410 |
1.90e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 89.49 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 115 AISLGFLGGAKAMNIVVPFMFKYAVDS------LNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVrnaVF 188
Cdd:cd18564 2 ALALLALLLETALRLLEPWPLKVVIDDvlgdkpLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTY---LT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 189 GKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPI---------MFEVMLVsgvl 259
Cdd:cd18564 79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDL---LSRLTGDVGAIQDLLVSGVLPLltnlltlvgMLGVMFW---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 260 yykCGAQFALVTLGTLgtyTAFTVAVTRWRTRFRIEMNKADNDAGN-AAI--DSLLNYETVKYFNNERYEAQRYDGFLKT 336
Cdd:cd18564 152 ---LDWQLALIALAVA---PLLLLAARRFSRRIKEASREQRRREGAlASVaqESLSAIRVVQAFGREEHEERRFARENRK 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 337 YETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLvmvngLLFqlslpLNFLGTVYRETRQ 410
Cdd:cd18564 226 SLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL-----LVF-----LAYLKNLYKPVRD 289
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
455-642 |
2.00e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.29 E-value: 2.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 455 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQDVSLES--LRRAVGVVPQ 527
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLFHNTIYYNLLYGnisaspeevyavAKLAGLHD-AILrmphgyDTQVgERGLK------------------LSGGEK 588
Cdd:PRK14239 94 QPNPFPMSIYENVVYG------------LRLKGIKDkQVL------DEAV-EKSLKgasiwdevkdrlhdsalgLSGGQQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 589 QRVAIARAILKDPPVILYDEATSSLDSIT----EETILGAMKD----VVKHrtSIFIAHRLS 642
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISagkiEETLLGLKDDytmlLVTR--SMQQASRIS 214
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
444-662 |
2.26e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 444 ATVAFDNVHFEYieGQKVLS-GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAV 522
Cdd:PRK11000 2 ASVTLRNVTKAY--GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDAVLF-HNTIYYNLLYGnisaspeevyavAKLAGLHDA-----------ILRMPHGYDTQVGErglkLSGGEKQR 590
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFG------------LKLAGAKKEeinqrvnqvaeVLQLAHLLDRKPKA----LSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 591 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVLDQGKVAERG 662
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
433-677 |
2.32e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 433 MASPLqITPQTATVAFDNVHfeyiEGQKVLSGISFEVPAGKKVAIVGGSGSGKS----TIVRLLFR---FYePQkGSIYL 505
Cdd:PRK15134 1 MTQPL-LAIENLSVAFRQQQ----TVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY-PS-GDIRF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 506 AGQNIQDVSLESLRRAVGvvPQDAVLFHNTI-----YYNL---LYGNIS--------ASPEEVYAVAKLAGLHDAILRM- 568
Cdd:PRK15134 74 HGESLLHASEQTLRGVRG--NKIAMIFQEPMvslnpLHTLekqLYEVLSlhrgmrreAARGEILNCLDRVGIRQAAKRLt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 569 --PHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTV 644
Cdd:PRK15134 152 dyPH-----------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIV 220
|
250 260 270
....*....|....*....|....*....|....
gi 411147367 645 VD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 677
Cdd:PRK15134 221 RKlADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
159-670 |
2.35e-19 |
|
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: 92.17 E-value: 2.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 159 VATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKnvflhlhnldLGFHlsRQTGALSKAIDrgtrgisfVL 238
Cdd:COG4615 59 VLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLER----------IGAA--RLLAALTEDVR--------TI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 239 SALVFNLLPIMFEVMLVSGVLYYKC--GAQFALVTLGTLGtytaFTVAVTRWRT-RFRIEMNKA--DNDAGNAAIDSL-- 311
Cdd:COG4615 119 SQAFVRLPELLQSVALVLGCLAYLAwlSPPLFLLTLVLLG----LGVAGYRLLVrRARRHLRRAreAEDRLFKHFRALle 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 312 ------LNYETVKYFNNERYEAQrydgfLKTYETASLKSTSTLAML-NFGQSAIFsvGLTAIMVLASQGIVAGTL-TVGD 383
Cdd:COG4615 195 gfkelkLNRRRRRAFFDEDLQPT-----AERYRDLRIRADTIFALAnNWGNLLFF--ALIGLILFLLPALGWADPaVLSG 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 384 LVMVngLLFqLSLPL-NFLGTV--YRETRQALIDMNTLFtlLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQK 460
Cdd:COG4615 268 FVLV--LLF-LRGPLsQLVGALptLSRANVALRKIEELE--LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 ----VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNti 536
Cdd:COG4615 343 degfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR-- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 yynlLYG-NISASPEEVYAVAKLaglhdaiLRMphgyDTQVGERG-----LKLSGGEKQRVAIARAILKDPPVILYDEAT 610
Cdd:COG4615 421 ----LLGlDGEADPARARELLER-------LEL----DHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWA 485
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 611 SSLD----SITEETILGAMKDvvKHRTSIFIAHrlstvvD------ADEIIVLDQGKVAERGTHHGLLAN 670
Cdd:COG4615 486 ADQDpefrRVFYTELLPELKA--RGKTVIAISH------DdryfdlADRVLKMDYGKLVELTGPAALAAS 547
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
462-662 |
3.35e-19 |
|
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: 87.14 E-value: 3.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVLFHNtiyYNLL 541
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQN---YSLL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 542 -----YGNISASPEEVYAVA------KLAGLHDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEAT 610
Cdd:TIGR01184 67 pwltvRENIALAVDRVLPDLskserrAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 611 SSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLDQGKVAERG 662
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
458-662 |
4.25e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAvlfhnTIY 537
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLlygnisaspeEVYAVAKLAglhdailRMPH--------GYDTQVGERGLK--------------LSGGEKQRVAIAR 595
Cdd:PRK09536 90 FEF----------DVRQVVEMG-------RTPHrsrfdtwtETDRAAVERAMErtgvaqfadrpvtsLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
464-663 |
4.67e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 86.65 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 464 GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLES--LRRAVGVVPQDAVL------FHNT 535
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPreVRRRIGIVFQDLSVddeltgWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 IYYNLLYGNISAS-PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:cd03265 95 YIHARLYGVPGAErRERIDELLDFVGLLEA-------ADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 615 SITEETILGAMKDVVK-HRTSIFI-------AHRLstvvdADEIIVLDQGKVAERGT 663
Cdd:cd03265 164 PQTRAHVWEYIEKLKEeFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGT 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
462-658 |
9.63e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLESLRRA----VGVVPQDAVLFHN-TI 536
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAialgIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 YYNLLYG---------NISASPEEVYAVAKLAGLH---DAIlrmphgydtqVGErglkLSGGEKQRVAIARAILKDPPVI 604
Cdd:COG3845 98 AENIVLGleptkggrlDRKAARARIRELSERYGLDvdpDAK----------VED----LSVGEQQRVEILKALYRGARIL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 605 LYDEATSSLdsiT-EET-----ILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:COG3845 164 ILDEPTAVL---TpQEAdelfeILRRLAA--EGKSIIFITHKLREVMAiADRVTVLRRGKV 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
427-664 |
1.11e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 427 QIKDKVMASPLQITPQTAtVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA 506
Cdd:PRK13536 24 QGISEAKASIPGSMSTVA-IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 507 GQNIQDVSlESLRRAVGVVPQ-DAVLFHNTIYYNLL-YGN-ISASPEEVYAVakLAGLHDaILRMPHGYDTQVGErglkL 583
Cdd:PRK13536 102 GVPVPARA-RLARARIGVVPQfDNLDLEFTVRENLLvFGRyFGMSTREIEAV--IPSLLE-FARLESKADARVSD----L 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 584 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-------AHRLstvvdADEIIVLDQG 656
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAG 248
|
....*....
gi 411147367 657 -KVAERGTH 664
Cdd:PRK13536 249 rKIAEGRPH 257
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
458-656 |
1.20e-18 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.13 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 537
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLLYGnISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 617
Cdd:TIGR01271 505 DNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 411147367 618 EETIL-GAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQG 656
Cdd:TIGR01271 584 EKEIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
460-658 |
1.30e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 85.02 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGVVPQDAVLFHN-TIYY 538
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYPKmKVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 539 NLLYgnisaspeevyaVAKLAGL-HDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAILKDPPVILYDEATS 611
Cdd:cd03269 90 QLVY------------LAQLKGLkKEEARRRIDEWLERLELSEYAnkrveeLSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 411147367 612 SLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
462-663 |
1.33e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLfRFYEPQ----KGSIYLAGQNIQdvsLESLRRAVGVVPQDAVLF-HNTI 536
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFIpTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 YYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHG--YDTQVGERGLK--LSGGEKQRVAIARAILKDPPVILYDEATSS 612
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 411147367 613 LDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDA--DEIIVLDQGKVAERGT 663
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGS 250
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
461-663 |
1.99e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdVS--LEslrraVGVVpqdavlFH----- 533
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSalLE-----LGAG------FHpeltg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 534 --NtIYYN-LLYGNISASPEEVYA-VAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:COG1134 106 reN-IYLNgRLLGLSRKEIDEKFDeIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 610 TSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 663
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
449-661 |
2.04e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVVPQD 528
Cdd:PRK11248 5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 AVLFHNTIYYNLLYG----NISASPEEVYAVAKLA--GLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPP 602
Cdd:PRK11248 80 GLLPWRNVQDNVAFGlqlaGVEKMQRLEIAHQMLKkvGLEGAEKRYI-----------WQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 603 VILYDEATSSLDSITEETilgaMKDV---VKHRTS---IFIAHRL-STVVDADEIIVL--DQGKVAER 661
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQ----MQTLllkLWQETGkqvLLITHDIeEAVFMATELVLLspGPGRVVER 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
459-671 |
2.58e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.59 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 459 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN- 534
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQSGALFTDm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 TIYYNLLYG--NISASPEEVY---AVAKL--AGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:PRK11831 100 NVFDNVAYPlrEHTQLPAPLLhstVMMKLeaVGLRGAAKLMPS-----------ELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 608 EATSSLDSITeETILGAMKDVVKHR---TSIFIAHRLSTVVD-AD-EIIVLDQGKVAErGTHHGLLANP 671
Cdd:PRK11831 169 EPFVGQDPIT-MGVLVKLISELNSAlgvTCVVVSHDVPEVLSiADhAYIVADKKIVAH-GSAQALQANP 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
455-681 |
4.13e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.51 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 455 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNI--QDVSLESLRRAVGVVPQ 527
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLF-HNTIYYNLLYG----NISAS----PEEVYAVAKLAGLHDAILRMPHGYDTQvgerglkLSGGEKQRVAIARAIL 598
Cdd:PRK14267 93 YPNPFpHLTIYDNVAIGvklnGLVKSkkelDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 677
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
....
gi 411147367 678 MWHT 681
Cdd:PRK14267 246 KYVT 249
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
461-625 |
7.04e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 7.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGvvPQDAVLFHNTIYYNL 540
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 541 -----LYGNisaSPEEVYAVAKLAGLHDaILRMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDS 615
Cdd:PRK13539 95 efwaaFLGG---EELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|
gi 411147367 616 ITEETILGAM 625
Cdd:PRK13539 161 AAVALFAELI 170
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
446-678 |
9.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 9.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIE----GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 517
Cdd:PRK13643 2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 518 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKlaglhdAILRMPhGYDTQVGERG-LKLSGGEKQRVA 592
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAEKIAA------EKLEMV-GLADEFWEKSpFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 593 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGThhgllan 670
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT------- 227
|
....*...
gi 411147367 671 PHSIYSEM 678
Cdd:PRK13643 228 PSDVFQEV 235
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
114-402 |
1.52e-17 |
|
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: 83.63 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQ 193
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV-IGGGLRELL--------WLLALLILGVALLRGVFRY---LQGYLAEKASQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGT-------RGISFVLSALVFNLLpiMFevmLVSGVLYYKCGAQ 266
Cdd:cd18542 69 KVAYDLRNDLYDHLQRLSFSFHDKARTGDL---MSRCTsdvdtirRFLAFGLVELVRAVL--LF---IGALIIMFSINWK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 267 FALVTLGTlgtyTAFTVAVTRW-----RTRFRI------EMNKA--DNDAGNaaidsllnyETVKYFNNERYEAQRYDGF 333
Cdd:cd18542 141 LTLISLAI----IPFIALFSYVffkkvRPAFEEireqegELNTVlqENLTGV---------RVVKAFAREDYEIEKFDKE 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 334 LKTYETASLKSTSTLA----MLNFgqsaIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLG 402
Cdd:cd18542 208 NEEYRDLNIKLAKLLAkywpLMDF----LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
439-663 |
1.97e-17 |
|
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: 86.01 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 439 ITPQTATVAFDnvhfeyieGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSI-----------YL 505
Cdd:TIGR03269 1 IEVKNLTKKFD--------GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 506 -----AGQNI---------QDVSL----ESLRRAVgvVPQDAVLFHNTIyynLLYGN-------ISASPEEVYAVAKLAG 560
Cdd:TIGR03269 73 erpskVGEPCpvcggtlepEEVDFwnlsDKLRRRI--RKRIAIMLQRTF---ALYGDdtvldnvLEALEEIGYEGKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 561 LHDAILRMphgydTQVGER----GLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TS 634
Cdd:TIGR03269 148 RAVDLIEM-----VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSM 222
|
250 260 270
....*....|....*....|....*....|
gi 411147367 635 IFIAHRLSTVVD-ADEIIVLDQGKVAERGT 663
Cdd:TIGR03269 223 VLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
450-662 |
2.51e-17 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.03 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVP 526
Cdd:cd03217 5 DLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 527 QdavlfhntiyynllygnisaSPEEVYAVaKLAGLhdaiLRmphgydtQVGErglKLSGGEKQRVAIARAILKDPPVILY 606
Cdd:cd03217 84 Q--------------------YPPEIPGV-KNADF----LR-------YVNE---GFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 607 DEATSSLD----SITEETIlGAMKDvvKHRTSIFIAH--RLSTVVDADEIIVLDQGKVAERG 662
Cdd:cd03217 129 DEPDSGLDidalRLVAEVI-NKLRE--EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
461-662 |
2.86e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.42 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLesLRRAVGVVPqDAVLFHNTIYYNL 540
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSL--LGLGGGFNP-ELTGRENIYLNGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 541 LYGnisASPEEVYA----VAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSI 616
Cdd:cd03220 111 LLG---LSRKEIDEkideIIEFSELGDFI-------DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 411147367 617 TEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:cd03220 177 FQEKCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
444-672 |
2.97e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 444 ATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAV 522
Cdd:PRK10895 2 ATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDAVLFHN-TIYYNLL-----YGNISASPEEVYAVAKLAGLHDAILRmphgydtqvGERGLKLSGGEKQRVAIARA 596
Cdd:PRK10895 81 GYLPQEASIFRRlSVYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLR---------DSMGQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETIlgamKDVVKH-RTS----IFIAHRLSTVVDADE-IIVLDQGKVAERGTHHGLLAN 670
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDI----KRIIEHlRDSglgvLITDHNVRETLAVCErAYIVSQGHLIAHGTPTEILQD 227
|
..
gi 411147367 671 PH 672
Cdd:PRK10895 228 EH 229
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
448-657 |
4.36e-17 |
|
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: 78.64 E-value: 4.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 448 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQNIQdvsleslrraVGVVPQ 527
Cdd:cd03221 3 LENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-TWGSTVK----------IGYFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 davlfhntiyynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 607
Cdd:cd03221 71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 411147367 608 EATSSLDSITEETILGAMKDvvKHRTSIFIAH-R--LSTVvdADEIIVLDQGK 657
Cdd:cd03221 96 EPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
442-662 |
4.54e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 81.85 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 442 QTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLrra 521
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQD-------AVLFHNTIYYNlLYGnisaspeevyavaklaglHDAILRMPHGYDTQVGERGL------------- 581
Cdd:PRK15056 80 VAYVPQSeevdwsfPVLVEDVVMMG-RYG------------------HMGWLRRAKKRDRQIVTAALarvdmvefrhrqi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 582 -KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDADEIIVLDQGKVA 659
Cdd:PRK15056 141 gELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
...
gi 411147367 660 ERG 662
Cdd:PRK15056 221 ASG 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
460-671 |
4.65e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 81.05 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-TIY 537
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLLygnisaspeevyAVAKLAGLHDAILRmpHGYDTQVGE---------RGLKLSGGEKQRVAIARAILKDPPVILYDE 608
Cdd:cd03218 94 ENIL------------AVLEIRGLSKKERE--EKLEELLEEfhithlrksKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 609 ATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
465-671 |
5.53e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 5.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRraVGVVPQDAVLFHN------TI 536
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPSTSLNprqrisQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 YYNLLYGNISASPEE----VYAVAKLAGL-HDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATS 611
Cdd:PRK15112 110 LDFPLRLNTDLEPEQrekqIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 612 SLDSITEETILGAMKDVV-KHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQeKQGISyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
446-660 |
6.99e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVV 525
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAVLFH--NTIYYNLLYGNISASPEEVYAVakLAGL----HDAilrmphgyDTQVGerglKLSGGEKQRVAIARAILK 599
Cdd:COG0488 384 DQHQEELDpdKTVLDELRDGAPGGTEQEVRGY--LGRFlfsgDDA--------FKPVG----VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 600 DPPVILYDEATSSLD--SIT--EETIL---GAMkdvvkhrtsIFIAH-R--LSTVvdADEIIVLDQGKVAE 660
Cdd:COG0488 450 PPNVLLLDEPTNHLDieTLEalEEALDdfpGTV---------LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
456-658 |
8.74e-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: 78.63 E-value: 8.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQD---AVL 531
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDrkrEGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 532 FHN-TIYYNLLYGNIsaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEAT 610
Cdd:cd03215 90 VLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 411147367 611 SSLDSITEETILGAMKDVVKHRTSIFIahrLSTVVD-----ADEIIVLDQGKV 658
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLL---ISSELDellglCDRILVMYEGRI 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
458-671 |
9.35e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.30 E-value: 9.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNI---QDVsLEsLRRAVGVVPQDA 529
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LE-FRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 530 VLFHNTIYYNLLYGNISAS--PEEVY---AVAKLA--GLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPP 602
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKlvPRKEFrgvAQARLTevGLWDAV-------KDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 603 VILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
458-663 |
1.26e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.92 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGvvpqdavlfhntiY 537
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG-------------Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 ynL-----LYGNISASpEEVYAVAKLAGL--HDAILRMPHGYDT-QVGERGLK----LSGGEKQRVAIARAILKDPPVIL 605
Cdd:COG4152 76 --LpeergLYPKMKVG-EQLVYLARLKGLskAEAKRRADEWLERlGLGDRANKkveeLSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 606 YDEATSSLDSITEETilgaMKDVVKH-----RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 663
Cdd:COG4152 153 LDEPFSGLDPVNVEL----LKDVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
462-663 |
1.41e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.88 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVL------FH 533
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPpfampvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 534 ntiyYNLLYGNISASPEEV-YAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI----- 604
Cdd:COG4138 89 ----YLALHQPAGASSEAVeQLLAQLAealGLEDKLSRPLT-----------QLSGGEWQRVRLAAVLLQVWPTInpegq 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 605 --LYDEATSSLDsITEETilgAMKDVVKH-----RTSIFIAHRLS-TVVDADEIIVLDQGKVAERGT 663
Cdd:COG4138 154 llLLDEPMNSLD-VAQQA---ALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
117-412 |
1.49e-16 |
|
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: 80.61 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 117 SLGFLGGAKAMNIVVPFMFKYAVDSLNQmSGNMLNLsdapNTVATMATAVLigygVSRAGAAFFnevRNAVFGKVAQNSI 196
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALG-GGDTASL----NQIALLLLGLF----LLQAVFSFF---RIYLFARVGERVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMfeVMLVSGV--LYYKcGAQFALVTLGT 274
Cdd:cd18576 69 ADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQI--LTLIGGVvlLFFI-SWKLTLLMLAT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 275 LGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFG 354
Cdd:cd18576 146 VPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSF 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 355 QSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18576 226 IIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
442-678 |
1.54e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 442 QTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRR 520
Cdd:PRK11288 1 SSPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 521 AVGVVPQDAVLFHN-TIYYNLLYGNISASPEEV-------YAVAKLAGLHDAIlrMPhgyDTQVGErglkLSGGEKQRVA 592
Cdd:PRK11288 80 GVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVnrrllnyEAREQLEHLGVDI--DP---DTPLKY----LSIGQRQMVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 593 IARAILKDPPVILYDEATSSLdSITEETIL----GAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAErgTHHGL 667
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSL-SAREIEQLfrviRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225
|
250
....*....|..
gi 411147367 668 LANPH-SIYSEM 678
Cdd:PRK11288 226 AQVDRdQLVQAM 237
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
114-412 |
2.14e-16 |
|
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: 80.25 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMAtavligygVSRAGAAFFNEVRNAVFGKVAQ 193
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLA--------GAYVLSALLGILRGRLLARLGE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRG-------ISFVLSALVFNLLPIMFevmlVSGVLYYkCGAQ 266
Cdd:cd18563 73 RITADLRRDLYEHLQRLSLSFFDKRQTGSL---MSRVTSDtdrlqdfLSDGLPDFLTNILMIIG----IGVVLFS-LNWK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 267 FALVTLGTLgtytAFTVAVTRW---RTRFRIEMNKADNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETASL 342
Cdd:cd18563 145 LALLVLIPV----PLVVWGSYFfwkKIRRLFHRQWRRWSRLNSVLnDTLPGIRVVKAFGQEKREIKRFDEANQELLDANI 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 343 KSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18563 221 RAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
438-663 |
6.51e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 438 QITPQTATVAFDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 517
Cdd:PRK10575 4 YTNHSDTTFALRNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 518 LRRAVGVVPQDavlfhntiyynlLYGNISASPEEVYAVAKLAgLHDAILRMPHGYDTQVGER----GLK---------LS 584
Cdd:PRK10575 83 FARKVAYLPQQ------------LPAAEGMTVRELVAIGRYP-WHGALGRFGAADREKVEEAislvGLKplahrlvdsLS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 585 GGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAER 661
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229
|
..
gi 411147367 662 GT 663
Cdd:PRK10575 230 GT 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
461-658 |
9.75e-16 |
|
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: 77.37 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV------------PQD 528
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgqktqlwwdlpVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 AVLFHNTIYynllygNIsaspEEVYAVAKLAGLHDaILRMPHGYDTQVgeRglKLSGGEKQRVAIARAILKDPPVILYDE 608
Cdd:cd03267 115 SFYLLAAIY------DL----PPARFKKRLDELSE-LLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 411147367 609 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
460-678 |
1.09e-15 |
|
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: 80.62 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIY-LAGQNIQDVS----LESLR--RAVGVVPQDAVLF 532
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMTkpgpDGRGRakRYIGILHQEYDLY 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 533 -HNTIYYNLLYGNISASPEE------VYaVAKLAGLHD----AIL-RMPHgydtqvgerglKLSGGEKQRVAIARAILKD 600
Cdd:TIGR03269 378 pHRTVLDNLTEAIGLELPDElarmkaVI-TLKMVGFDEekaeEILdKYPD-----------ELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 601 PPVILYDEATSSLDSITE----ETILGAMKDVvkHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGthhgllaNPHSIY 675
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIG-------DPEEIV 516
|
...
gi 411147367 676 SEM 678
Cdd:TIGR03269 517 EEL 519
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
456-673 |
1.27e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.43 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkGSIYLAGQNIQD---VSLESLR-RAVGVV---PQ 527
Cdd:PRK10418 12 LQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDgkpVAPCALRgRKIATImqnPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAvlfhntiyYNLLYGNISASPEEVYAVAKLAglHDAilRMPHGYDtQVG----ERGLKL-----SGGEKQRVAIARAIL 598
Cdd:PRK10418 90 SA--------FNPLHTMHTHARETCLALGKPA--DDA--TLTAALE-AVGlenaARVLKLypfemSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS--IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHS 673
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
445-660 |
2.35e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.63 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 445 TVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 524
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIyynllygnisaSPEEVYAVAKLAGLHDAILRMPHGYDTQVGE-RGLKLSGGEKQRVAIARAILKDPPV 603
Cdd:PRK10522 402 VFTDFHLFDQLL-----------GPEGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 604 ILYDEATSSLD----SITEETILGAMKDVVKhrTSIFIAHRLSTVVDADEIIVLDQGKVAE 660
Cdd:PRK10522 471 LLLDEWAADQDphfrREFYQVLLPLLQEMGK--TIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
442-670 |
3.10e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 442 QTATVAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD-VSLESLRR 520
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 521 AVGVVPQDAVLFHN-TIYYNLLYGNISASPEEVYA-VAKLAGLhdailrMPHGYDTQVgERGLKLSGGEKQRVAIARAIL 598
Cdd:PRK11614 81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQErIKWVYEL------FPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLS--TVVDADEIIVLDQGKVAERGTHHGLLAN 670
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
476-663 |
3.95e-15 |
|
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: 80.06 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 476 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQDAVLFHNTIY--YNLLYGNISASPEEVY 553
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHLTVaeHILFYAQLKGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 554 AVAKLAGLHDAilrmphGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRT 633
Cdd:TIGR01257 1039 QLEMEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
|
170 180 190
....*....|....*....|....*....|.
gi 411147367 634 SIFIAHRLSTV-VDADEIIVLDQGKVAERGT 663
Cdd:TIGR01257 1113 IIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
114-412 |
7.35e-15 |
|
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: 75.92 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQmsgnmlnlSDAPNTVATMATAVLIGYGVsRAGAAFFNEVrnaVFGKVAQ 193
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV--------EKDLEALLLVPLAIIGLFLL-RGLASYLQTY---LMAYVGQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-SKA---IDRGTRGISFVLSALVFNLLPIMFevmLVSGVLYYkcGAQFAL 269
Cdd:cd18552 69 RVVRDLRNDLFDKLLRLPLSFFDRNSSGDLiSRItndVNQVQNALTSALTVLVRDPLTVIG---LLGVLFYL--DWKLTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 270 VTLGTLGtytAFTVAVTRWRTRFRIEMNKADNDAGN---AAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTS 346
Cdd:cd18552 144 IALVVLP---LAALPIRRIGKRLRKISRRSQESMGDltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIAR 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 347 TLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18552 221 ARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGL 286
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
446-640 |
1.01e-14 |
|
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: 72.57 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVV 525
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 PQDAvlfhntiYYNLlyGNisaspeevyavaklagLHDAILRmPHGydtqvgergLKLSGGEKQRVAIARAILKDPPVIL 605
Cdd:cd03223 70 PQRP-------YLPL--GT----------------LREQLIY-PWD---------DVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 411147367 606 YDEATSSLDSITEETILGAMKDvvKHRTSIFIAHR 640
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
118-412 |
2.49e-14 |
|
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: 74.13 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 118 LGFLGGAKAMNIVVPFMFKYAVDSLNQMSGnmlnlSDAPNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVAQNSIR 197
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGD-----LDVLNELALILLAIYLLQSV-------FTFVRYYLFNIAGERIVA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 198 RIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLY--YKCGAQFALVTLGTL 275
Cdd:cd18557 70 RLRRDLFSSLLRQEIAFFDKHKTGEL---TSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIilFILSWKLTLVLLLVI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 276 GTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQ 355
Cdd:cd18557 147 PLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGIT 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 356 SAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18557 227 SLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKAL 283
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
416-660 |
2.50e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.68 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 416 NTLFTLLKVDtqikdKVMASPLQITPQTATV--AFdNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF 493
Cdd:COG2401 5 NPFFVLMRVT-----KVYSSVLDLSERVAIVleAF-GVELRVVE-RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 494 RFYE--PQKGSIYLAGQNI-QDVSLeslrravgvvpQDAVLfhntiyynllygnISASPEEVYAVAKLAGLHDAILrmph 570
Cdd:COG2401 78 GALKgtPVAGCVDVPDNQFgREASL-----------IDAIG-------------RKGDFKDAVELLNAVGLSDAVL---- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 571 gYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRlSTVVDA- 647
Cdd:COG2401 130 -WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDl 203
|
250
....*....|....*
gi 411147367 648 --DEIIVLDQGKVAE 660
Cdd:COG2401 204 qpDLLIFVGYGGVPE 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
461-621 |
2.56e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLR-RAVGVVPQDAVL----- 531
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLiptln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 532 -FHNTIYYNLLYG-NISASPEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:PRK10584 105 aLENVELPALLRGeSSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170
....*....|..
gi 411147367 610 TSSLDSITEETI 621
Cdd:PRK10584 174 TGNLDRQTGDKI 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
461-662 |
5.46e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 5.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 461 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 540
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 541 L-YGNISASP-------EEVYAVAK---LAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:PRK10253 102 VaRGRYPHQPlftrwrkEDEEAVTKamqATGITHLADQ---SVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 610 TSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
458-657 |
5.81e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 74.86 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 533
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 534 N-TIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSS 612
Cdd:TIGR02633 92 ElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 411147367 613 LDSITEETILGAMKDVVKHRTS-IFIAHRLSTV-VDADEIIVLDQGK 657
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVAcVYISHKLNEVkAVCDTICVIRDGQ 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
458-625 |
5.93e-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: 71.37 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 537
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLLY---GNISASPEEVYAVAKLAGLHDAilrmPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:cd03231 92 ENLRFwhaDHSDEQVEEALARVGLNGFEDR----PVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|.
gi 411147367 615 SITEETILGAM 625
Cdd:cd03231 158 KAGVARFAEAM 168
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
458-659 |
6.12e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV--VPQDAVLFHN- 534
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 TIYYNLLYGnisaSPEEVYAVAKLAGLHdAILRMPHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:PRK15439 102 SVKENILFG----LPKRQASMQKMKQLL-AALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 411147367 615 SITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVA 659
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIvFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
458-657 |
7.06e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 533
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 534 N-TIYYNLLYGN-ISASP----EEVYAVAK--LAGLHDAIlrmphGYDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 605
Cdd:PRK13549 96 ElSVLENIFLGNeITPGGimdyDAMYLRAQklLAQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 411147367 606 YDEATSSLDSITEETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGK 657
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
457-653 |
7.43e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 70.73 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 457 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVVPQdavlfhnti 536
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ--------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 yynllygnISASPEEVYA-VAKLAGL----HDAILRMPHGYDTQVGERGLK--------------LSGGEKQRVAIARAI 597
Cdd:NF040873 63 --------RSEVPDSLPLtVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGL 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 598 LKDPPVILYDEATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDADEIIVL 653
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
450-677 |
8.41e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.89 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYiEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNIQDVSLESLRRA- 521
Cdd:PRK10261 19 NIAFMQ-EQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQagglvQCDKMLLRRRSRQVIELSEQSAAq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 --------VGVVPQDAVLFHNTIY---------YNLLYGnisASPEEVYAVAK-------LAGLHDAILRMPHgydtqvg 577
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMTSLNPVFtvgeqiaesIRLHQG---ASREEAMVEAKrmldqvrIPEAQTILSRYPH------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 578 erglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKdVVKHRTS---IFIAHRLSTVVD-ADEIIVL 653
Cdd:PRK10261 168 ----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMSmgvIFITHDMGVVAEiADRVLVM 242
|
250 260
....*....|....*....|....
gi 411147367 654 DQGKVAERGTHHGLLANPHSIYSE 677
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQHPYTR 266
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
462-694 |
9.74e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESL--RRAVgVVPQDAVLFHNTIY 537
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELarHRAY-LSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNL-LYG----NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI-------L 605
Cdd:PRK03695 88 QYLtLHQpdktRTEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLQVWPDInpagqllL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 606 YDEATSSLDsITEEtilGAMKDVVKH-----RTSIFIAHRLS-TVVDADEIIVLDQGKVAERGTHHGLLANPhsIYSEMW 679
Cdd:PRK03695 157 LDEPMNSLD-VAQQ---AALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE--NLAQVF 230
|
250
....*....|....*
gi 411147367 680 HTQSSRVQNHDNPKW 694
Cdd:PRK03695 231 GVNFRRLDVEGHPML 245
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
458-661 |
1.11e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLFHN-T 535
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 IYYNLLYGNISASP------EEVYAVAklaglhDAILR---MPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 606
Cdd:PRK10762 96 IAENIFLGREFVNRfgridwKKMYAEA------DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 607 DEATSSL-DSITEE--TILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGK-VAER 661
Cdd:PRK10762 166 DEPTDALtDTETESlfRVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
460-665 |
1.20e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS---IYLAGQNIQDV-----SLESLRRAVGVVPQDAVL 531
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 532 FHN-TIYYNLLYGNISASP-----EEVYAVAKLAGLHDAILRMphGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVIL 605
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 606 YDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHH 665
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
446-662 |
1.34e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSLESLRRAVG 523
Cdd:PRK13638 2 LATSDLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 524 VVPQDAvlfHNTIYYNLLYGNISaspeevYAVAKLAGLHDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAI 597
Cdd:PRK13638 81 TVFQDP---EQQIFYTDIDSDIA------FSLRNLGVPEAEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 598 LKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-AHRLSTVVD-ADEIIVLDQGKVAERG 662
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
114-404 |
1.46e-13 |
|
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: 72.21 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLSDAPNTVATMATAVLIGY--GVSRAGAAFFNEVRNAVFGK 190
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAvFNGEASFLPLVPASLGPADPRGQLWLLGGltVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 191 VAQNSIRRIAKNVFLHLHNLDLGFHLSRQTG----ALSKAIDRGTRgisfVLSALVFNLLPIMFEVMLVSGVLYYkCGAQ 266
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGdlmsVLNNDVNQLER----FLDDGANSIIRVVVTVLGIGAILFY-LNWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 267 FALVTLGTLgtytAFTVAVTRWRTRfRIEMNKAD--NDAG--NAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETAS 341
Cdd:cd18565 156 LALVALLPV----PLIIAGTYWFQR-RIEPRYRAvrEAVGdlNARLeNNLSGIAVIKAFTAEDFERERVADASEEYRDAN 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 342 LKSTSTLAMLNFGQSAIFSVGLTAI------MVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTV 404
Cdd:cd18565 231 WRAIRLRAAFFPVIRLVAGAGFVATfvvggyWVLDGPPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDL 299
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
114-411 |
2.88e-13 |
|
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: 70.97 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVA- 192
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGP---------IAHGDRSALWPLVLLLLALGVAEAVLSF---LRRYLAGRLSl 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 193 --QNSIRRiakNVFLHLHNLDLGFHLSRQTGAL-SKAI-DRGT--RGISFVLSALVFNL-LPIMFEVMLVSGVLyykcga 265
Cdd:cd18543 69 gvEHDLRT---DLFAHLQRLDGAFHDRWQSGQLlSRATsDLSLvqRFLAFGPFLLGNLLtLVVGLVVMLVLSPP------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 266 qFALVTLGTLGtytAFTVAVTRWRTRFRIEMNKADNDAGNAAI---DSLLNYETVKYFNNERYEAQRYDGFLKTYETASL 342
Cdd:cd18543 140 -LALVALASLP---PLVLVARRFRRRYFPASRRAQDQAGDLATvveESVTGIRVVKAFGRERRELDRFEAAARRLRATRL 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 343 KSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQA 411
Cdd:cd18543 216 RAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRA 284
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
458-671 |
2.97e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.06 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIvrllfrFY------EPQKGSIYLAGQNIQDVSLEslRRA---VGVVPQD 528
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPMH--KRArlgIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 AVLFHN-TIYYNLLygnisaspeevyAVAKLAGLH--------DAIL---RMPHGYDTqvgeRGLKLSGGEKQRVAIARA 596
Cdd:COG1137 87 ASIFRKlTVEDNIL------------AVLELRKLSkkereerlEELLeefGITHLRKS----KAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETIlgamKDVVKHRTS----IFIA-HR----LSTVvdaDEIIVLDQGKVAERGTHHGL 667
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADI----QKIIRHLKErgigVLITdHNvretLGIC---DRAYIISEGKVLAEGTPEEI 223
|
....
gi 411147367 668 LANP 671
Cdd:COG1137 224 LNNP 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
451-670 |
4.95e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 451 VHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV----- 525
Cdd:COG4586 28 FRREYRE-VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 526 -------PQDAVLFHNTIYynllygNIsasPEEVYA--VAKLAGLhdaiLRMPHGYDTQVgeRglKLSGGEKQRVAIARA 596
Cdd:COG4586 106 qlwwdlpAIDSFRLLKAIY------RI---PDAEYKkrLDELVEL----LDLGELLDTPV--R--QLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLAN 670
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
450-632 |
5.30e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 450 NVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAV------- 522
Cdd:PRK13540 6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLcfvghrs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQdaVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDailrMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPP 602
Cdd:PRK13540 84 GINPY--LTLRENCLYDIHFSPGAVGITELCRLFSLEHLID----YPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190
....*....|....*....|....*....|
gi 411147367 603 VILYDEATSSLDSITEETIlgaMKDVVKHR 632
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTI---ITKIQEHR 174
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
465-677 |
5.67e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG----VVPQDAVLFHN-- 534
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPMTSLNpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 -TIYYNLLY-------GNISASPEEVYAVAKLAGLHDAILRM---PHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 603
Cdd:PRK11022 106 yTVGFQIMEaikvhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH-----------QLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 604 ILYDEATSSLDSITEETILGAMKDVVKHRTS--IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 677
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
128-449 |
2.08e-12 |
|
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: 68.24 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 128 NIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLH 206
Cdd:cd18570 18 GIAGSFFFQILIDDiIPSGDINLLNI---------ISIGLILLYLFQ----SLLSYIRSYLLLKLSQKLDIRLILGYFKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 207 LHNLDLGFHLSRQTGA-LSKAIDrgTRGISFVLSALVFNLlPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVA- 284
Cdd:cd18570 85 LLKLPLSFFETRKTGEiISRFND--ANKIREAISSTTISL-FLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLf 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 285 VTRWRTRFRIEMNK-ADNDAgnAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIF---- 359
Cdd:cd18570 162 NKPFKKKNREVMESnAELNS--YLIESLKGIETIKSLNAEEQFLKKIEKKFSKL----LKKSFKLGKLSNLQSSIKglis 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 360 SVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLfqlslpLNFLGTVyretrQALIDmntlftllkvdtqikdkvmaspLQI 439
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFNALL------GYFLGPI-----ENLIN----------------------LQP 282
|
330
....*....|
gi 411147367 440 TPQTATVAFD 449
Cdd:cd18570 283 KIQEAKVAAD 292
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
363-648 |
2.72e-12 |
|
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: 70.16 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 363 LTAIMVLASQGIVAGTLTVGDLV---MVNG-LLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKV-------------- 424
Cdd:TIGR00954 344 AVSIPIFDKTHPAFLEMSEEELMqefYNNGrLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVlddvksgnfkrprv 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 425 --DTQIKDKVMASPL-----QITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF---- 493
Cdd:TIGR00954 424 eeIESGREGGRNSNLvpgrgIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwp 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 494 ----RFYEPQKGSIYLAGQNIQdVSLESLRravgvvpqDAVLFHNTIYYNLLYGNISASPEEVYAVAKLaglhDAILRMP 569
Cdd:TIGR00954 504 vyggRLTKPAKGKLFYVPQRPY-MTLGTLR--------DQIIYPDSSEDMKRRGLSDKDLEQILDNVQL----THILERE 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 570 HGYDTqVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDV------VKHRTSIFIAHRLST 643
Cdd:TIGR00954 571 GGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFgitlfsVSHRKSLWKYHEYLL 649
|
....*
gi 411147367 644 VVDAD 648
Cdd:TIGR00954 650 YMDGR 654
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
116-387 |
3.33e-12 |
|
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: 67.88 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 116 ISLGFLG--GAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATA-VLIGygvsrAGAAFFNEVRNAVFGKVA 192
Cdd:cd18577 1 LIIGLLAaiAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYfVYLG-----IGSFVLSYIQTACWTITG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 193 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTR----GISFVLSALVFNLlpimfeVMLVSGV---LYYkcGA 265
Cdd:cd18577 76 ERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNliqdGIGEKLGLLIQSL------STFIAGFiiaFIY--SW 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 266 QFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKST 345
Cdd:cd18577 148 KLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 411147367 346 STLAMlnfgQSAIFSVGLTAIMVLA----SQGIVAGTLTVGDLVMV 387
Cdd:cd18577 228 LVSGL----GLGLLFFIIFAMYALAfwygSRLVRDGEISPGDVLTV 269
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
455-678 |
4.22e-12 |
|
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: 66.66 E-value: 4.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 455 YIEGQKVLSGISFEVPAG-----KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIylagqniqdvslESLRRAVGVVPQDA 529
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 530 VLFHNTIYYNLLYGNISASPEEVYAVAKLAGlhdaILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:cd03237 71 KADYEGTVRDLLSSITKDFYTHPYFKTEIAK----PLQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 610 TSSLDSitEETILGAmkDVVKHrtsiFIAHRLST--VVD---------ADEIIVLDqGKVAERGTHHGllanPHSIYSEM 678
Cdd:cd03237 143 SAYLDV--EQRLMAS--KVIRR----FAENNEKTafVVEhdiimidylADRLIVFE-GEPSVNGVANP----PQSLRSGM 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
458-614 |
5.17e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA-VGVVPQD-----AVL 531
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 532 fHNTIYYNLLYGNISASP---------EEVYAVAKlaglhDAILRM---PHGYDTQVGerglKLSGGEKQRVAIARAILK 599
Cdd:COG3845 350 -DMSVAENLILGRYRRPPfsrggfldrKAIRAFAE-----ELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSR 419
|
170
....*....|....*
gi 411147367 600 DPPVILYDEATSSLD 614
Cdd:COG3845 420 DPKLLIAAQPTRGLD 434
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
443-614 |
7.65e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 443 TATVAFDNVHFEYieGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRra 521
Cdd:PRK09544 2 TSLVSLENVSVSF--GQrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 VGVVPQ----DAVLFHNTIYYNLLYGNI-SASPEEVYAVAKLAGLHDAILRmphgydtqvgerglKLSGGEKQRVAIARA 596
Cdd:PRK09544 69 IGYVPQklylDTTLPLTVNRFLRLRPGTkKEDILPALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARA 134
|
170
....*....|....*...
gi 411147367 597 ILKDPPVILYDEATSSLD 614
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVD 152
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
464-674 |
8.03e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.17 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 464 GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVVP--QDAVLFHN-TIYYNL 540
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRtfQHVRLFREmTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 541 LygnisaspeevyaVAK--------LAGL----------HDAILRMPHGYDtQVGERGL------KLSGGEKQRVAIARA 596
Cdd:PRK11300 102 L-------------VAQhqqlktglFSGLlktpafrraeSEALDRAATWLE-RVGLLEHanrqagNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 597 ILKDPPVILYDEATSSLDSitEETI-LGAMKDVVK--HRTSI-FIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 671
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNP--KETKeLDELIAELRneHNVTVlLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245
|
...
gi 411147367 672 HSI 674
Cdd:PRK11300 246 DVI 248
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
458-678 |
9.41e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL----ESLRRAV-----GVVPQD 528
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalsEAERRRLlrtewGFVHQH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 A-------VLFHNTIYYNLL------YGNISASpeevyAVAKLAGLHDAILRM---PHGYdtqvgerglklSGGEKQRVA 592
Cdd:PRK11701 98 PrdglrmqVSAGGNIGERLMavgarhYGDIRAT-----AGDWLERVEIDAARIddlPTTF-----------SGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 593 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTV-VDADEIIVLDQGKVAERGTHHGLLA 669
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVArLLAHRLLVMKQGRVVESGLTDQVLD 241
|
....*....
gi 411147367 670 NPHSIYSEM 678
Cdd:PRK11701 242 DPQHPYTQL 250
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
114-386 |
1.19e-11 |
|
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: 66.26 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVA 192
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDyIVPGQGDLQGL-----------LLLALLYLGLLLLSFLLQYLQTYLLQKLG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 193 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSkaidrgTRGIS--------F--VLSALVFNLLPI--MFEVMLVSGVly 260
Cdd:cd18544 70 QRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLV------TRVTNdtealnelFtsGLVTLIGDLLLLigILIAMFLLNW-- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 261 ykcgaQFALVTLGTLgtytAFTVAVTRWrtrFRIEMNKADND--AGNAAIDSLLNyE------TVKYFNNERYEAQRYDG 332
Cdd:cd18544 142 -----RLALISLLVL----PLLLLATYL---FRKKSRKAYREvrEKLSRLNAFLQ-EsisgmsVIQLFNREKREFEEFDE 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 411147367 333 FLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVM 386
Cdd:cd18544 209 INQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
117-412 |
3.52e-11 |
|
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: 64.49 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 117 SLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGnmlnlsdapntVATMATAVLIgYGVSRAGAAFFNEVRNAVFGKVAQNSI 196
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGS-----------REAFYRAVLL-LLLLSVLSGLFSGLRGGCFSYAGTRLV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSaLVFNllpIMFE--VMLVSGVLY-YKCGAQFALVTLG 273
Cdd:cd18572 69 RRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLS-TNLN---VFLRnlVQLVGGLAFmFSLSWRLTLLAFI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 274 TLGtytaFTVAVTRWRTRFRIEMNKADND----AGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKStstlA 349
Cdd:cd18572 145 TVP----VIALITKVYGRYYRKLSKEIQDalaeANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQ----A 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 350 MLNFGQSAIFSVGLTAIMVLA----SQGIVAGTLTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQAL 412
Cdd:cd18572 217 LAYAGYVAVNTLLQNGTQVLVlfygGHLVLSGRMSAGQLVTF--MLYQQQLgeAFQSLGDVFSSLMQAV 283
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
458-610 |
3.60e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.20 E-value: 3.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSlESLRRAVGVVPQD----AVL 531
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPEDrkgeGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 532 FHNTIYYNLLYGNISA-------SPEEVYAVAKlaglhDAILRM---PHGYDTQVGErglkLSGGEKQRVAIARAILKDP 601
Cdd:COG1129 343 LDLSIRENITLASLDRlsrggllDRRRERALAE-----EYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDP 413
|
....*....
gi 411147367 602 PVILYDEAT 610
Cdd:COG1129 414 KVLILDEPT 422
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
472-654 |
8.93e-11 |
|
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: 60.46 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 472 GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS-IYLAGQNIQDVSLESLRravgvvpqdavlfhntiyynllygnisaspe 550
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 551 evyavaklaglhdailrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK 630
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180 190
....*....|....*....|....*....|.
gi 411147367 631 HRTS-------IFIAHRLSTVVDADEIIVLD 654
Cdd:smart00382 109 LLLKseknltvILTTNDEKDLGPALLRRRFD 139
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
454-657 |
1.30e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 454 EYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQKGSIYLAgqNIQDVSLESLRRaVGVVPQDAVLF 532
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNFTGTILA--NNRKPTKQILKR-TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 533 -HNTIYYNLLYGNISASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDE 608
Cdd:PLN03211 153 pHLTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 411147367 609 ATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDA--DEIIVLDQGK 657
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
433-656 |
1.94e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.04 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 433 MASPLqITPQTATVAFDNVHfeyiegqkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD 512
Cdd:PRK09700 1 MATPY-ISMAGIGKSFGPVH--------ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 513 VSLE-SLRRAVGVVPQD-AVLFHNTIYYNLLYGNISASP---------EEVYAVAKLAGLHDAILRMPhgyDTQVGErgl 581
Cdd:PRK09700 72 LDHKlAAQLGIGIIYQElSVIDELTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDL---DEKVAN--- 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 582 kLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQG 656
Cdd:PRK09700 146 -LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIvYISHKLAEIRRiCDRYTVMKDG 221
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
458-614 |
7.57e-10 |
|
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: 61.87 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAG--QNIQDVSLESLRRAVGVVPQDAVLFHN- 534
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGvdKDFNGEARPQPGIKVGYLPQEPQLDPTk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 TIYYNLLYG-----NISASPEEVYA------------VAKLAGLHDAI------------------LRMPHGyDTQVGer 579
Cdd:TIGR03719 84 TVRENVEEGvaeikDALDRFNEISAkyaepdadfdklAAEQAELQEIIdaadawdldsqleiamdaLRCPPW-DADVT-- 160
|
170 180 190
....*....|....*....|....*....|....*
gi 411147367 580 glKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:TIGR03719 161 --KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
462-651 |
7.73e-10 |
|
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: 58.49 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVrllfrfyepqKGSIYLAGQNIQDVSLESlrravgvvpqdavlfhntiyynll 541
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV----------NEGLYASGKARLISFLPK------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 542 ygnisASPEEVYAVAKLAGLHDAILrmphGYDTqVGERGLKLSGGEKQRVAIARAILKDPPVILY--DEATSSLDSITEE 619
Cdd:cd03238 57 -----FSRNKLIFIDQLQFLIDVGL----GYLT-LGQKLSTLSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|...
gi 411147367 620 TILGAMKDVV-KHRTSIFIAHRLSTVVDADEII 651
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
453-666 |
1.33e-09 |
|
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: 61.34 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 453 FEYIEGQKVLSGISFEVPAGK-----KVAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLagQNIQDVSLE 516
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYI--SPDYDGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 S-LRRAVGVVpqdavlFHNTIYYNLlygnisaspeevyaVAKLAGLHdailRMphgYDTQVGErglkLSGGEKQRVAIAR 595
Cdd:COG1245 420 EfLRSANTDD------FGSSYYKTE--------------IIKPLGLE----KL---LDKNVKD----LSGGELQRVAIAA 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 596 AILKDPPVILYDEATSSLDSitEETILGA--MKDVV--KHRTSIFIAHRLsTVVD--ADEIIVLDqGKVAERGTHHG 666
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDV--EQRLAVAkaIRRFAenRGKTAMVVDHDI-YLIDyiSDRLMVFE-GEPGVHGHASG 541
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
114-385 |
2.12e-09 |
|
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: 59.47 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlsdapnTVATMATAVLIGYGVSRAGA----AFFNEVRNAVFG 189
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLV---------------TIGSKSLGLLLGLALLLLGAyllrALLNFLRIYLNH 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 190 KVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFAL 269
Cdd:cd18778 66 VAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSI-NPKLAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 270 VTLGTLGTYTAFTVAVTRW-RTRFRI------EMNKA--DNDAGNAAIdsllnyetvKYFNNERYEAQRYDGFLKTYETA 340
Cdd:cd18778 145 LTLIPIPFLALGAWLYSKKvRPRYRKvrealgELNALlqDNLSGIREI---------QAFGREEEEAKRFEALSRRYRKA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 411147367 341 SLKSTSTLAMlnFGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDLV 385
Cdd:cd18778 216 QLRAMKLWAI--FHPLMEFLTSLGTVLVLGFGGrlVLAGELTIGDLV 260
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
204-418 |
3.17e-09 |
|
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: 58.73 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 204 FLHLHNLDLGFHLSRQTGALskaIDR-----------GTRGISFVLSAL-VFNLLPIMFevmlvsgvlYYKcgAQFALVT 271
Cdd:cd18568 82 YKHLLSLPLSFFASRKVGDI---ITRfqenqkirrflTRSALTTILDLLmVFIYLGLMF---------YYN--LQLTLIV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 272 LGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAML 351
Cdd:cd18568 148 LAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 352 NFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 418
Cdd:cd18568 228 QLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
454-666 |
3.52e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 454 EYIEGQKVLSGISFEVPAGKK-----VAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQniQDVSLES 517
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqYIKPD--YDGTVED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 518 LRRAVGVVpqdavlFHNTIYYNLLygnisASPeevyavaklaglhdaiLRMPHGYDTQVGErglkLSGGEKQRVAIARAI 597
Cdd:PRK13409 420 LLRSITDD------LGSSYYKSEI-----IKP----------------LQLERLLDKNVKD----LSGGELQRVAIAACL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 598 LKDPPVILYDEATSSLDSitEETILGA--MKDVVKHR--TSIFIAHRLsTVVD--ADEIIVLDqGKVAERGTHHG 666
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDV--EQRLAVAkaIRRIAEEReaTALVVDHDI-YMIDyiSDRLMVFE-GEPGKHGHASG 539
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
113-405 |
3.87e-09 |
|
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: 58.63 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 113 RVAISLGFLGGAKAMNIVVPFMFKYAVDSlNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVA 192
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDE-YIPNGDLSGL-----------LIIALLFLALNLVNWVASRLRIYLMAKVG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 193 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKAI-DRGTrgISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALV 270
Cdd:cd18545 69 QRILYDLRQDLFSHLQKLSFSFFDSRPVGKiLSRVInDVNS--LSDLLSNGLINLIPDLLTLVGIVIIMFSL-NVRLALV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 271 TLGTLgtyTAFTVAVTRW----RTRFRIEMNKADNdaGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKST 345
Cdd:cd18545 146 TLAVL---PLLVLVVFLLrrraRKAWQRVRKKISN--LNAYLhESISGIRVIQSFAREDENEEIFDELNRENRKANMRAV 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 346 STLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV-MVN--GLLFQlslPLNFLGTVY 405
Cdd:cd18545 221 RLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVaFIGyvGRFWQ---PIRNLSNFY 280
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
458-657 |
4.43e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLF-HNT 535
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 IYYNLLYGNisaspeevYAVAKLAGLHDAILRMPH------GYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:PRK10982 90 VMDNMWLGR--------YPTKGMFVDQDKMYRDTKaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 610 TSSLdsiTEE------TILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGK 657
Cdd:PRK10982 162 TSSL---TEKevnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
458-660 |
4.47e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL-----FRFYEpqkGSIYLAGQ-----NIQDvsleSLRRAVGVVPQ 527
Cdd:NF040905 13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILFDGEvcrfkDIRD----SEALGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 D-AVLFHNTIYYNLLYGNISASP-----EEVYAVAK--LA--GLHDAilrmPhgyDTQVGERGLklsgGEKQRVAIARAI 597
Cdd:NF040905 86 ElALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 598 LKDPPVILYDEATSSL---DSiteETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 660
Cdd:NF040905 155 SKDVKLLILDEPTAALneeDS---AALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
550-657 |
4.62e-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: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 550 EEVYAvAKLAGLHDAILRMPHGYDTQVGE---RGLklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMK 626
Cdd:TIGR00956 177 REEYA-KHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK 253
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 411147367 627 dvvkhrTSIFIAHRLSTVV------DA----DEIIVLDQGK 657
Cdd:TIGR00956 254 ------TSANILDTTPLVAiyqcsqDAyelfDKVIVLYEGY 288
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
462-659 |
4.67e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSG-----ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAVGVV--PQD------ 528
Cdd:PRK15439 274 LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylPEDrqssgl 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 ---AVLFHNTiyYNLLYGNISASPEEVYAVAKLAGLHDAI-LRMPHGyDTQVGerglKLSGGEKQRVAIARAILKDPPVI 604
Cdd:PRK15439 353 yldAPLAWNV--CALTHNRRGFWIKPARENAVLERYRRALnIKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 605 LYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVA 659
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
472-654 |
8.65e-09 |
|
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: 58.64 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 472 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLEslrravgvVPQDAVL--FHNTI---YYNLLY- 542
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKIL-------------SGElkpNLGDYDEE--------PSWDEVLkrFRGTElqdYFKKLAn 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 543 GNISAS--PEEVYAVAKL--------------AGLHDAI---LRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPV 603
Cdd:COG1245 158 GEIKVAhkPQYVDLIPKVfkgtvrellekvdeRGKLDELaekLGLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 411147367 604 ILYDEATSSLDsITEE-TILGAMKDVVKHRTSIFiahrlstVVDADeIIVLD 654
Cdd:COG1245 234 YFFDEPSSYLD-IYQRlNVARLIRELAEEGKYVL-------VVEHD-LAILD 276
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
117-395 |
9.20e-09 |
|
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: 57.52 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 117 SLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVAT-MATAVLIGygvsragaAFFNEVRNAVFGKVAQNS 195
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALaLLGVFVVG--------AAANFGRVYLLRIAGERI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 196 IRRIAKNVFLHLHNLDLGFHLSRQTG---------------ALSKAIDRGTRGISFVLSALVfnllpIMFevmLVSgvly 260
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGelvsrlssdtsvvgkSLTQNLSDGLRSLVSGVGGIG-----MML---YIS---- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 261 ykcgAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGflKTYETA 340
Cdd:cd18573 141 ----PKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAK--KVDEVF 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 341 SLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDL-------VMVNGLLFQLS 395
Cdd:cd18573 215 DLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGslVASGELTVGDLtsflmyaVYVGSSVSGLS 278
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
114-404 |
1.10e-08 |
|
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: 57.02 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDS---------LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAGAAFFNEVR 184
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEgiangdlsyILRTGLLMLLL-----ALLGLIAGILAGYFAAKASQGFGRDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 185 NAVFGKVAQNSirriaknvflhLHNLDlgfHLSrqTGALskaIDRGTRGISFVLSAlVFNLL------PIMFevmLVSGV 258
Cdd:cd18548 76 KDLFEKIQSFS-----------FAEID---KFG--TSSL---ITRLTNDVTQVQNF-VMMLLrmlvraPIML---IGAII 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 259 LYYKCGAQFALVTLGTLGTYTAFTVAVTRW-RTRFRIEMNKadNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKT 336
Cdd:cd18548 133 MAFRINPKLALILLVAIPILALVVFLIMKKaIPLFKKVQKK--LDRLNRVVrENLTGIRVIRAFNREDYEEERFDKANDD 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 337 YETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTV 404
Cdd:cd18548 211 LTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMV 278
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
443-658 |
1.23e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.73 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 443 TATVAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL---FRFYEPQKGSIYLAGQNIQDVSlE 516
Cdd:cd03233 1 ASTLSWRNISFTTGKGRskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFA-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 517 SLRRAVGVVPQDAVLFHN-TIYynllygnisaspEEVYAVAKLAGlhDAILRmphgydtqvgerglKLSGGEKQRVAIAR 595
Cdd:cd03233 80 KYPGEIIYVSEEDVHFPTlTVR------------ETLDFALRCKG--NEFVR--------------GISGGERKRVSIAE 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 596 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKhrtsifiAHRLSTVVDA-----------DEIIVLDQGKV 658
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAD-------VLKTTTFVSLyqasdeiydlfDKVLVLYEGRQ 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
460-667 |
1.29e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.91 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-KGSIYLAGQNIQDVS-LESLRRAVGVVPQDAVlfHNTIY 537
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRK--RHGIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 YNLLYG-NISASPEEVY-------AVAKLAGLHDAILRM---PHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVILY 606
Cdd:TIGR02633 352 PILGVGkNITLSVLKSFcfkmridAAAELQIIGSAIQRLkvkTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 607 DEATSSLDSITEETILGAMKDVVKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGL 667
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHAL 490
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
203-418 |
1.56e-08 |
|
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: 56.74 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 203 VFLHLHNLDLGFHLSRQTGALskaIDRgTRGIS----FVLSALVFNLLPIMFEVMLVSGVLYYKcgAQFALVTLGTLGTY 278
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDT---VAR-VRELEsirqFLTGSALTLVLDLVFSVVFLAVMFYYS--PTLTLIVLASLPLY 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 279 TAFTVAVTRwRTRFRIEmNKADNDAGNAA--IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKsTSTLAmlNFGQS 356
Cdd:cd18588 155 ALLSLLVTP-ILRRRLE-EKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK-TANLS--NLASQ 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 357 AIFSVGLT---AIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 418
Cdd:cd18588 230 IVQLIQKLttlAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
465-677 |
1.85e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRR----AVGVVPQDAVLFHNTiy 537
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDPMTSLNP-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 538 ynllYGNISASPEEVYAVAKLAGLHDAI---LRM----------------PHgydtqvgerglKLSGGEKQRVAIARAIL 598
Cdd:PRK09473 113 ----YMRVGEQLMEVLMLHKGMSKAEAFeesVRMldavkmpearkrmkmyPH-----------EFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 675
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAiIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
..
gi 411147367 676 SE 677
Cdd:PRK09473 258 SI 259
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
456-614 |
1.95e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdvsleSLRRAvgvvpqdavlFHn 534
Cdd:PRK13538 10 ERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDE----------YH- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 tiyYNLLY-GNISA-----SPEE-VYAVAKLAGLHD-----AILRmphgydtQVGERGLK------LSGGEKQRVAIARA 596
Cdd:PRK13538 74 ---QDLLYlGHQPGiktelTALEnLRFYQRLHGPGDdealwEALA-------QVGLAGFEdvpvrqLSAGQQRRVALARL 143
|
170
....*....|....*...
gi 411147367 597 ILKDPPVILYDEATSSLD 614
Cdd:PRK13538 144 WLTRAPLWILDEPFTAID 161
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
114-412 |
2.51e-08 |
|
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: 55.90 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAkaMNIVVPFMFKYAVDSLNQMSGNMlnlsdapNTVATMATAVLIGygvsragaAFFNEVRNAVFGKVAQ 193
Cdd:cd18551 3 LALLLSLLGTA--ASLAQPLLVKNLIDALSAGGSSG-------GLLALLVALFLLQ--------AVLSALSSYLLGRTGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTG-----------ALSKAIDRGTrgISFVLSALVFNL-LPIMFevmLVSGVLyy 261
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGdlvsrvtndttLLRELITSGL--PQLVTGVLTVVGaVVLMF---LLDWVL-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 262 kcgaqfALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETAS 341
Cdd:cd18551 139 ------TLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAG 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147367 342 LKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV---MvngLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18551 213 LKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVaflL---YLFQLITPLSQLSSFFTQLQKAL 283
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
456-676 |
3.66e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNiqdVSLESLRRAV--GVV--PQD--- 528
Cdd:PRK11288 263 LKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP---IDIRSPRDAIraGIMlcPEDrka 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 -AVLFHNTIYYNLlygNISASPEEVYA--------VAKLAGLHDAILRM--PHGyDTQVGerglKLSGGEKQRVAIARAI 597
Cdd:PRK11288 340 eGIIPVHSVADNI---NISARRHHLRAgclinnrwEAENADRFIRSLNIktPSR-EQLIM----NLSGGNQQKAILGRWL 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 598 LKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGllANPHSIY 675
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ--ATERQAL 489
|
.
gi 411147367 676 S 676
Cdd:PRK11288 490 S 490
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
441-665 |
4.63e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 441 PQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlagqniqdvslESLRR 520
Cdd:PLN03073 504 PGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKV 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 521 AVGVVPQdavlfHNTIYYNLlygniSASPEeVYAVAKLAGLHDAILRMPHGYDTQVGERGLK----LSGGEKQRVAIARA 596
Cdd:PLN03073 573 RMAVFSQ-----HHVDGLDL-----SSNPL-LYMMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKI 641
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 597 ILKDPPVILYDEATSSLDSITEETILGAMkdVVKHRTSIFIAHRLSTVVDA-DEIIVLDQGKVAE-RGTHH 665
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
472-653 |
6.01e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 472 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLES-----LRRAVGVVPQDavlfhntiYYNLLY- 542
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKIL-------------SGElipNLGDYEEEPswdevLKRFRGTELQN--------YFKKLYn 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 543 GNISAS--PEEVYAVAK-LAGLHDAILRmphgydtQVGERGL-------------------KLSGGEKQRVAIARAILKD 600
Cdd:PRK13409 158 GEIKVVhkPQYVDLIPKvFKGKVRELLK-------KVDERGKldevverlglenildrdisELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 601 PPVILYDEATSSLDsITEE-TILGAMKDVVKHRTSIFIAHRLsTVVD--ADEIIVL 653
Cdd:PRK13409 231 ADFYFFDEPTSYLD-IRQRlNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
460-656 |
6.69e-08 |
|
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: 53.40 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 460 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ--KGSIYLAGQNIQdvslESLRRAVGVVPQDAVLFHN-TI 536
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KNFQRSTGYVEQQDVHSPNlTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 YYNLLYGnisaspeevyavAKLaglhdailrmphgydtqvgeRGLKLSggEKQRVAIARAILKDPPVILYDEATSSLDSI 616
Cdd:cd03232 97 REALRFS------------ALL--------------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 411147367 617 TEETILGAMKDVVKH-RTSIFIAHRLSTVVDA--DEIIVLDQG 656
Cdd:cd03232 143 AAYNIVRFLKKLADSgQAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
456-664 |
8.17e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF--RFYEPQKGSIYLAGQNIQDVSLESlRRAVGV--------- 524
Cdd:PRK09580 11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIfmafqypve 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGlkLSGGEKQRVAIARAILKDPPVI 604
Cdd:PRK09580 90 IPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 605 LYDEATSSLD----SITEETIlGAMKDvvKHRTSIFIAH--RLSTVVDADEIIVLDQGKVAERGTH 664
Cdd:PRK09580 168 ILDESDSGLDidalKIVADGV-NSLRD--GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
458-622 |
9.00e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVVPQ--DAVLFHN 534
Cdd:TIGR03719 333 GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 535 TIYynllygnisaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGGEKQRVAIARAIL 598
Cdd:TIGR03719 402 TVW------------EEI------SGGLDIIKlgkrEIPsrayvgrfnfKGSDQQkkVGQ----LSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|....*...
gi 411147367 599 KDPPVILYDEATSSLDSIT----EETIL 622
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETlralEEALL 487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
457-639 |
1.61e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 457 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgQNIQdvsleslrraVGVVPQD-AVLFHNT 535
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENAN----------IGYYAQDhAYDFEND 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 536 IyyNLLygnisaspeEVYAVAKLAGlHD-----AIL-RMPHGYDtQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 609
Cdd:PRK15064 399 L--TLF---------DWMSQWRQEG-DDeqavrGTLgRLLFSQD-DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
170 180 190
....*....|....*....|....*....|..
gi 411147367 610 TSSLD--SIteETILGAMKDVvkHRTSIFIAH 639
Cdd:PRK15064 466 TNHMDmeSI--ESLNMALEKY--EGTLIFVSH 493
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
465-660 |
1.71e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 465 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQ---DAVLFHN-TIYYN 539
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 540 L-------------LYGNISASPEevyavAKLAGLHDAILRMP-HGYDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 605
Cdd:PRK09700 362 MaisrslkdggykgAMGLFHEVDE-----QRTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 606 YDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDA-DEIIVLDQGKVAE 660
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
197-412 |
2.49e-07 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 52.86 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 197 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSAlvfNLLPIMFEVMLVSGVLYY--KCGAQFALVTLGT 274
Cdd:cd18589 69 SRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSE---NLSLLMWYLARGLFLFIFmlWLSPKLALLTALG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 275 LGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFL-KTYETASLKSTS-TLAMLN 352
Cdd:cd18589 146 LPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLqKTYRLNKKEAAAyAVSMWT 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 353 FGQSAIF-SVGltaIMVLASQGIVAGTLTVGDLVMVngLLFQL--SLPLNFLGTVYRETRQAL 412
Cdd:cd18589 226 SSFSGLAlKVG---ILYYGGQLVTAGTVSSGDLVTF--VLYELqfTSAVEVLLSYYPSVMKAV 283
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
128-412 |
2.68e-07 |
|
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: 53.02 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 128 NIVVPFMFKYAVDSLNQMSGNmlNLSDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLHL 207
Cdd:cd18780 12 NLALPYFFGQVIDAVTNHSGS--GGEEALRALNQAVLILLGVVLIG----SIATFLRSWLFTLAGERVVARLRKRLFSAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 208 HNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCgaqfALVTLGTLGTYTAFTVAvTR 287
Cdd:cd18780 86 IAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTS----WKLTLVMLSVVPPLSIG-AV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 288 WRTRFRIEMNKADND----AGNAAIDSLLNYETVKYFNNERYEAQRYDGflKTYETASL--KSTSTLAMLNFGQSAIFSV 361
Cdd:cd18780 161 IYGKYVRKLSKKFQDalaaASTVAEESISNIRTVRSFAKETKEVSRYSE--KINESYLLgkKLARASGGFNGFMGAAAQL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 411147367 362 GLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAV 289
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
175-392 |
2.78e-07 |
|
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: 52.84 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 175 AGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFH--LSRQTGALSKAIDRGT---RGI-SFVLSALVFNLlpi 248
Cdd:cd18578 63 IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDAsdvRGLvGDRLGLILQAI--- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 249 mfeVMLVSGV---LYYkcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERY 325
Cdd:cd18578 140 ---VTLVAGLiiaFVY--GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDY 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 326 EAQRYDGFLKTYETASLKStSTLAMLNFG--QSAIFSVglTAI-----MVLasqgIVAGTLTVGDLVMV-NGLLF 392
Cdd:cd18578 215 FLEKYEEALEEPLKKGLRR-ALISGLGFGlsQSLTFFA--YALafwygGRL----VANGEYTFEQFFIVfMALIF 282
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
114-412 |
3.24e-07 |
|
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: 52.48 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDS---------LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAGAAFFNEVR 184
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDalpqgdlglLVLLALGMVAV-----AVASALLGVVQTYLSARIGQGVMYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 185 NAVFGkvaqnsirriaknvflHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcG 264
Cdd:cd18550 76 VQLYA----------------HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLAL-D 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 265 AQFALVTLGTLgtytAFTVAVTRW--RTRFRIEMNKADNdagNAAIDSLLNyET--------VKYFNNERYEAQRYDGfl 334
Cdd:cd18550 139 WRLALLSLVLL----PLFVLPTRRvgRRRRKLTREQQEK---LAELNSIMQ-ETlsvsgallVKLFGREDDEAARFAR-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 335 KTYETASLKSTSTLAMLNFGQ--SAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18550 209 RSRELRDLGVRQALAGRWFFAalGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSL 288
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
458-614 |
3.45e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA-GQNI------------QDVsLESLRRAVGV 524
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVgylpqepqldpeKTV-RENVEEGVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VpQDAVLFHNTIYynLLYGNISASPEEVyaVAKLAGLHDAI------------------LRMPHGyDTQVGerglKLSGG 586
Cdd:PRK11819 98 V-KAALDRFNEIY--AAYAEPDADFDAL--AAEQGELQEIIdaadawdldsqleiamdaLRCPPW-DAKVT----KLSGG 167
|
170 180
....*....|....*....|....*...
gi 411147367 587 EKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
114-399 |
4.36e-07 |
|
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: 52.41 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNlsDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQ 193
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGG--VDFSGLLRILLLLLGLYLLS----ALFSYLQNRLMARVSQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKA---IDRGTRGISFVLSALVFNLLPI--MFEVMLV-SGVLyykcgaq 266
Cdd:cd18547 75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDiMSRVtndVDNISQALSQSLTQLISSILTIvgTLIMMLYiSPLL------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 267 fALVTLGTLGTYTAFTVAVTRW-RTRFRIEMNKadndAG--NAAID-SLLNYETVKYFNNERYEAQRYDGFLKTYETASL 342
Cdd:cd18547 148 -TLIVLVTVPLSLLVTKFIAKRsQKYFRKQQKA----LGelNGYIEeMISGQKVVKAFNREEEAIEEFDEINEELYKASF 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147367 343 KSTSTLAML--------NFGQSAIFSVGltAIMVLasqgivAGTLTVGDLV----MVNgllfQLSLPLN 399
Cdd:cd18547 223 KAQFYSGLLmpimnfinNLGYVLVAVVG--GLLVI------NGALTVGVIQaflqYSR----QFSQPIN 279
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
456-663 |
4.48e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 456 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDvsLESLRRA------------ 521
Cdd:CHL00131 17 VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILD--LEPEERAhlgiflafqypi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 522 --VGVVPQDavlFHNTIYYNLL--YGNISASPEEVYAV----AKLAGLHdailrmPHGYDTQVGErglKLSGGEKQRVAI 593
Cdd:CHL00131 95 eiPGVSNAD---FLRLAYNSKRkfQGLPELDPLEFLEIinekLKLVGMD------PSFLSRNVNE---GFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147367 594 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAH--RLSTVVDADEIIVLDQGKVAERGT 663
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIiLITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
114-411 |
6.60e-07 |
|
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: 51.72 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 114 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAgaaffnevRNAVFGKVA 192
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGVLLL-----AAAAYLAVVLAGWVAQRA--------QTRLTGRTG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 193 QNSIRRIAKNVFLHLHNLDLGFH--------LSRQTG---ALSKAIDRGtrgisfvLSALVFNLLPIMF-EVMLVsgVLy 260
Cdd:cd18546 68 ERLLYDLRLRVFAHLQRLSLDFHeretsgriMTRMTSdidALSELLQTG-------LVQLVVSLLTLVGiAVVLL--VL- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 261 ykcGAQFALVTLGTLgtytAFTVAVTRWrtrFRIEMNKADNDAGNAAIDSLLNY-ET------VKYFNNERYEAQRYDGF 333
Cdd:cd18546 138 ---DPRLALVALAAL----PPLALATRW---FRRRSSRAYRRARERIAAVNADLqETlagirvVQAFRRERRNAERFAEL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 334 LKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV---MVNGLLFQlslPLNFLGTVYRETRQ 410
Cdd:cd18546 208 SDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVaflLYLRRFFA---PIQQLSQVFDSYQQ 284
|
.
gi 411147367 411 A 411
Cdd:cd18546 285 A 285
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
462-716 |
1.07e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvSLESLRRAVGVVPQDAVLfHNTIYYNLL 541
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGI-ENIELKGLM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 542 YGNISASPEEVY-AVAKLAGLHDAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 620
Cdd:PRK13545 113 MGLTKEKIKEIIpEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 621 ILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANphsiYSEMwhtqssrvqnhdnpkweAKK 698
Cdd:PRK13545 182 CLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDH----YDEF-----------------LKK 240
|
250
....*....|....*...
gi 411147367 699 ENISKEEERKKLQEEIVN 716
Cdd:PRK13545 241 YNQMSVEERKDFREEQIS 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
459-659 |
1.31e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 459 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESL----------RRAVGVVPQ 527
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAInhgfalvteeRRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 528 DAVLFhNTIYYNL--------LYGNISASPEEVYAVaklaglhDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILK 599
Cdd:PRK10982 341 LDIGF-NSLISNIrnyknkvgLLDNSRMKSDTQWVI-------DSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLT 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 600 DPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 659
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSEMPELLGiTDRILVMSNGLVA 470
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
449-619 |
1.55e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 449 DNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlAGQNIQDVSLESLRRAVGvvPQd 528
Cdd:PRK11147 323 ENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLEVAYFDQHRAELD--PE- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 529 avlfhNTIYYNLLYGN----ISASPEEVyavakLAGLHDaILRMPHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVI 604
Cdd:PRK11147 398 -----KTVMDNLAEGKqevmVNGRPRHV-----LGYLQD-FLFHPKRAMTPVK----ALSGGERNRLLLARLFLKPSNLL 462
|
170
....*....|....*
gi 411147367 605 LYDEATSSLDSITEE 619
Cdd:PRK11147 463 ILDEPTNDLDVETLE 477
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
458-672 |
2.36e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQ-------KGSIYLAGQNIQDVSLESLRRAVGVVPQDA 529
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 530 V-LFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILK--------- 599
Cdd:PRK13547 93 QpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 600 DPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVV-DADEIIVLDQGKVAERGTHHGLLANPH 672
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVLTPAH 247
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
115-402 |
5.52e-06 |
|
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: 48.95 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 115 AISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFFneVRNAVFGkvaqn 194
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQL--------LRYALLILLLALLIGIFRFL--WRYLIFG----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 195 SIRRIAK----NVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYykcgAQFAL- 269
Cdd:cd18541 67 ASRRIEYdlrnDLFAHLLTLSPSFYQKNRTGDL---MARATNDLNAVRMALGPGILYLVDALFLGVLVLV----MMFTIs 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 270 --VTLGTLGTYTAFTVAVTRW----RTRFRI------EMNkadndagNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTY 337
Cdd:cd18541 140 pkLTLIALLPLPLLALLVYRLgkkiHKRFRKvqeafsDLS-------DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEY 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147367 338 ETASLKSTSTLAMlnFGQSAIFSVGLTAIMVLA--SQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLG 402
Cdd:cd18541 213 VEKNLRLARVDAL--FFPLIGLLIGLSFLIVLWygGRLVIRGTITLGDLVAFNSYLGMLIWPMMALG 277
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
462-669 |
6.32e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 462 LSG-----ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVlfHNTI 536
Cdd:PRK10762 263 LSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS-----------PQDGL--ANGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 537 YY--------NLLYG-----NISASP--------------EEVYAVAKLAGLHDaiLRMPhGYDTQVGerglKLSGGEKQ 589
Cdd:PRK10762 330 VYisedrkrdGLVLGmsvkeNMSLTAlryfsraggslkhaDEQQAVSDFIRLFN--IKTP-SMEQAIG----LLSGGNQQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 590 RVAIARAILKDPPVILYDEATSSLDsiteetiLGAMKDVVKhRTSIFIAHRLSTVV----------DADEIIVLDQGKV- 658
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVD-------VGAKKEIYQ-LINQFKAEGLSIILvssempevlgMSDRILVMHEGRIs 474
|
250
....*....|....*
gi 411147367 659 ----AERGTHHGLLA 669
Cdd:PRK10762 475 geftREQATQEKLMA 489
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
194-412 |
6.67e-06 |
|
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: 48.40 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLP----IMFEVMLVSGVLYYKCGAQFAL 269
Cdd:cd18556 74 ELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPpllqLIIAIVVILSSGDYFVAALFLL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 270 VTLgtlgTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETAS---LKSTS 346
Cdd:cd18556 154 YAV----LFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQkryWKLTF 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 347 TLAMLNFGQSAIFsVGLTAIMVLAsqGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 412
Cdd:cd18556 230 KMLILNSLLNVIL-FGLSFFYSLY--GVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
582-677 |
7.52e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 7.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 582 KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|....*....
gi 411147367 659 AERGTHHGLLANPHSIYSE 677
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQ 256
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
116-416 |
7.68e-06 |
|
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: 48.57 E-value: 7.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 116 ISLGFLGGAKAMNI--VVPFMFKYAVDSLNQmsGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQ 193
Cdd:cd18554 1 IIITIVIGLVRFGIplLLPLILKYIVDDVIQ--GSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEY---YRQYFAQWIAN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 194 NSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-SKAIDRGTRGISFVLSALVfNLLPIMFEVMLVSGVLyYKCGAQFALVTL 272
Cdd:cd18554 76 KILYDIRKDLFDHLQKLSLRYYANNRSGEIiSRVINDVEQTKDFITTGLM-NIWLDMITIIIAICIM-LVLNPKLTFVSL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 273 GTLGTYtafTVAVTRWRTRFRI---EMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTS--- 346
Cdd:cd18554 154 VIFPFY---ILAVKYFFGRLRKltkERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRwna 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147367 347 -TLAMLNfgqsAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMN 416
Cdd:cd18554 231 kTFSAVN----TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMD 297
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
156-399 |
7.91e-06 |
|
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: 48.35 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 156 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGIS 235
Cdd:cd18566 34 PNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIRE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 236 FVLSALVFNLLPIMFEVMLVSGVLYYkcGAQFALVTLGTLGTYTAFTVAV-TRWRTRFRiEMNKADNDAGNAAIDSLLNY 314
Cdd:cd18566 114 FLTGQALLALLDLPFVLIFLGLIWYL--GGKLVLVPLVLLGLFVLVAILLgPILRRALK-ERSRADERRQNFLIETLTGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 315 ETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNfGQSAIFSVgLTAIMVLA--SQGIVAGTLTVGDLVMVNGLLF 392
Cdd:cd18566 191 HTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ-TLGQLFSQ-VSMVAVVAfgALLVINGDLTVGALIACTMLSG 268
|
....*..
gi 411147367 393 QLSLPLN 399
Cdd:cd18566 269 RVLQPLQ 275
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
458-658 |
8.23e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 8.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 458 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK-GSIYLAGQniqDVSLESLRRAV-------------- 522
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGK---PVKIRNPQQAIaqgiamvpedrkrd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 523 GVVPQDAVLfHNTIYYNL----LYGNISASPEEVYAVAKLAGLHdaiLRMPHGyDTQVGerglKLSGGEKQRVAIARAIL 598
Cdd:PRK13549 351 GIVPVMGVG-KNITLAALdrftGGSRIDDAAELKTILESIQRLK---VKTASP-ELAIA----RLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147367 599 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
583-658 |
8.94e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 8.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147367 583 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDvvkHRTSI-FIAHRLSTVVD-ADEIIVLDQGKV 658
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT---FQGSIiFISHDRSFIRNmATRIVDLDRGKL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
469-614 |
1.02e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 469 VPA-GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQNIQDVsLESLRRA---VGVVPQDAVLFH 533
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNY-FTKLLEGdvkVIVKPQYVDLIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 534 NTIYynllyGNISASPEEVYAVAKLAGLHDAiLRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSL 613
Cdd:cd03236 101 KAVK-----GKVGELLKKKDERGKLDELVDQ-LELRHVLDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
.
gi 411147367 614 D 614
Cdd:cd03236 171 D 171
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
581-663 |
4.24e-05 |
|
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: 44.87 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 581 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVDADEIIVLDQGKV 658
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
....*
gi 411147367 659 AERGT 663
Cdd:cd03222 150 GVYGI 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
469-641 |
4.36e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 469 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQ-DAVlfhntiyYNLLYGNisa 547
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQfDAI-------DDLLTGR--- 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 548 spEEVYAVAKLAGLHDAILRMPHGYDTQvgERGLKL---------SGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 618
Cdd:TIGR01257 2031 --EHLYLYARLRGVPAEEIEKVANWSIQ--SLGLSLyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180
....*....|....*....|....
gi 411147367 619 ETILGAMKDVVKH-RTSIFIAHRL 641
Cdd:TIGR01257 2107 RMLWNTIVSIIREgRAVVLTSHSM 2130
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
126-407 |
6.95e-05 |
|
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: 45.58 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 126 AMNIVVPFMFKYAVDSLNqMSGNMLNLsdapNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVaQNSI-RRIAKNVF 204
Cdd:cd18555 16 LLTLLIPILTQYVIDNVI-VPGNLNLL----NVLGIGILILFLLYGL-------FSFLRGYIIIKL-QTKLdKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 205 LHLHNLDLGFHLSRQTGAL-----SKAIDRG---TRGISFVLSALvfnLLPIMFEVMLVSGVLYykcgaqfALVTLgTLG 276
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLlfranSNVYIRQilsNQVISLIIDLL---LLVIYLIYMLYYSPLL-------TLIVL-LLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 277 TYTAFTVAVTRWRTRFRIEMNKADN-DAGNAAIDSLLNYETVKYFNNERyeaQRYDGFLKTYET---ASLKSTSTLAMLN 352
Cdd:cd18555 152 LLIVLLLLLTRKKIKKLNQEEIVAQtKVQSYLTETLYGIETIKSLGSEK---NIYKKWENLFKKqlkAFKKKERLSNILN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 411147367 353 FGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRE 407
Cdd:cd18555 229 SISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQ 283
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
470-651 |
1.19e-04 |
|
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: 43.12 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 470 PAGKKVAIVGGSGSGKSTIVR-----LLFRFYEPQKGSIYLAGQNIQDVSLEslrrAVGVVPQdavlfhntiyynllygn 544
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDaiglaLGGAQSATRRRSGVKAGCIVAAVSAE----LIFTRLQ----------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 545 isaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAI----LKDPPVILYDEATSSLDSITEET 620
Cdd:cd03227 78 --------------------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119
|
170 180 190
....*....|....*....|....*....|..
gi 411147367 621 ILGAMKD-VVKHRTSIFIAHRLSTVVDADEII 651
Cdd:cd03227 120 LAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
168-405 |
1.29e-04 |
|
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: 44.64 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 168 IGY-GVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTrgisfvlsALVFNLL 246
Cdd:cd18590 39 IGLmCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDT--------TLMSRSV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 247 PIMFEVMLVS-----GVLYYKCGA--QFALVTL-GTLGTYTAFTVAVTRWRtRFRIEMNKADNDAGNAAIDSLLNYETVK 318
Cdd:cd18590 111 ALNANVLLRSlvktlGMLGFMLSLswQLTLLTLiEMPLTAIAQKVYNTYHQ-KLSQAVQDSIAKAGELAREAVSSIRTVR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 319 YFNNERYEAQRYDGFLK-TYETASLKSTSTLAMLNFGQsaIFSVGLTAIMV-LASQGIVAGTLTVGDLVMVngLLFQLSL 396
Cdd:cd18590 190 SFKAEEEEACRYSEALErTYNLKDRRDTVRAVYLLVRR--VLQLGVQVLMLyCGRQLIQSGHLTTGSLVSF--ILYQKNL 265
|
....*....
gi 411147367 397 PLNFLGTVY 405
Cdd:cd18590 266 GSYVRTLVY 274
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
477-614 |
1.30e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 477 IVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvVPQDAVLFHN-------TIYYNL-LYGNISAS 548
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----------KPYCTYIGHNlglklemTVFENLkFWSEIYNS 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147367 549 PEEVYAVAKLAGLHDAIlrmphgydtqvGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 614
Cdd:PRK13541 101 AETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
302-385 |
1.30e-04 |
|
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: 44.40 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 302 DAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFgqSAIFSV--GLTAIMVLASQGIVAGTL 379
Cdd:cd18575 173 DLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTA--LVIFLVfgAIVFVLWLGAHDVLAGRM 250
|
....*.
gi 411147367 380 TVGDLV 385
Cdd:cd18575 251 SAGELS 256
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
233-405 |
1.31e-04 |
|
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: 44.61 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 233 GISFVLSALVFNLLPIMFEVMLVSGVlYYKcgaqfalvtlgtlgtytaftvavtrwrtRFRIEMNKADNDAGNAAIDSLL 312
Cdd:cd18784 133 KLSWQLSLVTLIGLPLIAIVSKVYGD-YYK----------------------------KLSKAVQDSLAKANEVAEETIS 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 313 NYETVKYFNNERYEAQRYDGFLKtyETASLKSTSTLAMLNF-GQSAIFSVGLTAIMvLASQG--IVAGTLTVGDLVMVng 389
Cdd:cd18784 184 SIRTVRSFANEDGEANRYSEKLK--DTYKLKIKEALAYGGYvWSNELTELALTVST-LYYGGhlVITGQISGGNLISF-- 258
|
170
....*....|....*...
gi 411147367 390 LLFQLSL--PLNFLGTVY 405
Cdd:cd18784 259 ILYQLELgsCLESVGSVY 276
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
446-627 |
1.61e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 446 VAFDNVHFEYieGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGV 524
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 525 VPQ--DAVLFHNTIYynllygnisaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGG 586
Cdd:PRK11819 392 VDQsrDALDPNKTVW------------EEI------SGGLDIIKvgnrEIPsrayvgrfnfKGGDQQkkVGV----LSGG 449
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 411147367 587 EKQRVAIARAILKDPPVILYDEATSSLDSiteETiLGAMKD 627
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDV---ET-LRALEE 486
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
577-662 |
4.10e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 577 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD--ADEIIVLD 654
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218
|
....*...
gi 411147367 655 QGKVAERG 662
Cdd:NF000106 219 RGRVIADG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
476-692 |
9.93e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 476 AIVGGSGSGKSTIVRLLfrfyEPQKGSIYLAGqniqDVSL-------ESLRRAVGVVPQDAVlfHN---TIYYNLLYGNI 545
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVL----AGRKTGGYIEG----DIRIsgfpkkqETFARISGYCEQNDI--HSpqvTVRESLIYSAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 546 SASPEEVYAVAK------------LAGLHDAILRMPhgydtqvGERGlkLSGGEKQRVAIARAILKDPPVILYDEATSSL 613
Cdd:PLN03140 980 LRLPKEVSKEEKmmfvdevmelveLDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 614 DSITEETILGAMKDVVKH-RTSIFIAHRLST-VVDA-DEIIVLDQ-GKVAERGThhgLLANPHSI--YSEMWHtQSSRVQ 687
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTgRTVVCTIHQPSIdIFEAfDELLLMKRgGQVIYSGP---LGRNSHKIieYFEAIP-GVPKIK 1126
|
....*
gi 411147367 688 NHDNP 692
Cdd:PLN03140 1127 EKYNP 1131
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
573-669 |
1.06e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 573 DTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA---- 647
Cdd:PLN03140 326 DTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlf 405
|
90 100
....*....|....*....|..
gi 411147367 648 DEIIVLDQGKVAERGTHHGLLA 669
Cdd:PLN03140 406 DDIILLSEGQIVYQGPRDHILE 427
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
126-385 |
2.11e-03 |
|
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: 40.90 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 126 AMNIVVPFMFKYAVDSLNQmSGNMlnlsdapNTVATMATAVLIGYGVsRAGAAFFNEVRNAVFGKVAQNSIRRiakNVFL 205
Cdd:cd18549 16 ALDLVFPLIVRYIIDDLLP-SKNL-------RLILIIGAILLALYIL-RTLLNYFVTYWGHVMGARIETDMRR---DLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 206 HLHNLDLGFHLSRQTGALSkaidrgTRGIS--FVLSALVFNLLpimfEVMLVSGVLYykCGA---------QFALVTLGT 274
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLM------SRITNdlFDISELAHHGP----EDLFISIITI--IGSfiilltinvPLTLIVFAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 275 LGTYTAFTVAVT-RWRTRFRieMNKADNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETAslKSTSTLAMLN 352
Cdd:cd18549 152 LPLMIIFTIYFNkKMKKAFR--RVREKIGEINAQLeDSLSGIRVVKAFANEEYEIEKFDEGNDRFLES--KKKAYKAMAY 227
|
250 260 270
....*....|....*....|....*....|....*
gi 411147367 353 FGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDLV 385
Cdd:cd18549 228 FFSGMNFFTNLLNLVVLVAGGyfIIKGEITLGDLV 262
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
163-395 |
6.51e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 39.11 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 163 ATAVLIGYGVSRAGAAFFNEV----RNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDR--------- 229
Cdd:cd18782 37 DLATLYVIGVVMLVAALLEAVltalRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISEldtirgflt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 230 GTRGISFVLSALVFNLLPIMFevmLVSGVLyykcgaqfALVTLGTLGTYTAFTVAVTRwRTRFRIEMNKADNDAGNAA-I 308
Cdd:cd18782 117 GTALTTLLDVLFSVIYIAVLF---SYSPLL--------TLVVLATVPLQLLLTFLFGP-ILRRQIRRRAEASAKTQSYlV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147367 309 DSLLNYETVKYFNNE---RYEAQ-RYDGFL-KTYETASLKSTS--TLAMLNFGQSAIFsVGLTAIMVLAsqgivaGTLTV 381
Cdd:cd18782 185 ESLTGIQTVKAQNAElkaRWRWQnRYARSLgEGFKLTVLGTTSgsLSQFLNKLSSLLV-LWVGAYLVLR------GELTL 257
|
250 260
....*....|....*....|.
gi 411147367 382 GDLV-------MVNGLLFQLS 395
Cdd:cd18782 258 GQLIafrilsgYVTGPILRLS 278
|
|
| |
