|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-571 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 626.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 1 MKSFRKLLQYLKPYMFFAIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYS 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 81 TKAAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFP 160
Cdd:COG1132 86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 161 ILLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLIS 240
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 241 LMMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRVQQVLNTEVDII 320
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 321 SAANAIEPEKIEGNIEFKNVSYSYtKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV 400
Cdd:COG1132 326 DPPGAVPLPPVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 401 KTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQR 480
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
570
....*....|.
gi 1265247244 561 SEVYQEIYLSQ 571
Cdd:COG1132 565 GGLYARLYRLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-571 |
1.15e-129 |
|
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: 396.13 E-value: 1.15e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 3 SFRKLLQYLKPY---MFFAIIGPLFMVLevaMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMY 79
Cdd:COG2274 143 GLRWFLRLLRRYrrlLLQVLLASLLINL---LALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 80 STKAAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVtNDITSIQSAMT-MTLRVLVRGPLLFMGSIIIVFVtAREL 158
Cdd:COG2274 220 LLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTgSLLTALLDLLFVLIFLIVLFFY-SPPL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 159 FPILLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQL 238
Cdd:COG2274 298 ALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 239 ISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRVQQVLNTEVD 318
Cdd:COG2274 378 SNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 319 IISAANAIEPEKIEGNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGI 398
Cdd:COG2274 458 REEGRSKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 399 DVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQK 478
Cdd:COG2274 538 DLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQR 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 479 QRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLL 558
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697
|
570
....*....|...
gi 1265247244 559 ERSEVYQEIYLSQ 571
Cdd:COG2274 698 ARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-568 |
3.62e-122 |
|
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: 372.13 E-value: 3.62e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 3 SFRKLLQYLKPYMFFAIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTK 82
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 83 AAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPIL 162
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 163 LVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLM 242
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 243 MPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRVQQVLNT--EVDii 320
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSppEKD-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 321 saANAIEPEKIEGNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV 400
Cdd:TIGR02203 319 --TGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 401 KTYDLQKLRASIGFVPQKALLFSGSIEENLRYGK-ENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQ 479
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 480 RVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLE 559
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA 556
|
....*....
gi 1265247244 560 RSEVYQEIY 568
Cdd:TIGR02203 557 RNGLYAQLH 565
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
5-567 |
4.62e-118 |
|
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: 361.71 E-value: 4.62e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 5 RKLLQYLKPYMFFAIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYvIKMGLLMIGAAALGLVGGLGCMMYS-TKA 83
Cdd:TIGR02204 7 AALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGL-LNRYFAFLLVVALVLALGTAARFYLvTWL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 84 AVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILL 163
Cdd:TIGR02204 86 GERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 164 VVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMM 243
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 244 PIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRVQQVLNTEVDIISAA 323
Cdd:TIGR02204 246 AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 324 NAIE-PEKIEGNIEFKNVSYSY-TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVK 401
Cdd:TIGR02204 326 HPKTlPVPLRGEIEFEQVNFAYpARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 402 TYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRV 481
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRI 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 482 SIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERS 561
Cdd:TIGR02204 486 AIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKG 565
|
....*.
gi 1265247244 562 EVYQEI 567
Cdd:TIGR02204 566 GLYARL 571
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
18-309 |
6.86e-111 |
|
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: 333.21 E-value: 6.86e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 18 AIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFA 97
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 98 KIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIA 177
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 178 SKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVAT 257
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 258 LWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
335-568 |
9.33e-99 |
|
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: 299.92 E-value: 9.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIY 568
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
248-564 |
9.33e-96 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 304.82 E-value: 9.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 248 LVVSGGIVATLWIGGEKVFNGTLRVGAiLAFIN-YLNIILMSLMSISMVFIQIARAFPSADRVQQVLNTEVDIISAANAI 326
Cdd:COG5265 271 LIIALGLTAMMLMAAQGVVAGTMTVGD-FVLVNaYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 327 EPEKIEGNIEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQ 406
Cdd:COG5265 350 PLVVGGGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARA 486
Cdd:COG5265 429 SLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIART 508
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVY 564
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
83-568 |
3.51e-95 |
|
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: 302.07 E-value: 3.51e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 83 AAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAmtmTLRVLVrgPLL--FMGSIIIVFVTAR---- 156
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNL---YLRVLL--PLLvaLLVILAAVAFLAFfspa 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 157 --ELFPILLVVVPILLLAIILIASKASGtfKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIR 234
Cdd:COG4987 157 laLVLALGLLLAGLLLPLLAARLGRRAG--RRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRR 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 235 AVQLISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLRvGAILAFInylniILMSL------MSISMVFIQIARAFPSADR 308
Cdd:COG4987 235 LARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALL-----VLAALalfealAPLPAAAQHLGRVRAAARR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 309 VQQVLNTEVDIISAANAIEPEKiEGNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDV 388
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPG-GPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 389 DQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQ 468
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 469 GATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGEL 548
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRI 547
|
490 500
....*....|....*....|
gi 1265247244 549 VGNGTHEQLLERSEVYQEIY 568
Cdd:COG4987 548 VEQGTHEELLAQNGRYRQLY 567
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
335-571 |
3.72e-93 |
|
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: 285.59 E-value: 3.72e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSY-TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIG 413
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPI 493
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 494 LILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIYLSQ 571
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-560 |
3.52e-91 |
|
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: 280.27 E-value: 3.52e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYtKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASI 412
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLER 560
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
335-571 |
3.23e-89 |
|
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: 275.26 E-value: 3.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIYLSQ 571
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-574 |
5.86e-88 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 283.83 E-value: 5.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 1 MKSFRKLLQYLKPYMFFAIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGaaaLGLVGGLG----- 75
Cdd:PRK11176 10 WQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIG---LMILRGITsfiss 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 76 -CMMY-STKAAVNfatdIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFV 153
Cdd:PRK11176 87 yCISWvSGKVVMT----MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 154 TARELFPILLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINI 233
Cdd:PRK11176 163 YSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 234 RAVQLISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRVQQVL 313
Cdd:PRK11176 243 KMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAIL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 314 N--TEVDIisaaNAIEPEKIEGNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQG 391
Cdd:PRK11176 323 DleQEKDE----GKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 392 EICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENA-THDELEVAAASACATEFINKLEESYQYNLTQGA 470
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 471 TNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVG 550
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVE 558
|
570 580
....*....|....*....|....
gi 1265247244 551 NGTHEQLLERSEVYQEIYLSQGGN 574
Cdd:PRK11176 559 RGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
5-564 |
1.71e-86 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 283.15 E-value: 1.71e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 5 RKLLQYLKPYMFFAIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDL----NYVIKMGLLMIGAAALGLVGGlGCMMYs 80
Cdd:TIGR00958 150 FRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPpalaSAIFFMCLLSIASSVSAGLRG-GSFNY- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 81 TKAAVNFAtdIRKDVFAK-----IETFSSNNrdsfgTGKLLTIVTNDITSIQSAMTMTLRVLVR------GPLLFM--GS 147
Cdd:TIGR00958 228 TMARINLR--IREDLFRSllrqdLGFFDENK-----TGELTSRLSSDTQTMSRSLSLNVNVLLRnlvmllGLLGFMlwLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 148 IIIVFVTareLFPILLVVVPilllaiiliaSKASGTF-----KKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFG 222
Cdd:TIGR00958 301 PRLTMVT---LINLPLVFLA----------EKVFGKRyqllsEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 223 SVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARA 302
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 303 FPSADRVQQVLNTEVDIiSAANAIEPEKIEGNIEFKNVSYSY-TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKL 381
Cdd:TIGR00958 448 VGASEKVFEYLDRKPNI-PLTGTLAPLNLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAAL 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 382 LPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEES 461
Cdd:TIGR00958 527 LQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNG 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 462 YQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTAlkTKYKGTTTLLIASKISSIMDADKIL 541
Cdd:TIGR00958 607 YDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRLSTVERADQIL 684
|
570 580
....*....|....*....|...
gi 1265247244 542 VLDNGELVGNGTHEQLLERSEVY 564
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQGCY 707
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
202-560 |
5.74e-86 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 278.77 E-value: 5.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 202 LSGVRVIKAYVRQKYEIAQFGSVntnltkinirAVQLISLMMPII--MLVVSGG--------IVATLWIGGEKVFNGTLR 271
Cdd:PRK13657 202 IGNVSVVQSYNRIEAETQALRDI----------ADNLLAAQMPVLswWALASVLnraastitMLAILVLGAALVQKGQLR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 272 VGAILAFINYLNIILMSLMSISMVFIQIaraFPSADRVQ---QVLNTEVDIISAANAIEPEKIEGNIEFKNVSYSYtKNN 348
Cdd:PRK13657 272 VGEVVAFVGFATLLIGRLDQVVAFINQV---FMAAPKLEeffEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSY-DNS 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 349 EYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEE 428
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIED 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSE 508
Cdd:PRK13657 428 NIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 509 ATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLER 560
Cdd:PRK13657 508 AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-560 |
1.01e-82 |
|
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: 269.32 E-value: 1.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 1 MKSFRK-LLQYLKPYMFFAIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRD-----LNYVIKMGLLMIGAAALGLVGGL 74
Cdd:COG4988 1 QKPLDKrLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAplsalLPLLGLLLAVLLLRALLAWLRER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 75 gcmmYSTKAAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQS-----------AMTMTLRVLVR---- 139
Cdd:COG4988 81 ----AAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGyfarylpqlflAALVPLLILVAvfpl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 140 -----------GPL--LFMgsIIIVFVTARELfpillvvvpilllaiiliaskasgtfKKVQEALDKVNTKLQENLSGVR 206
Cdd:COG4988 157 dwlsglillvtAPLipLFM--ILVGKGAAKAS--------------------------RRQWRALARLSGHFLDRLRGLT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 207 VIKAYVRQKYEIAQFGSVNTNLTKINIR--AVQLISLMMpiIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAfinylnI 284
Cdd:COG4988 209 TLKLFGRAKAEAERIAEASEDFRKRTMKvlRVAFLSSAV--LEFFASLSIALVAVYIGFRLLGGSLTLFAALF------V 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 285 ILMSlmsiSMVFI---QIARAF-------PSADRVQQVLNTEVDIISAANAIEPEKIEGNIEFKNVSYSYTKNNEyVLKD 354
Cdd:COG4988 281 LLLA----PEFFLplrDLGSFYharangiAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP-ALDG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 355 ISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGK 434
Cdd:COG4988 356 LSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 435 ENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTA 514
Cdd:COG4988 436 PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA 515
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 1265247244 515 LKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG4988 516 LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-547 |
4.79e-80 |
|
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: 249.22 E-value: 4.79e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLrygkenathdelevaaasacatefinkleesyqynltqgatnLSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGE 547
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-553 |
4.60e-76 |
|
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: 240.86 E-value: 4.60e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASI 412
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSGSIEENLRYGKEnATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGT 553
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
184-571 |
7.27e-71 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 238.07 E-value: 7.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 184 FKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVsgGIVATLWIGGE 263
Cdd:PRK10789 165 FKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAI--GMANLLAIGGG 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 264 K--VFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRVQQVLNTEVDIISAANAIEPEKIEGNIEFKnvS 341
Cdd:PRK10789 243 SwmVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIR--Q 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 342 YSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALL 421
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 422 FSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 502 AVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIYLSQ 571
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
335-571 |
7.91e-71 |
|
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: 227.75 E-value: 7.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIYLSQ 571
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-552 |
3.31e-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: 222.85 E-value: 3.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASI 412
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKtKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNG 552
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLR-QLLGDKTLIIITHRPSLLDlVDRIIVMDSGRIVADG 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
328-548 |
1.57e-63 |
|
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: 208.09 E-value: 1.57e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 328 PEKIEGNIEFKNVSYSY-TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQ 406
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARA 486
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGEL 548
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
83-527 |
2.24e-60 |
|
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: 209.14 E-value: 2.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 83 AAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSamtMTLRVLVrgPL---LFMGSIIIVFVTAreLF 159
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQD---LYVRVIV--PAgvaLVVGAAAVAAIAV--LS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 160 PILLVVVPILLLAIILIASKASGTFKKVQEALDK-----VNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIR 234
Cdd:TIGR02868 153 VPAALILAAGLLLAGFVAPLVSLRAARAAEQALArlrgeLAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERR 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 235 AVQLISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLrVGAILAFInylniILMSL------MSISMVFIQIARAFPSADR 308
Cdd:TIGR02868 233 AAAATALGAALTLLAAGLAVLGALWAGGPAVADGRL-APVTLAVL-----VLLPLaafeafAALPAAAQQLTRVRAAAER 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 309 VQQVLNTEVDI----ISAANAIEPEKIegNIEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPR 384
Cdd:TIGR02868 307 IVEVLDAAGPVaegsAPAAGAVGLGKP--TLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 385 LYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQY 464
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDT 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 465 NLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLI 527
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLI 526
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
246-568 |
6.43e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.91 E-value: 6.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 246 IMLVVSG-GIVATLWIGGEKVFNGTLRvGAILAFINYLNIILM-SLMSISMVFIQIARAFPSADRVQQVLNTEVDIISAA 323
Cdd:PRK11160 250 LMILANGlTVVLMLWLAAGGVGGNAQP-GALIALFVFAALAAFeALMPVAGAFQHLGQVIASARRINEITEQKPEVTFPT 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 324 NAiEPEKIEGNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTY 403
Cdd:PRK11160 329 TS-TAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 404 DLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELevaaasacaTEFINK------LEESYQYN--LTQGATNLSG 475
Cdd:PRK11160 408 SEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEAL---------IEVLQQvgleklLEDDKGLNawLGEGGRQLSG 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 476 GQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHE 555
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQ 558
|
330
....*....|...
gi 1265247244 556 QLLERSEVYQEIY 568
Cdd:PRK11160 559 ELLAQQGRYYQLK 571
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-549 |
1.32e-58 |
|
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: 194.55 E-value: 1.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASI 412
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSGSIEENL-RYGKenatHDELEVAAAsacatefinkleesyqYNLTQGATNLSGGQKQRVSIARALVRKP 491
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLdPFDE----YSDEEIYGA----------------LRVSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELV 549
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-309 |
4.92e-57 |
|
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: 193.15 E-value: 4.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAK 98
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 99 IETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIAS 178
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 179 KASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATL 258
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 259 WIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd07346 242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
183-568 |
1.57e-56 |
|
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: 202.28 E-value: 1.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 183 TFKK----VQEALDKVNTKLQENLSGVRVIKA-------YVRQKYEIAQFgsVNTNLTKINIRAVQ-LISLMMPIIMLVV 250
Cdd:TIGR01193 318 TFNKlnhdAMQANAVLNSSIIEDLNGIETIKSltseaerYSKIDSEFGDY--LNKSFKYQKADQGQqAIKAVTKLILNVV 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 251 sggivaTLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRVQQVLNTEVDIISAANAIEPEK 330
Cdd:TIGR01193 396 ------ILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 331 IEGNIEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRA 410
Cdd:TIGR01193 470 LNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 411 SIGFVPQKALLFSGSIEENLRYG-KENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVR 489
Cdd:TIGR01193 549 FINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLT 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALkTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIY 568
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-573 |
5.76e-55 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 195.71 E-value: 5.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 1 MKSFRK-------LLQYLKPYMFFAIIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGL------LMIGAAA 67
Cdd:PRK10790 1 MRSFSQlwptlkrLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLaaayvgLQLLAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 68 LGLVGGLgcmMYStKAAVNFATDIRKDVF-----AKIETFssnnrDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPL 142
Cdd:PRK10790 81 LHYAQSL---LFN-RAAVGVVQQLRTDVMdaalrQPLSAF-----DTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 143 LFMGSIIIVFVTARELFPILLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYvRQKyeiAQFG 222
Cdd:PRK10790 152 LIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF-RQQ---ARFG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 223 ----SVNTNLTKINIRAVQLIS-LMMPIIML---VVSGGIVATLWIGGEkvfnGTLRVGAILAFINYL---NIILMSLMS 291
Cdd:PRK10790 228 ermgEASRSHYMARMQTLRLDGfLLRPLLSLfsaLILCGLLMLFGFSAS----GTIEVGVLYAFISYLgrlNEPLIELTT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 292 ISMVFIQIA----RAFPSADRVQQVLNTEVDIISAanaiepekieGNIEFKNVSYSYtKNNEYVLKDISFSIQKGEKVGI 367
Cdd:PRK10790 304 QQSMLQQAVvageRVFELMDGPRQQYGNDDRPLQS----------GRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVAL 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 368 IGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAA 447
Cdd:PRK10790 373 VGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 448 SACAtEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLI 527
Cdd:PRK10790 453 VQLA-ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVI 531
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1265247244 528 ASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIY-LSQGG 573
Cdd:PRK10790 532 AHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYqLQLAG 578
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
19-309 |
1.30e-53 |
|
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: 184.17 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAK 98
Cdd:cd18542 2 LLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 99 IETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIAS 178
Cdd:cd18542 82 LQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 179 KASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATL 258
Cdd:cd18542 162 KVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 259 WIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18542 242 WVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
58-543 |
8.07e-52 |
|
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: 185.95 E-value: 8.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 58 MGLLMIGAAALGLVGGLgcmmYSTKAAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITS-----------I 126
Cdd:TIGR02857 50 LALVLLLRALLGWLQER----AAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEAldgyfarylpqL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 127 QSAMTMTLRVLVRGPLLFMGSIIIVFVTAR--ELFPILLVvvpilllaiiliaSKASGTFKKVQEALDKVNTKLQENLSG 204
Cdd:TIGR02857 126 VLAVIVPLAILAAVFPQDWISGLILLLTAPliPIFMILIG-------------WAAQAAARKQWAALSRLSGHFLDRLRG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 205 VRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVvsggivATLWIGGEKVFNG-TLRVGAILAFINYLN 283
Cdd:TIGR02857 193 LPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELF------ATLSVALVAVYIGfRLLAGDLDLATGLFV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 284 IIL-----MSLMSISMVFIQIARAFPSADRVQQVLntevdiiSAANAIEPEKIE------GNIEFKNVSYSYtKNNEYVL 352
Cdd:TIGR02857 267 LLLapefyLPLRQLGAQYHARADGVAAAEALFAVL-------DAAPRPLAGKAPvtaapaSSLEFSGVSVAY-PGRRPAL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 353 KDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRY 432
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 433 GKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQ 512
Cdd:TIGR02857 419 ARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVL 498
|
490 500 510
....*....|....*....|....*....|.
gi 1265247244 513 TALKTKYKGTTTLLIASKISSIMDADKILVL 543
Cdd:TIGR02857 499 EALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
222-560 |
3.47e-51 |
|
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: 184.95 E-value: 3.47e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 222 GSVNTNLTKInIRavqlisLMMPIIMLvvsgGIVATLwiggekVFNGTLRVGAILAfinylNIILMS--LMSISMV---- 295
Cdd:COG4618 238 AGGFSALSKF-LR------LLLQSAVL----GLGAYL------VIQGEITPGAMIA-----ASILMGraLAPIEQAiggw 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 296 --FIQiARAfpSADRVQQVLntevdiisAANAIEPEKI-----EGNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGII 368
Cdd:COG4618 296 kqFVS-ARQ--AYRRLNELL--------AAVPAEPERMplprpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVI 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 369 GSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENL-RYGKENathDELEVAAA 447
Cdd:COG4618 365 GPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGDAD---PEKVVAAA 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 448 SAC-ATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKT-KYKGTTTL 525
Cdd:COG4618 442 KLAgVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVV 521
|
330 340 350
....*....|....*....|....*....|....*
gi 1265247244 526 LIASKISSIMDADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG4618 522 VITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-562 |
3.80e-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: 175.60 E-value: 3.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKAL--LFSGSIEENLRYGKENATHDELEVAA-ASACATEF-INKLEESYQYnltqgatNLSGGQKQRVSIARALVRK 490
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRErVEEALELVgLEHLADRPPH-------ELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 491 PPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIAS-KISSIMD-ADKILVLDNGELVGNGTHEQLLERSE 562
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVThDLDLVAElADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
66-564 |
1.82e-50 |
|
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: 188.23 E-value: 1.82e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 66 AALGLVGGLGCMMYSTKAAVN--FATD-IRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVrGPL 142
Cdd:TIGR00957 1012 GALGILQGFAVFGYSMAVSIGgiQASRvLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM-GSL 1090
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 143 LFMGSIIIVFVTARELFPILLVVVPILLLAIILIASKASGTFKKVQE-ALDKVNTKLQENLSGVRVIKAYVRQK-YEIAQ 220
Cdd:TIGR00957 1091 FNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESvSRSPVYSHFNETLLGVSVIRAFEEQErFIHQS 1170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 221 FGSVNTNLTKI--NIRAVQLISLMMPII--MLVVSGGIVATlwIGGEKVFNGT--LRVGAILAFINYLN--IILMSLMSI 292
Cdd:TIGR00957 1171 DLKVDENQKAYypSIVANRWLAVRLECVgnCIVLFAALFAV--ISRHSLSAGLvgLSVSYSLQVTFYLNwlVRMSSEMET 1248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 293 SMVfiqiarafpSADRVQQVLNTEVD---IISAANAIEPEKIEGNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIG 369
Cdd:TIGR00957 1249 NIV---------AVERLKEYSETEKEapwQIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVG 1319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 370 STGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENL----RYGKEnathdELEVA 445
Cdd:TIGR00957 1320 RTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDE-----EVWWA 1394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 446 AASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTL 525
Cdd:TIGR00957 1395 LELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVL 1474
|
490 500 510
....*....|....*....|....*....|....*....
gi 1265247244 526 LIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVY 564
Cdd:TIGR00957 1475 TIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-548 |
2.62e-49 |
|
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: 168.55 E-value: 2.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLrygkenathdelevaaasacatefinkleesyqynltqgatnLSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALK-TKYKGTTTLLIASKISSIMDADKILVLDNGEL 548
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAaLKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
202-558 |
1.71e-48 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 182.25 E-value: 1.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 202 LSGVRVIKAYVRqkyeiaqFGSVNTNLTKINIR--AVQLISLMMPIIMLVVSGGIVatLWIGGEKVFNGTLRVGAILAFI 279
Cdd:PLN03130 1102 LSTIRAYKAYDR-------MAEINGRSMDNNIRftLVNMSSNRWLAIRLETLGGLM--IWLTASFAVMQNGRAENQAAFA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 280 NYLNIILMSLMSI----SMVFIQIARAFPSADRVQQVlNTEVDIISAAnaiePEKIEGN-----------IEFKNVSYSY 344
Cdd:PLN03130 1173 STMGLLLSYALNItsllTAVLRLASLAENSLNAVERV-GTYIDLPSEA----PLVIENNrpppgwpssgsIKFEDVVLRY 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 345 TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSG 424
Cdd:PLN03130 1248 RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG 1327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 SIEENLRYGKENATHDELEvAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVD 504
Cdd:PLN03130 1328 TVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 505 AKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLL 558
Cdd:PLN03130 1407 VRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
202-560 |
1.65e-47 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 179.40 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 202 LSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIR-----AVQLISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLrvGAIL 276
Cdd:PLN03232 1099 LSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSsnrwlTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTM--GLLL 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 277 AFInyLNIILMslmsISMVFIQIARAFPSADRVQQVlNTEVDIISAANAIEPEK-------IEGNIEFKNVSYSYTKNNE 349
Cdd:PLN03232 1177 SYT--LNITTL----LSGVLRQASKAENSLNSVERV-GNYIDLPSEATAIIENNrpvsgwpSRGSIKFEDVHLRYRPGLP 1249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 350 YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEEN 429
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFN 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 430 LRYGKENATHDELEvAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEA 509
Cdd:PLN03232 1330 IDPFSEHNDADLWE-ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 510 TIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLER 560
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
336-547 |
1.04e-46 |
|
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: 163.02 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 336 EFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFV 415
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 416 PQKA--LLFSGSIEENLRYGKENATHDELEV-AAASACATEF-INKLEESYQYnltqgatNLSGGQKQRVSIARALVRKP 491
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIeERVEEALELVgLEGLRDRSPF-------TLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLDNGE 547
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
355-557 |
3.43e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 171.57 E-value: 3.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 355 ISFSIQKGEKVGIIGSTGSGKSTLAKLL----PrlYdvdQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENL 430
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALlgflP--Y---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 431 RYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEAT 510
Cdd:PRK11174 444 LLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265247244 511 IQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQL 557
Cdd:PRK11174 524 VMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
19-309 |
4.07e-46 |
|
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: 164.12 E-value: 4.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDvGIANRDLNY--VIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVF 96
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAID-ALTAGTLTAsqLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 97 AKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILI 176
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 177 ASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVA 256
Cdd:cd18541 161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 257 TLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18541 241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
331-558 |
1.70e-45 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 173.29 E-value: 1.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 331 IEGNIEFKNVSYSY-TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDV--------------------- 388
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 389 ---------------------------------DQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENLRYGKE 435
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 436 NATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQ-TA 514
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEkTI 1401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1265247244 515 LKTKYKGTTTLL-IASKISSIMDADKILVLDNGELVGN-----GTHEQLL 558
Cdd:PTZ00265 1402 VDIKDKADKTIItIAHRIASIKRSDKIVVFNNPDRTGSfvqahGTHEELL 1451
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
335-548 |
3.13e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 3.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENL----RYGKENATHDELEVAAASACatefinkLEESYqynLTQGATNLSGGQKQRVSIARALVRK 490
Cdd:COG4619 79 VPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDI---LDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 491 PPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLI------ASKIssimdADKILVLDNGEL 548
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVshdpeqIERV-----ADRVLTLEAGRL 209
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
335-569 |
1.04e-43 |
|
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: 156.82 E-value: 1.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD-LQKLRASIG 413
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FV---P--QkallFSGSI-EENLRYGKENA--THDELEVAAASACA----TEFINKleESYqynltqgatNLSGGQKQRV 481
Cdd:TIGR04520 81 MVfqnPdnQ----FVGATvEDDVAFGLENLgvPREEMRKRVDEALKlvgmEDFRDR--EPH---------LLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 482 SIARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLE 559
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
250
....*....|
gi 1265247244 560 RSEVYQEIYL 569
Cdd:TIGR04520 226 QVELLKEIGL 235
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
14-309 |
1.21e-43 |
|
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: 157.24 E-value: 1.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 14 YMFFAIigpLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRK 93
Cdd:cd18545 1 KLLLAL---LLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 94 DVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAI 173
Cdd:cd18545 78 DLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 174 ILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGG 253
Cdd:cd18545 158 FLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 254 IVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18545 238 TALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-557 |
1.52e-43 |
|
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: 155.03 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDV-----DQGEICIDGIDVKT--YDLQK 407
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQKALLFSGSIEENLRYG------KENATHDELEVAAASACA--TEFINKLeesyqynltqGATNLSGGQKQ 479
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAAlwDEVKDRL----------HALGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 480 RVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKtKYKGTTTLLIAS----KISSImdADKILVLDNGELVGNGTHE 555
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIA-ELKKEYTIVIVThnmqQAARV--ADRTAFLLNGRLVEFGPTE 225
|
..
gi 1265247244 556 QL 557
Cdd:cd03260 226 QI 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
352-501 |
6.33e-43 |
|
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: 6.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSG-SIEENL 430
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 431 RYGkenATHDELEVAAASACATEFINKLEESYQYN--LTQGATNLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
19-309 |
1.65e-42 |
|
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: 154.47 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANR--DLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVF 96
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDDYIVPGqgDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 97 AKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILI 176
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 177 ASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVA 256
Cdd:cd18544 162 RKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 257 TLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18544 242 VLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
15-309 |
5.40e-42 |
|
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: 152.96 E-value: 5.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 15 MFFAIIgplFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKD 94
Cdd:cd18552 1 LALAIL---GMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 95 VFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAII 174
Cdd:cd18552 78 LFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 175 LIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGI 254
Cdd:cd18552 158 RIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 255 VATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18552 238 ALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-568 |
7.83e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.60 E-value: 7.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNneYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGF 414
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYGKE--NATHDELEVAAASACA----TEFINKLeesyqynltqgATNLSGGQKQRVSIARAL 487
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLElfglTDAADRK-----------VGTLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD--ADKILVLDNGELVGNGTHEQLLERS--EV 563
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAErlCDRVAIIDKGRIVADGTPDELKARLleDV 226
|
....*
gi 1265247244 564 YQEIY 568
Cdd:COG1131 227 FLELT 231
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
335-549 |
8.56e-42 |
|
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: 150.35 E-value: 8.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYV--LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLR 409
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 ASIGFVPQKAL-----LFS--GSIEENLR-YGKENATHDELEVAAASAC----ATEFINKLeeSYQynltqgatnLSGGQ 477
Cdd:cd03257 82 KEIQMVFQDPMsslnpRMTigEQIAEPLRiHGKLSKKEARKEAVLLLLVgvglPEEVLNRY--PHE---------LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 478 KQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLI------ASKIssimdADKILVLDNGELV 549
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFIthdlgvVAKI-----ADRVAVMYAGKIV 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
335-547 |
1.27e-41 |
|
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: 149.16 E-value: 1.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNE---YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklraS 411
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSGSIEENLRYGKEnatHDELEVAAA-SACA-TEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVR 489
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP---FDEERYEKViKACAlEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 490 KPPILILDDSTSAVDAKSEATI-----QTALKtkyKGTTTLLIASKISSIMDADKILVLDNGE 547
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIfenciLGLLL---NNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
333-558 |
1.88e-41 |
|
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: 150.44 E-value: 1.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASI 412
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSGSIEENLRYGKEnATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLL 558
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-552 |
6.18e-41 |
|
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: 146.30 E-value: 6.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQkLRASIGF 414
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLrygkenathdelevaaasacatefinkleesyqynltqgATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNG 552
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-560 |
2.95e-40 |
|
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: 153.52 E-value: 2.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD---QGEICIDGIDVKTYDLQKLRAS 411
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKAL--LFSGSIEENLRYGKEN--ATHDELEVAAASACATEFINKLEESYQYnltqgatNLSGGQKQRVSIARAL 487
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALENlgLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-548 |
2.96e-40 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 145.71 E-value: 2.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNE--YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKL---- 408
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 RASIGFVPQK-ALLFSGSIEENLRYGKENATHDELEvaaASACATEFINK--LEESyqynLTQGATNLSGGQKQRVSIAR 485
Cdd:cd03255 81 RRHIGFVFQSfNLLPDLTALENVELPLLLAGVPKKE---RRERAEELLERvgLGDR----LNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 486 ALVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMDADKILVLDNGEL 548
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
335-560 |
6.49e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 145.77 E-value: 6.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLqKLRASIGF 414
Cdd:COG4555 2 IEVENLSKKYGKVP--ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYgkENATHDeLEVAAASACATEFINKLE-ESYqynLTQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:COG4555 79 LPDERGLYDRlTVRENIRY--FAELYG-LFDEELKKRIEELIELLGlEEF---LDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDA--DKILVLDNGELVGNGTHEQLLER 560
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlcDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
335-562 |
1.10e-39 |
|
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: 144.65 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVS--YSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTY---DLQKLR 409
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 ASIGFVPQK-ALLFSGSIEENLRYgkenathdELEVAAAS-ACATEFINKLEEsyQYNLTQGA----TNLSGGQKQRVSI 483
Cdd:cd03258 82 RRIGMIFQHfNLLSSRTVFENVAL--------PLEIAGVPkAEIEERVLELLE--LVGLEDKAdaypAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 484 ARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLER 560
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 1265247244 561 SE 562
Cdd:cd03258 232 PQ 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
335-560 |
1.68e-39 |
|
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: 151.21 E-value: 1.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYT---KNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTY---DLQKL 408
Cdd:COG1123 261 LEVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 RASIGFVPQ--KALLFSG-SIEENLRYGKENatHDELEVAAASACATEFinkLEesyQYNLTQGATN-----LSGGQKQR 480
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRmTVGDIIAEPLRL--HGLLSRAERRERVAEL---LE---RVGLPPDLADrypheLSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIA---SKISSImdADKILVLDNGELVGNGTHE 555
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLTYLFIShdlAVVRYI--ADRVAVMYDGRIVEDGPTE 490
|
....*
gi 1265247244 556 QLLER 560
Cdd:COG1123 491 EVFAN 495
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-309 |
4.37e-39 |
|
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: 144.99 E-value: 4.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 18 AIIGPLFMVLEVAMDLIQPTIMQHIID-VGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVF 96
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDlVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 97 AKIETFSSNNRDSFGTGKLLTIVTNDITSIQsamtmtlRVLVRG-------PLLFMGSIIIVFVTARELFPILLVVVPIL 169
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVE-------RLIADGipqgitnVLTLVGVAIILFSINPKLALLTLIPIPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 170 LLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLV 249
Cdd:cd18778 154 ALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 250 VSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18778 234 TSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
15-309 |
4.71e-39 |
|
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: 144.85 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 15 MFFAIIgplFMVLEVAMDLIQPTIMQHIID------VGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFA 88
Cdd:cd18547 1 LILVII---LAIISTLLSVLGPYLLGKAIDliieglGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 89 TDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPI 168
Cdd:cd18547 78 YDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 169 LLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIML 248
Cdd:cd18547 158 SLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNF 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 249 VVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18547 238 INNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
23-309 |
5.34e-39 |
|
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: 144.55 E-value: 5.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 23 LFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAKIET- 101
Cdd:cd18576 3 ILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 102 ---FSSNNRdsfgTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELfpillVVVPILLLAIILIAS 178
Cdd:cd18576 83 plsFFHERR----VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKL-----TLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 179 KASGTF-----KKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGG 253
Cdd:cd18576 154 VLFGRRirklsKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 254 IVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
198-547 |
6.28e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 153.65 E-value: 6.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 198 LQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATLWIGGEKVF--------NGT 269
Cdd:PTZ00265 239 IEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIIsdlsnqqpNND 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 270 LRVGAIlafINYLNIILMSLMSISMVFIQIA---RAFPSADRVQQVLNTEvDIISAANAIEPEKIEGNIEFKNVSYSY-T 345
Cdd:PTZ00265 319 FHGGSV---ISILLGVLISMFMLTIILPNITeymKSLEATNSLYEIINRK-PLVENNDDGKKLKDIKKIQFKNVRFHYdT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 346 KNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICI-DGIDVKTYDLQKLRASIGFVPQKALLFSG 424
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSN 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 SIEENLRYG-------------------------------------------------------KENATHDELEVAAAS- 448
Cdd:PTZ00265 475 SIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrKNYQTIKDSEVVDVSk 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 449 -ACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALkTKYKGT---TT 524
Cdd:PTZ00265 555 kVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI-NNLKGNenrIT 633
|
410 420
....*....|....*....|...
gi 1265247244 525 LLIASKISSIMDADKILVLDNGE 547
Cdd:PTZ00265 634 IIIAHRLSTIRYANTIFVLSNRE 656
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
335-569 |
7.44e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 143.59 E-value: 7.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKA-LLFSGS-IEENLRYGKENATHDELEVAA---ASACATEFINKLEESYQynltqgatNLSGGQKQRVSIARALVR 489
Cdd:PRK13632 88 IFQNPdNQFIGAtVEDDIAFGLENKKVPPKKMKDiidDLAKKVGMEDYLDKEPQ--------NLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 490 KPPILILDDSTSAVDAKSEATI-QTALKTKYKGTTTLL-IASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEI 567
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIkKIMVDLRKTRKKTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILEKA 239
|
..
gi 1265247244 568 YL 569
Cdd:PRK13632 240 KI 241
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-547 |
7.94e-39 |
|
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: 140.40 E-value: 7.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD--LQKLRASI 412
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSG-SIEENLRYGkenathdelevaaasacatefinkleesyqynltqgatnLSGGQKQRVSIARALVRKP 491
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGE 547
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
335-565 |
9.09e-39 |
|
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: 142.88 E-value: 9.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:COG1120 2 LEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALL-FSGSIEENLRYGK-------ENATHDELEVAAASACATEfINKLEESYqynltqgATNLSGGQKQRVSIARA 486
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfGRPSAEDREAVEEALERTG-LEHLADRP-------VDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLI------ASKIssimdADKILVLDNGELVGNGTHEQLL 558
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVlhdlnlAARY-----ADRLVLLKDGRIVAQGPPEEVL 226
|
250
....*....|
gi 1265247244 559 ER---SEVYQ 565
Cdd:COG1120 227 TPellEEVYG 236
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
336-552 |
2.53e-38 |
|
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: 140.36 E-value: 2.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 336 EFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktYDLQKLRASIGFV 415
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 416 PQKALL---FSGSIEENL---RYGKENATH-------DELEVAAASACATEFINKleesyqyNLTQgatnLSGGQKQRVS 482
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVlmgLYGHKGLFRrlskadkAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 483 IARALVRKPPILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLdNGELVGNG 552
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
335-569 |
2.61e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.46 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKA-LLFSGS-IEENLRYGKEN--ATHDEL----EVAAASACATEFinkleesyqynLTQGATNLSGGQKQRVSIARA 486
Cdd:PRK13635 86 VFQNPdNQFVGAtVQDDVAFGLENigVPREEMvervDQALRQVGMEDF-----------LNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEA----TIQTaLKTKyKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSE 562
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRRevleTVRQ-LKEQ-KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
....*..
gi 1265247244 563 VYQEIYL 569
Cdd:PRK13635 233 MLQEIGL 239
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-558 |
5.22e-38 |
|
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: 140.51 E-value: 5.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:cd03295 1 IEFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEEN-------LRYGKE--NATHDELeVAAASACATEFINKleesYQYnltqgatNLSGGQKQRVSIA 484
Cdd:cd03295 80 VIQQIGLFPHmTVEENialvpklLKWPKEkiRERADEL-LALVGLDPAEFADR----YPH-------ELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKI-SSIMDADKILVLDNGELVGNGTHEQLL 558
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
335-551 |
8.69e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 139.41 E-value: 8.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNE--YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLR 409
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 A-SIGFVPQKALLFSG-SIEEN----LRYGKENATHDELEVAAA------SACATEFINKLeesyqynltqgatnlSGGQ 477
Cdd:COG1136 85 RrHIGFVFQFFNLLPElTALENvalpLLLAGVSRKERRERARELlervglGDRLDHRPSQL---------------SGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 478 KQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLL------IASKissimdADKILVLDNGELV 549
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMvthdpeLAAR------ADRVIRLRDGRIV 223
|
..
gi 1265247244 550 GN 551
Cdd:COG1136 224 SD 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
336-547 |
1.10e-37 |
|
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: 136.61 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 336 EFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFV 415
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 416 PQkallfsgsieenlrygkenathdelevaaasacatefinkleesyqynltqgatnLSGGQKQRVSIARALVRKPPILI 495
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 496 LDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD--ADKILVLDNGE 547
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElaADRVIVLKDGK 157
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-568 |
1.56e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktYDLQKLRASIGF 414
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKAllfsgSIEENL-----------RYGKENA-----THDELEVAAA--SACATEFINKleesyQYNltqgatNLSGG 476
Cdd:COG1121 80 VPQRA-----EVDWDFpitvrdvvlmgRYGRRGLfrrpsRADREAVDEAleRVGLEDLADR-----PIG------ELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 477 QKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLdNGELVGNGTH 554
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLL-NRGLVAHGPP 222
|
250
....*....|....
gi 1265247244 555 EQLLeRSEVYQEIY 568
Cdd:COG1121 223 EEVL-TPENLSRAY 235
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
335-549 |
2.38e-37 |
|
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: 137.65 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIGF 414
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYnltqgATNLSGGQKQRVSIARALVRKPPI 493
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRY-----PHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 494 LILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKISSIMD-ADKILVLDNGELV 549
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIV 210
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-309 |
2.55e-37 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 140.34 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 18 AIIGPLFMVLEVAMDLIQPTIMQHIID----VGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRK 93
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 94 DVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAI 173
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 174 ILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGG 253
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 254 IVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
19-309 |
4.55e-37 |
|
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: 139.15 E-value: 4.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAK 98
Cdd:cd18543 2 ILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 99 IETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGpLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIAS 178
Cdd:cd18543 82 LQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNL-LTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 179 KASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATL 258
Cdd:cd18543 161 RYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 259 WIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18543 241 ALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
333-567 |
6.50e-37 |
|
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: 138.45 E-value: 6.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDqGEICIDGIDVKTYDLQKLRASI 412
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSGSIEENLR-YGKENatHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKP 491
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLL-ERSEVYQEI 567
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLnEKSHFKQAI 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
335-549 |
1.00e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.34 E-value: 1.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRAS 411
Cdd:COG2884 2 IRFENVSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQ--KaLLFSGSIEENLRYGkenathdeLEVAAASAcatEFINK-----LEesyQYNLTQGA----TNLSGGQKQR 480
Cdd:COG2884 81 IGVVFQdfR-LLPDRTVYENVALP--------LRVTGKSR---KEIRRrvrevLD---LVGLSDKAkalpHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDA--DKILVLDNGELV 549
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRmpKRVLELEDGRLV 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-557 |
1.03e-36 |
|
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: 136.48 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRAS 411
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYG-KENATHDELEVAAASACATEFINKLEESYQYnltqgATNLSGGQKQRVSIARALVR 489
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPlREHTRLSEEEIREIVLEKLEAVGLRGAEDLY-----PAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
335-559 |
2.19e-36 |
|
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: 135.88 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLRAS 411
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYG-KENATHDELEVAAASacatefINKLEESyqyNLTqGATN-----LSGGQKQRVSIA 484
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPlREHTDLSEAEIRELV------LEKLELV---GLP-GAADkmpseLSGGMRKRVALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQT---ALKTKYkGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLE 559
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDElirELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
336-552 |
7.81e-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: 132.17 E-value: 7.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 336 EFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFV 415
Cdd:cd03214 1 EVENLSVGYGGRT--VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 416 PQkALlfsgsieenlrygkenathDELEVAaasacatEFINKleesyqynltqGATNLSGGQKQRVSIARALVRKPPILI 495
Cdd:cd03214 79 PQ-AL-------------------ELLGLA-------HLADR-----------PFNELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 496 LDDSTSAVDAKSEATIQTALK--TKYKGTTTLLI------ASKIssimdADKILVLDNGELVGNG 552
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRrlARERGKTVVMVlhdlnlAARY-----ADRVILLKDGRIVAQG 180
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-562 |
1.22e-35 |
|
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: 134.16 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNE--YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASI 412
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALlfsGS----------IEENLRYGKENATHDELEVAAASAcatefinKLEESYqynLTQGATNLSGGQKQRVS 482
Cdd:COG1124 82 QMVFQDPY---ASlhprhtvdriLAEPLRIHGLPDREERIAELLEQV-------GLPPSF---LDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 483 IARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSI--MdADKILVLDNGELVGNGTHEQLL 558
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDlrEERGLTYLFVSHDLAVVahL-CDRVAVMQNGRIVEELTVADLL 227
|
....
gi 1265247244 559 ERSE 562
Cdd:COG1124 228 AGPK 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-553 |
1.89e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.98 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVS--YSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLR 409
Cdd:COG1135 2 IELENLSktFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 ASIGFVPQK-ALLFSGSIEENLRYGkenathdeLEVAAASAcatEFINK----------LEE-SYQYnltqgATNLSGGQ 477
Cdd:COG1135 82 RKIGMIFQHfNLLSSRTVAENVALP--------LEIAGVPK---AEIRKrvaellelvgLSDkADAY-----PSQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 478 KQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKT---KYkGTTTLLI---ASKISSImdADKILVLDNGELVGN 551
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDinrEL-GLTIVLItheMDVVRRI--CDRVAVLENGRIVEQ 222
|
..
gi 1265247244 552 GT 553
Cdd:COG1135 223 GP 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
335-548 |
2.25e-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: 130.98 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNneYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGF 414
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYgkenathdelevaaasacatefinkleesyqynltqgatnlSGGQKQRVSIARALVRKPPI 493
Cdd:cd03230 78 LPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 494 LILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIAskiSSIMD-----ADKILVLDNGEL 548
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLS---SHILEeaerlCDRVAILNNGRI 173
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
23-309 |
4.78e-35 |
|
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: 133.45 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 23 LFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAK---- 98
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 99 -IETFssnnrDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIA 177
Cdd:cd18557 83 eIAFF-----DKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 178 SKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVAT 257
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 258 LWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
112-567 |
1.11e-34 |
|
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: 140.43 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 112 TGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIAsKASGTFKKVQ-EA 190
Cdd:TIGR01271 981 AGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFL-RTSQQLKQLEsEA 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 191 LDKVNTKLQENLSGVRVIKAYVRQKY-EIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVAT-LWIGGEKVFNG 268
Cdd:TIGR01271 1060 RSPIFSHLITSLKGLWTIRAFGRQSYfETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTfIAIGTNQDGEG 1139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 269 tlRVGAILAF-INYL---------NIILMSLM-SISMVF--IQIARAFP-SADRVQQVLNTEVDIISAANAIEPEKIEGN 334
Cdd:TIGR01271 1140 --EVGIILTLaMNILstlqwavnsSIDVDGLMrSVSRVFkfIDLPQEEPrPSGGGGKYQLSTVLVIENPHAQKCWPSGGQ 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDqGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGV 1296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENL----RYGKENATHDELEVAAASACaTEFINKLEesyqYNLTQGATNLSGGQKQRVSIARALVRK 490
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLdpyeQWSDEEIWKVAEEVGLKSVI-EQFPDKLD----FVLVDGGYVLSNGHKQLMCLARSILSK 1371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 491 PPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLL-ERSEVYQEI 567
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLnETSLFKQAM 1449
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
335-560 |
1.30e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.88 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV--KTYDLQKLRASI 412
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSG-SIEENLRYG-----KENAthdelevAAASACATEFINK---LEESYQYnltqgATNLSGGQKQRVSI 483
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApikvkKMSK-------AEAEERAMELLERvglADKADAY-----PAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 484 ARALVRKPPILILDDSTSAVD--------------AKSeatiqtalktkykGTTTLLI------ASKIssimdADKILVL 543
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDpelvgevldvmrdlAKE-------------GMTMVVVthemgfAREV-----ADRVVFM 209
|
250
....*....|....*..
gi 1265247244 544 DNGELVGNGTHEQLLER 560
Cdd:COG1126 210 DGGRIVEEGPPEEFFEN 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-568 |
1.73e-34 |
|
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: 130.77 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRAS 411
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQK-ALLFSGSIEENLRYGKENATH---------DELEVAAASACaTEFINKLEESYQYnltqgATNLSGGQKQRV 481
Cdd:cd03256 80 IGMIFQQfNLIERLSVLENVLSGRLGRRStwrslfglfPKEEKQRALAA-LERVGLLDKAYQR-----ADQLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 482 SIARALVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLL 558
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELT 233
|
250
....*....|
gi 1265247244 559 ErsEVYQEIY 568
Cdd:cd03256 234 D--EVLDEIY 241
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
335-549 |
1.82e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.93 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYD-VDQ----GEICIDGIDV--KTYDLQK 407
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQKALLFSGSIEENLRYG------KENATHDEL------------EVAaasacatefiNKLEESyqynltqg 469
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslrkaalwdEVK----------DRLKKS-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 470 ATNLSGGQKQRVSIARALVRKPPILILDDSTSAVD----AKSEATIQTaLKTKYkgttTLLI-------ASKISsimdaD 538
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELILE-LKKDY----TIVIvthnmqqAARVS-----D 221
|
250
....*....|.
gi 1265247244 539 KILVLDNGELV 549
Cdd:COG1117 222 YTAFFYLGELV 232
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-545 |
3.73e-34 |
|
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: 129.13 E-value: 3.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY--VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktYDLQKLRASI 412
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFS-GSIEENLRYGKENATHDELEVAAAsacATEFINKL-----EESY--QynltqgatnLSGGQKQRVSIA 484
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARER---AEELLELVglsgfENAYphQ---------LSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKIS-SIMDADKILVLDN 545
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSA 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
335-546 |
1.10e-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: 129.05 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSY-TKNNEY-VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtydlqKLRASI 412
Cdd:COG1116 8 LELRGVSKRFpTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLF---SgsIEENLRYGKENATHDELEVAAAsacATEFINKL-----EESYQYNLtqgatnlSGGQKQRVSIA 484
Cdd:COG1116 83 GVVFQEPALLpwlT--VLDNVALGLELRGVPKAERRER---ARELLELVglagfEDAYPHQL-------SGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTAL-----KTkykGTTTLLIASKIS-SIMDADKILVLDNG 546
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELlrlwqET---GKTVLFVTHDVDeAVFLADRVVVLSAR 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
335-568 |
2.49e-33 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 127.41 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRAS 411
Cdd:TIGR02315 2 LEVENLSKVYP-NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQK-ALLFSGSIEENLRYGKENAT----------HDELEVAAASAcaTEFINKLEESYQYnltqgATNLSGGQKQR 480
Cdd:TIGR02315 81 IGMIFQHyNLIERLTVLENVLHGRLGYKptwrsllgrfSEEDKERALSA--LERVGLADKAYQR-----ADQLSGGQQQR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLL------IASKIssimdADKILVLDNGELVGNG 552
Cdd:TIGR02315 154 VAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKriNKEDGITVIInlhqvdLAKKY-----ADRIVGLKAGEIVFDG 228
|
250
....*....|....*.
gi 1265247244 553 THEQLLErsEVYQEIY 568
Cdd:TIGR02315 229 APSELDD--EVLRHIY 242
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
335-568 |
3.06e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 127.48 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRAS 411
Cdd:COG3638 3 LELRNLSKRYPGGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQK----------------AL--------LFSgsieenlRYGKEnathdelEVAAASACATEFiNKLEESYQYnlt 467
Cdd:COG3638 82 IGMIFQQfnlvprlsvltnvlagRLgrtstwrsLLG-------LFPPE-------DRERALEALERV-GLADKAYQR--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 468 qgATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLL------IASKIssimdADK 539
Cdd:COG3638 144 --ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVnlhqvdLARRY-----ADR 216
|
250 260
....*....|....*....|....*....
gi 1265247244 540 ILVLDNGELVGNGTHEQLLErsEVYQEIY 568
Cdd:COG3638 217 IIGLRDGRVVFDGPPAELTD--AVLREIY 243
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
19-296 |
3.56e-33 |
|
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: 128.38 E-value: 3.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAK 98
Cdd:cd18546 2 ALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 99 IETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIAS 178
Cdd:cd18546 82 LQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 179 KASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATL 258
Cdd:cd18546 162 RSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVL 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 1265247244 259 WIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVF 296
Cdd:cd18546 242 LVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVF 279
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
348-560 |
7.87e-33 |
|
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: 125.91 E-value: 7.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 348 NEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIGFVPQKALLFSG-SI 426
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 427 EENLRYGKENATHDELEVAAASACATEFINkleesYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAK 506
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLG-----IDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 507 SEATIQTALKT--KYKGTTTLLIASKISSI-MDADKILVLDNGELVGNGTHEQLLER 560
Cdd:cd03299 164 TKEKLREELKKirKEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
335-548 |
1.22e-32 |
|
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: 124.56 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV--KTYDLQKLRASI 412
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSG-SIEENLRYGKENATHdeLEVAAASACATEFINK---LEESYQYnltqgATNLSGGQKQRVSIARALV 488
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITLAPIKVKG--MSKAEAEERALELLEKvglADKADAY-----PAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 489 RKPPILILDDSTSAVDAKseaTIQTALKT----KYKGTTTLLIASKISSIMD-ADKILVLDNGEL 548
Cdd:cd03262 152 MNPKVMLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
19-309 |
1.36e-32 |
|
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: 126.78 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANR-DLNYVIKMGLLMIGAAALGLVGG--LGcmmystKAAVNFATDIRKDV 95
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGsSGGLLALLVALFLLQAVLSALSSylLG------RTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 96 FAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIIL 175
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 176 IASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIV 255
Cdd:cd18551 156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 256 ATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18551 236 VVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
338-549 |
2.00e-32 |
|
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: 123.91 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 338 KNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKlraSIGFVPQ 417
Cdd:cd03226 3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRK---SIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 418 KA--LLFSGSIEENLRYGKENAtHDELEVAAAsACATEFINKLEEsyqynltQGATNLSGGQKQRVSIARALVRKPPILI 495
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKEL-DAGNEQAET-VLKDLDLYALKE-------RHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 496 LDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLDNGELV 549
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
335-569 |
6.04e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.48 E-value: 6.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKAL-LFSGSI-EENLRYGKEN--ATHDEL-EVAAASACATEFINKLEESYQynltqgatNLSGGQKQRVSIARALVR 489
Cdd:PRK13648 88 VFQNPDnQFVGSIvKYDVAFGLENhaVPYDEMhRRVSEALKQVDMLERADYEPN--------ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEI 567
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELTRI 239
|
..
gi 1265247244 568 YL 569
Cdd:PRK13648 240 GL 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
335-569 |
7.97e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.53 E-value: 7.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLY---DVDQGEICIDGIDVKTYDLQKLRAS 411
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKA--LLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEesYQYNLTQgatNLSGGQKQRVSIARALVR 489
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLD--YIDSEPA---NLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEI 567
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEI 240
|
..
gi 1265247244 568 YL 569
Cdd:PRK13640 241 GL 242
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
335-560 |
1.62e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 125.21 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVktydlQKLRAS--- 411
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPPEkrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYGkenathdeLEV-----AAASACATEF-----INKLEESYqynltqgATNLSGGQKQR 480
Cdd:COG3842 79 VGMVFQDYALFPHlTVAENVAFG--------LRMrgvpkAEIRARVAELlelvgLEGLADRY-------PHQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDAKSEATIQTALKtkykgttTLLIASKISSIM---D-------ADKILVLDNGELVG 550
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELR-------RLQRELGITFIYvthDqeealalADRIAVMNDGRIEQ 216
|
250
....*....|
gi 1265247244 551 NGTHEQLLER 560
Cdd:COG3842 217 VGTPEEIYER 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
335-558 |
3.59e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 122.40 E-value: 3.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD-LQKLRASIG 413
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQKA-LLFSG-SIEENLRYGKENATHDELEVAAASACATEFInKLEEsYQYnltQGATNLSGGQKQRVSIARALVRKP 491
Cdd:PRK13644 81 IVFQNPeTQFVGrTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-GLEK-YRH---RSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 492 PILILDDSTSAVDAKS-EATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
335-570 |
4.73e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 122.12 E-value: 4.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNE----YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVK-TYDLQKLR 409
Cdd:PRK13633 5 IKCKNVSYKYESNEEstekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 ASIGFVPQKA--LLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLE-ESYQYNLtqgatnLSGGQKQRVSIARA 486
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEyRRHAPHL------LSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVY 564
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKEVEMM 238
|
....*.
gi 1265247244 565 QEIYLS 570
Cdd:PRK13633 239 KKIGLD 244
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
19-289 |
6.27e-31 |
|
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: 121.60 E-value: 6.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNY--VIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVF 96
Cdd:pfam00664 2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 97 AKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILI 176
Cdd:pfam00664 82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 177 ASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVA 256
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 1265247244 257 TLWIGGEKVFNGTLRVGAILAFINYLNIILMSL 289
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
335-560 |
1.22e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVktydlQKLRAS--- 411
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKdrn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQK-ALLFSGSIEENLRYGKENATHDELEVAAASACATEF--INKLEESYqynltqgATNLSGGQKQRVSIARALV 488
Cdd:COG3839 77 IAMVFQSyALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELlgLEDLLDRK-------PKQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 489 RKPPILILDDSTSAVDAK------SE-ATIQTALKTkykgTT-----------TLliaskissimdADKILVLDNGELVG 550
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRLGT----TTiyvthdqveamTL-----------ADRIAVMNDGRIQQ 214
|
250
....*....|
gi 1265247244 551 NGTHEQLLER 560
Cdd:COG3839 215 VGTPEELYDR 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
335-559 |
1.24e-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: 119.08 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYdlQKLRAS 411
Cdd:cd03224 1 LEVENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglPPH--ERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYGKENATHDELEvaaasacatefiNKLEESYQY------NLTQGATNLSGGQKQRVSIA 484
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLLLGAYARRRAKRK------------ARLERVYELfprlkeRRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLI---ASKISSImdADKILVLDNGELVGNGTHEQLLE 559
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVeqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
23-309 |
1.24e-30 |
|
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: 121.05 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 23 LFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAKIETF 102
Cdd:cd18575 3 IALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 103 SSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIASKASG 182
Cdd:cd18575 83 SPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 183 TFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATLWIGG 262
Cdd:cd18575 163 LSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGA 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1265247244 263 EKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18575 243 HDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
351-569 |
2.24e-30 |
|
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: 118.93 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLqkLRASIGFVPQKALLFSG-SI 426
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglPPHRI--ARLGIGYVPEGRRIFPSlTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 427 EENLRYGkenathdelevAAASACATEFINKLEESYQY------NLTQGATNLSGGQKQRVSIARALVRKPPILILDdst 500
Cdd:COG0410 96 EENLLLG-----------AYARRDRAEVRADLERVYELfprlkeRRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 501 savdaksEAT----------IQTALKT-KYKGTTTLLI---ASKISSImdADKILVLDNGELVGNGTHEQLLERSEVyQE 566
Cdd:COG0410 162 -------EPSlglapliveeIFEIIRRlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPEV-RE 231
|
...
gi 1265247244 567 IYL 569
Cdd:COG0410 232 AYL 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-562 |
3.50e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 126.82 E-value: 3.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASI 412
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSGSIEENLRYGKEnATHDELEVAAASACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 493 ILIL-DDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSE 562
Cdd:PTZ00243 1466 GFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
335-569 |
3.98e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.45 E-value: 3.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNE-YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIG 413
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQKA-LLFSG-SIEENLRYGKENATHDELEVAAASACATEFINKLEESyqynlTQGATNLSGGQKQRVSIARALVRKP 491
Cdd:PRK13650 85 MVFQNPdNQFVGaTVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFK-----EREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 492 PILILDDSTSAVDAKSE-ATIQT--ALKTKYkGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIY 568
Cdd:PRK13650 160 KIIILDEATSMLDPEGRlELIKTikGIRDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQLG 238
|
.
gi 1265247244 569 L 569
Cdd:PRK13650 239 L 239
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
335-570 |
4.06e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY---VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV--KTYDLQKLR 409
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 ASIGFVPQ--KALLFSGSIEENLRYGKENATHDELEVaaaSACATEFINKLEESYQYNLTQGATNLSGGQKQRVSIARAL 487
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEEEI---ENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKT---KYKGTTTLliaskISSIMD-----ADKILVLDNGELVGNGTHEQLLE 559
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKElhkEYNMTIIL-----VSHSMEdvaklADRIIVMNKGKCELQGTPREVFK 234
|
250
....*....|.
gi 1265247244 560 RSEVYQEIYLS 570
Cdd:PRK13637 235 EVETLESIGLA 245
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
335-561 |
1.29e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.12 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVK--TYDLQKLRASI 412
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKALLFSG-SIEENLRYGKenathdeLEV-----AAASACATEFINKL---EESYQYnltqgATNLSGGQKQRVSI 483
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENVMFGP-------LRVrgaskEEAEKQARELLAKVglaERAHHY-----PSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 484 ARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLI-------ASKISSimdadKILVLDNGELVGNGTHEQ 556
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIvtheigfAEKVAS-----RLIFIDKGRIAEDGDPQV 222
|
....*
gi 1265247244 557 LLERS 561
Cdd:PRK09493 223 LIKNP 227
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-549 |
3.35e-29 |
|
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: 115.04 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIGF 414
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQK-ALLFSGSIEENLRYGKE--NATHDELEVAAASACATEFINKLeesyqynLTQGATNLSGGQKQRVSIARALVRKP 491
Cdd:cd03301 77 VFQNyALYPHMTVYDNIAFGLKlrKVPKDEIDERVREVAELLQIEHL-------LDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKISSIMD-ADKILVLDNGELV 549
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHDQVEAMTmADRIAVMNDGQIQ 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
335-553 |
3.48e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 115.29 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGF 414
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRY-----GKENATHDELEVAAASACA-TEFINKLeesyqynltqgATNLSGGQKQRVSIARAL 487
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLRVLGlTDKANKR-----------ARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLiaskISSIMD-----ADKILVLDNGELVGNGT 553
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIIL----TTHSMDeaealCDRIAIMSDGKLRCIGS 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-560 |
3.77e-29 |
|
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: 115.41 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIGF 414
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYGKENATHDELEVAAASACATEFInKLEESYQYNLTQgatnLSGGQKQRVSIARALVRKPPI 493
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLV-QLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 494 LILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLER 560
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
95-572 |
4.88e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 123.16 E-value: 4.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 95 VFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSaMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAII 174
Cdd:PLN03232 380 IFHKSLRLTHEARKNFASGKVTNMITTDANALQQ-IAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQT 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 175 LIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQK-YEIAQFGSVNTNLTKIniRAVQLISLM-------MPII 246
Cdd:PLN03232 459 LIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKsFESRIQGIRNEELSWF--RKAQLLSAFnsfilnsIPVV 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 247 MLVVSGGIVATLwiGGE----KVFNgTLRVGAILAFInyLNIiLMSLMSismvfiQIARAFPSADRVQQVLNTEVDIISA 322
Cdd:PLN03232 537 VTLVSFGVFVLL--GGDltpaRAFT-SLSLFAVLRSP--LNM-LPNLLS------QVVNANVSLQRIEELLLSEERILAQ 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 323 ANAIEPEKIEGNIEFKNVSYSyTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTL-AKLLPRLYDVDQGEICIdgidvk 401
Cdd:PLN03232 605 NPPLQPGAPAISIKNGYFSWD-SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLiSAMLGELSHAETSSVVI------ 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 402 tydlqklRASIGFVPQKALLFSGSIEENLRYGKENathdELEVAAASACATEFINKLEESYQYNLTQ---GATNLSGGQK 478
Cdd:PLN03232 678 -------RGSVAYVPQVSWIFNATVRENILFGSDF----ESERYWRAIDVTALQHDLDLLPGRDLTEigeRGVNISGGQK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 479 QRVSIARALVRKPPILILDDSTSAVDAK-SEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQL 557
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
490
....*....|....*
gi 1265247244 558 LERSEVYQEIYLSQG 572
Cdd:PLN03232 827 SKSGSLFKKLMENAG 841
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-548 |
5.57e-29 |
|
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: 114.43 E-value: 5.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLRAS 411
Cdd:cd03292 1 IEFINVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYnltqgATNLSGGQKQRVSIARALVRK 490
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRAL-----PAELSGGEQQRVAIARAIVNS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 491 PPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADK--ILVLDNGEL 548
Cdd:cd03292 155 PTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
352-559 |
1.19e-28 |
|
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: 115.05 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTY---DLQKLRA-SIGFVPQK-ALLFSGSI 426
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRkKISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 427 EENLRYGKENATHDELEVAAASACATEFINKLEESYQYnltqgATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAK 506
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKY-----PDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 507 SEATIQT---ALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLE 559
Cdd:cd03294 195 IRREMQDellRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
335-560 |
1.92e-28 |
|
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: 115.92 E-value: 1.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYV--LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYD---VDQGEICIDGIDVKTYD---LQ 406
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRAS-IGFVPQKALlfsGS----------IEENLRYgkenatHDELEVAAASACATEFINKLE--------ESY--Qyn 465
Cdd:COG0444 82 KIRGReIQMIFQDPM---TSlnpvmtvgdqIAEPLRI------HGGLSKAEARERAIELLERVGlpdperrlDRYphE-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 466 ltqgatnLSGGQKQRVSIARALVRKPPILILDDSTSAVDakseATIQ-------TALKTKYkGTTTLLI------ASKIs 532
Cdd:COG0444 151 -------LSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQaqilnllKDLQREL-GLAILFIthdlgvVAEI- 217
|
250 260
....*....|....*....|....*...
gi 1265247244 533 simdADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG0444 218 ----ADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
15-309 |
2.25e-28 |
|
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: 114.89 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 15 MFFAIIgplfmVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKD 94
Cdd:cd18550 3 LVLLLI-----LLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 95 VFAKIE----TFSSNNRdsfgTGKLLTIVTNDITSIQSAMTMTLRVLVRgpllfmgSIIIVFVTARELFP-------ILL 163
Cdd:cd18550 78 LYAHLQrmslAFFTRTR----TGEIQSRLNNDVGGAQSVVTGTLTSVVS-------NVVTLVATLVAMLAldwrlalLSL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 164 VVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLS--GVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISL 241
Cdd:cd18550 147 VLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRW 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 242 MMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18550 227 FFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
335-553 |
2.41e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 116.05 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYV--LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLR 409
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 ASIGFVPQK-ALLFSGSIEENLRYgkenathdELEVAAASAcatEFINK-----LE--------ESYqynltqgATNLSG 475
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVAL--------PLELAGTPK---AEIKArvtelLElvglsdkaDRY-------PAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 476 GQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKissiMD-----ADKILVLDNGEL 548
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRELGLTIVLITHE----MDvvkriCDRVAVIDAGRL 219
|
....*
gi 1265247244 549 VGNGT 553
Cdd:PRK11153 220 VEQGT 224
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-309 |
4.79e-28 |
|
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: 114.15 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 19 IIGPLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVI---------KMGLLMIGAAALGLVGGLGCM------MYSTKA 83
Cdd:cd18564 2 ALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLglapllgpdPLALLLLAAAALVGIALLRGLasyagtYLTALV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 84 AVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQS-AMTMTLRVLVRGpLLFMGSIIIVFVTARELFPIL 162
Cdd:cd18564 82 GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDlLVSGVLPLLTNL-LTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 163 LVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLM 242
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 243 MPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
282-582 |
5.48e-28 |
|
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: 120.05 E-value: 5.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 282 LNIILMSLMSISMVFIQIARAFPSADRVQQVLNTEvdiisaanAIEPEKIE--------GN-IEFKNVSYSYTKNNEYVL 352
Cdd:TIGR00957 583 FNILRFPLNILPMVISSIVQASVSLKRLRIFLSHE--------ELEPDSIErrtikpgeGNsITVHNATFTWARDLPPTL 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 353 KDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklraSIGFVPQKALLFSGSIEENLRY 432
Cdd:TIGR00957 655 NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILF 721
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 433 GKenATHDELEVAAASACAT-EFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATI 511
Cdd:TIGR00957 722 GK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 512 QTAL---KTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEiYLSQGGNLHKEGGEE 582
Cdd:TIGR00957 800 FEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE-FLRTYAPDEQQGHLE 872
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
335-560 |
3.52e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.93 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTY-DLQKLRasIG 413
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRERR--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQKALLFSG-SIEENLRYGKENATHDElevAAASACATEFINK-----LEESYqynltqgATNLSGGQKQRVSIARAL 487
Cdd:COG1118 79 FVFQHYALFPHmTVAENIAFGLRVRPPSK---AEIRARVEELLELvqlegLADRY-------PSQLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALK---TKYKGtTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG1118 149 AVEPEVLLLDEPFGALDAKVRKELRRWLRrlhDELGG-TTVFVTHDQEEALElADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-552 |
4.01e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 108.41 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYS----YTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLP--RLYDVDQGEICIDGIDVktyDLQKL 408
Cdd:cd03213 4 LSFRNLTVTvkssPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 RASIGFVPQKALLFSG-SIEENLRYgkenathdelevaaaSAcatefinKLEesyqynltqgatNLSGGQKQRVSIARAL 487
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF---------------AA-------KLR------------GLSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKTKYK-GTTTLLIASKISSIM--DADKILVLDNGELVGNG 552
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
335-569 |
4.39e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.95 E-value: 4.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY-VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIG 413
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQKA--LLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESyqynlTQGATNLSGGQKQRVSIARALVRKP 491
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFK-----TREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTA---LKTKYKgTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLERSEVYQEIY 568
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRViheIKEKYQ-LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIG 238
|
.
gi 1265247244 569 L 569
Cdd:PRK13642 239 L 239
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
351-563 |
4.52e-27 |
|
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: 109.45 E-value: 4.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKL-RASIGFVPQKALLFSG-SIEE 428
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLRYGKENATHDELEVAAASACATEFINKLEESYQY-NLT----QGATNLSGGQKQRVSIARALVRKPPILILDDSTSAV 503
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAEELLERvGLAdladRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 504 -DAKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERSEV 563
Cdd:cd03219 175 nPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
335-571 |
5.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 5.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYV---LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG--IDVKTYD--LQK 407
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQ--KALLFSGSIEENLRYGKEN--ATHDElevaaASACATEFINKLEESYQYnLTQGATNLSGGQKQRVSI 483
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDE-----AKEKALKWLKKVGLSEDL-ISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 484 ARALVRKPPILILDDSTSAVDAKS-EATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERS 561
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
250
....*....|
gi 1265247244 562 EVYQEIYLSQ 571
Cdd:PRK13641 237 EWLKKHYLDE 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
335-565 |
6.35e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.86 E-value: 6.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK13548 3 LEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALL-FSGSIEENLRYG----KENATHDELEVAAASACA--TEFINKleeSYQynltqgatNLSGGQKQRVSIARAL 487
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGraphGLSRAEDDALVAAALAQVdlAHLAGR---DYP--------QLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 488 VR------KPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLI------ASkissiMDADKILVLDNGELVGNGT 553
Cdd:PRK13548 150 AQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARqlAHERGLAVIVVlhdlnlAA-----RYADRIVLLHQGRLVADGT 224
|
250
....*....|....*
gi 1265247244 554 HEQLLER---SEVYQ 565
Cdd:PRK13548 225 PAEVLTPetlRRVYG 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
335-545 |
1.13e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.56 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQkLRASIGF 414
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRY----GKENATHDELEVAAASACATEFINKLeesyqynltqgATNLSGGQKQRVSIARALVR 489
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLP-----------VRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDN 545
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGD 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
335-549 |
4.65e-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: 106.75 E-value: 4.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYV--LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLR 409
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 A-SIGFVPQK-ALLFSGSIEENLRYGKENATHDELEVAAASAcatefinkLEesyQYNLTQGATN----LSGGQKQRVSI 483
Cdd:COG4181 89 ArHVGFVFQSfQLLPTLTALENVMLPLELAGRRDARARARAL--------LE---RVGLGHRLDHypaqLSGGEQQRVAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 484 ARALVRKPPILILDDSTSAVDAKSEATIQTAL--KTKYKGTTTLLIASKISSIMDADKILVLDNGELV 549
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTHDPALAARCDRVLRLRAGRLV 225
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
335-564 |
7.82e-26 |
|
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: 106.27 E-value: 7.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKlrASIGF 414
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYG----KENATHDELEVAAASACATEFI--NKLEESYqynltqgATNLSGGQKQRVSIARAL 487
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVqlDWLADRY-------PAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKISSIMD-ADKILVLDNGELvgngthEQLLERSEVY 564
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRI------EQVGTPDEVY 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
339-569 |
9.06e-26 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 105.70 E-value: 9.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 339 NVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDL-QKLRASIGFVPQ 417
Cdd:cd03218 5 NLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 418 KALLFSG-SIEENLRYGKENATHDElevaaasacaTEFINKLEE-----SYQYNLTQGATNLSGGQKQRVSIARALVRKP 491
Cdd:cd03218 83 EASIFRKlTVEENILAVLEIRGLSK----------KEREEKLEElleefHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERSEVyQEIYL 569
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANELV-RKVYL 231
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
351-557 |
1.16e-25 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 105.30 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYdlQKLRASIGFVPQKALLFSG-SI 426
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItklPPH--ERARAGIAYVPQGREIFPRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 427 EENLRYGkenathdelevAAASACATEFInkLEESYQY------NLTQGATNLSGGQKQRVSIARALVRKPPILILDDST 500
Cdd:TIGR03410 93 EENLLTG-----------LAALPRRSRKI--PDEIYELfpvlkeMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 501 SAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRrlRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
335-565 |
1.26e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.74 E-value: 1.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKA--LLFSGSIEENLRYGKENA--THDELEVAAASACATEFINKLEESYQYnltqgatNLSGGQKQRVSIARALVRK 490
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGPVNMglDKDEVERRVEEALKAVRMWDFRDKPPY-------HLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 491 PPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKissIMD-----ADKILVLDNGELVGNGTHEQLLERSEVYQ 565
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATH---DVDlaaewADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
335-575 |
1.33e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.70 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG--IDVKTYDLQKLRASI 412
Cdd:PRK13639 2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKA--LLFSGSIEENLRYGKENATHDELEVAaasacatefiNKLEESYQYNLTQGATN-----LSGGQKQRVSIAR 485
Cdd:PRK13639 81 GIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVE----------KRVKEALKAVGMEGFENkpphhLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 486 ALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD--ADKILVLDNGELVGNGTHEqllersEV 563
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPvyADKVYVMSDGKIIKEGTPK------EV 224
|
250
....*....|..
gi 1265247244 564 YQEIYLSQGGNL 575
Cdd:PRK13639 225 FSDIETIRKANL 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
335-551 |
1.37e-25 |
|
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: 103.28 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQK-LRASIG 413
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQkallfsgsieenlrygkenathdelevaaasacatefinkleesyqynltqgatnLSGGQKQRVSIARALVRKPPI 493
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 494 LILDDSTSAVDAK-SEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGN 551
Cdd:cd03216 104 LILDEPTAALTPAeVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
335-570 |
1.37e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY---VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIdGIDV-----KTYDLQ 406
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRASIGFVPQ--KALLFSGSIEENLRYGKENATHDELEvaaASACATEFIN--KLEESYqynLTQGATNLSGGQKQRVS 482
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEED---AKQKAREMIElvGLPEEL---LARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 483 IARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLE 559
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
250
....*....|.
gi 1265247244 560 RSEVYQEIYLS 570
Cdd:PRK13634 236 DPDELEAIGLD 246
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
224-528 |
3.25e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.90 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 224 VNTNLTKINiRAVQLISLMMPIImlvvsggIVATlwiggeKVFNGTLRVGAilafinylniilmsLMSISMVFIQIARA- 302
Cdd:COG4178 264 RQRNLTFFT-TGYGQLAVIFPIL-------VAAP------RYFAGEITLGG--------------LMQAASAFGQVQGAl 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 303 ------FPS-------ADRV---QQVLNTEVDIISAANAIEPEKiEGNIEFKNVSYsYTKNNEYVLKDISFSIQKGEKVG 366
Cdd:COG4178 316 swfvdnYQSlaewratVDRLagfEEALEAADALPEAASRIETSE-DGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 367 IIGSTGSGKSTLAKLLPRLYDVDQGEICI-DGidvktydlqklrASIGFVPQKALLFSGSIEENLRYGKENATHDELEVA 445
Cdd:COG4178 394 ITGPSGSGKSTLLRAIAGLWPYGSGRIARpAG------------ARVLFLPQRPYLPLGTLREALLYPATAEAFSDAELR 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 446 AA--SACATEFINKLEESYQYNLTqgatnLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTT 523
Cdd:COG4178 462 EAleAVGLGHLAERLDEEADWDQV-----LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTT 536
|
....*
gi 1265247244 524 TLLIA 528
Cdd:COG4178 537 VISVG 541
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-552 |
1.35e-24 |
|
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: 101.89 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGeKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGF 414
Cdd:cd03264 1 LQLENLTKRY--GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYgkenathdeleVAAASACAT-----EFINKLEEsyqYNLTQGATN----LSGGQKQRVSIA 484
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDY-----------IAWLKGIPSkevkaRVDEVLEL---VNLGDRAKKkigsLSGGMRRRVGIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLL---IASKISSImdADKILVLDNGELVGNG 552
Cdd:cd03264 143 QALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILsthIVEDVESL--CNQVAVLNKGKLVFEG 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-561 |
1.48e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 105.19 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV----KTYDLQKLRASIGFVPQKALLFSG-SIEE 428
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLRYGKENATHDELEVAAASACATEFINKLeesyqynLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSE 508
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFERVIELLGIGHL-------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 509 ATIQTALK--TKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERS 561
Cdd:TIGR02142 168 YEILPYLErlHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
341-552 |
1.81e-24 |
|
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: 101.68 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 341 SYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGFVPQKAL 420
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 421 LFSG-SIEENLRY-----G-KENATHDELEVAAASACATEFINKLEESyqynltqgatnLSGGQKQRVSIARALVRKPPI 493
Cdd:cd03266 89 LYDRlTARENLEYfaglyGlKGDELTARLEELADRLGMEELLDRRVGG-----------FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 494 LILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMDA--DKILVLDNGELVGNG 552
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlcDRVVVLHRGRVVYEG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
351-548 |
2.17e-24 |
|
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: 100.20 E-value: 2.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQK-LRASIGFVP---QKALLFSG-S 425
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPedrKREGLVLDlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 IEENLrygkenathdelevaaasacateFINKLeesyqynltqgatnLSGGQKQRVSIARALVRKPPILILDDSTSAVDA 505
Cdd:cd03215 95 VAENI-----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265247244 506 KSEATI-QTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGEL 548
Cdd:cd03215 138 GAKAEIyRLIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
95-567 |
2.59e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 108.29 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 95 VFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQ-------SAMTMTLRVLVRGPLLF--------MGSIIIVFVTARELF 159
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQqicqqlhTLWSAPFRIIIAMVLLYqqlgvaslIGSLMLVLMFPIQTF 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 160 PIllvvvpilllaiiliaskaSGTFKKVQEALDKVNTK---LQENLSGVRVIKAYVRQKYEIAQFGSV-NTNLTKIniRA 235
Cdd:PLN03130 460 II-------------------SKMQKLTKEGLQRTDKRiglMNEVLAAMDTVKCYAWENSFQSKVQTVrDDELSWF--RK 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 236 VQLISLM-------MPIIMLVVSGGIVATLwiGGE----KVFNgTLRVGAILAFinylniilmSLMSISMVFIQIARAFP 304
Cdd:PLN03130 519 AQLLSAFnsfilnsIPVLVTVVSFGVFTLL--GGDltpaRAFT-SLSLFAVLRF---------PLFMLPNLITQAVNANV 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 305 SADRVQQVLNTEVDIISAANAIEPEkiEGNIEFKNVSYSY-TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTL-AKLL 382
Cdd:PLN03130 587 SLKRLEELLLAEERVLLPNPPLEPG--LPAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLiSAML 664
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 383 PRLYDVDQGEICIdgidvktydlqklRASIGFVPQKALLFSGSIEENLRYGKE-NATHDELEVAaasacATEFINKLEES 461
Cdd:PLN03130 665 GELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNILFGSPfDPERYERAID-----VTALQHDLDLL 726
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 462 YQYNLT---QGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAK-SEATIQTALKTKYKGTTTLLIASKISSIMDA 537
Cdd:PLN03130 727 PGGDLTeigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV 806
|
490 500 510
....*....|....*....|....*....|
gi 1265247244 538 DKILVLDNGELVGNGTHEQLLERSEVYQEI 567
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
30-303 |
2.74e-24 |
|
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: 103.30 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 30 AMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGL-----VGGLGCMMystkaAVNFATDIRKDVFAKIETFSS 104
Cdd:cd18549 16 ALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTllnyfVTYWGHVM-----GARIETDMRRDLFEHLQKLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 105 ----NNRdsfgTGKLLTIVTNDITSIQSamtmtlrVLVRGP-------LLFMGSIIIVFVTARELFPILLVVVPILLLAI 173
Cdd:cd18549 91 sffdNNK----TGQLMSRITNDLFDISE-------LAHHGPedlfisiITIIGSFIILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 174 ILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGG 253
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1265247244 254 IVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAF 303
Cdd:cd18549 240 NLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGM 289
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
351-557 |
3.76e-24 |
|
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: 102.63 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEIcidgidvktydlqKLRASIGFVPQKALLFSGSIEENL 430
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------------KHSGRISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 431 RYGkenATHDELEV-AAASACA-TEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSE 508
Cdd:cd03291 119 IFG---VSYDEYRYkSVVKACQlEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265247244 509 ATIQTALKTKYKGTTT-LLIASKISSIMDADKILVLDNGELVGNGTHEQL 557
Cdd:cd03291 196 KEIFESCVCKLMANKTrILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
334-561 |
4.81e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.98 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 334 NIEFKNVSYSYtknNEYVLKdISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIG 413
Cdd:COG3840 1 MLRLDDLTYRY---GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FvpQKALLFSG-SIEEN--------LRYGKENatHDELEVAAASACATEFINKLEESyqynltqgatnLSGGQKQRVSIA 484
Cdd:COG3840 77 F--QENNLFPHlTVAQNiglglrpgLKLTAEQ--RAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 485 RALVRKPPILILDDSTSAVDAkseatiqtALK----------TKYKGTTTLLI------ASKIssimdADKILVLDNGEL 548
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDP--------ALRqemldlvdelCRERGLTVLMVthdpedAARI-----ADRVLLVADGRI 208
|
250
....*....|...
gi 1265247244 549 VGNGTHEQLLERS 561
Cdd:COG3840 209 AADGPTAALLDGE 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
335-567 |
5.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.12 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYV---LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQK---- 407
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQ--KALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQynltQGATNLSGGQKQRVSIAR 485
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWE----KSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 486 ALVRKPPILILDDSTSAVDAKSEATIQTALKTKYK-GTTTLLIASKISSIMD-ADKILVLDNGELVGNGTheqlleRSEV 563
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT------PSDV 231
|
....
gi 1265247244 564 YQEI 567
Cdd:PRK13643 232 FQEV 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
352-560 |
6.81e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.54 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDvDQGEICIDGIDVKTYD---LQKLRASIGFVPQKALlfsGS--- 425
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPF---GSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 -------IEENLRYGKENATHDELEVAAASAcatefinkLEESyqyNLTQGATN-----LSGGQKQRVSIARALVRKPPI 493
Cdd:COG4172 378 rmtvgqiIAEGLRVHGPGLSAAERRARVAEA--------LEEV---GLDPAARHrypheFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 494 LILDDSTSAVDakseATIQT-------ALKTKYkGTTTLLIA---SKISSImdADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG4172 447 LVLDEPTSALD----VSVQAqildllrDLQREH-GLAYLFIShdlAVVRAL--AHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
351-566 |
1.14e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQK-LRASIGFVP----QKALLFSGS 425
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 IEENL------RYGKENATHDELEVAAasacATEFINKLEESYQyNLTQGATNLSGGQKQRVSIARALVRKPPILILDDS 499
Cdd:COG1129 347 IRENItlasldRLSRGGLLDRRRERAL----AEEYIKRLRIKTP-SPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 500 TSAVD--AKSE--ATIQTALKtkyKGTTTLLIASKISSIMD-ADKILVLDNGELVGNgtheqlLERSEVYQE 566
Cdd:COG1129 422 TRGIDvgAKAEiyRLIRELAA---EGKAVIVISSELPELLGlSDRILVMREGRIVGE------LDREEATEE 484
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-569 |
1.94e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY---VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV----KTYDLQK 407
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQ--KALLFSGSIEENLRYGKEN--ATHDELEVAAASACATEFINklEESYQYNltqgATNLSGGQKQRVSI 483
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS--ESLFEKN----PFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 484 ARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIaskISSIMD-----ADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL---VTHLMDdvanyADFVYVLEKGKLVLSGKPKDIF 233
|
250
....*....|.
gi 1265247244 559 ERSEVYQEIYL 569
Cdd:PRK13649 234 QDVDFLEEKQL 244
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
305-577 |
2.18e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.45 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 305 SADRVQQVLNTEVDIISAANAIEPekIEGN-----IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLA 379
Cdd:PRK13536 9 EAPRRLELSPIERKHQGISEAKAS--IPGSmstvaIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 380 KLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGFVPQ-KALLFSGSIEENL----RYGKENAThdelEVAAASACATEF 454
Cdd:PRK13536 85 RMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENLlvfgRYFGMSTR----EIEAVIPSLLEF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 455 InKLEESYQYNLTQgatnLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKY-KGTTTLLiaskISS 533
Cdd:PRK13536 160 A-RLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILL----TTH 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 534 IMD-----ADKILVLDNGELVGNGTHEQLLERS---EVYqEIYlsqGGNLHK 577
Cdd:PRK13536 231 FMEeaerlCDRLCVLEAGRKIAEGRPHALIDEHigcQVI-EIY---GGDPHE 278
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
351-549 |
3.12e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.38 E-value: 3.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRA-----------SIGFV-PQK 418
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiqmvfqdSISAVnPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 419 ALlfSGSIEENLRY----GKENATHDELEVAAASACATEFINKLEESyqynltqgatnLSGGQKQRVSIARALVRKPPIL 494
Cdd:PRK10419 107 TV--REIIREPLRHllslDKAERLARASEMLRAVDLDDSVLDKRPPQ-----------LSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELV 549
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-565 |
4.15e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:COG4559 2 LEAENLSVRLGGRT--LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALL-FSGSIEENLRYGKE----NATHDE---LEVAAASACATefinkLEE-SYQynltqgatNLSGGQKQRVSIAR 485
Cdd:COG4559 80 LPQHSSLaFPFTVEEVVALGRAphgsSAAQDRqivREALALVGLAH-----LAGrSYQ--------TLSGGEQQRVQLAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 486 ALV-------RKPPILILDDSTSAVD-AKSEATIQTALKTKYKGTTTLLI------ASkissiMDADKILVLDNGELVGN 551
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDlAHQHAVLRLARQLARRGGGVVAVlhdlnlAA-----QYADRILLLHQGRLVAQ 221
|
250
....*....|....*..
gi 1265247244 552 GTHEQLLER---SEVYQ 565
Cdd:COG4559 222 GTPEEVLTDellERVYG 238
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
335-557 |
4.27e-23 |
|
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: 97.83 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVkTYDLQKLRASIGF 414
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLR-----YGKENATHDE--LEVAAASACaTEFINKLEESYqynltqgatnlSGGQKQRVSIARA 486
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiharlYGVPGAERREriDELLDFVGL-LEAADRLVKTY-----------SGGMRRRLEIARS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLiaskISSIMD-----ADKILVLDNGELVGNGTHEQL 557
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILL----TTHYMEeaeqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
335-569 |
5.03e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 5.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK13652 4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKA--LLFSGSIEENLRYGKENATHDELEVAAASACATEFINkLEESyqynLTQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLG-LEEL----RDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 493 ILILDDSTSAVDAKSEATI---QTALKTKYkGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERSEVYQEIY 568
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELidfLNDLPETY-GMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLLARVH 236
|
.
gi 1265247244 569 L 569
Cdd:PRK13652 237 L 237
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
345-565 |
5.06e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.92 E-value: 5.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 345 TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV----------------KTYDLQKL 408
Cdd:PRK13631 35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpyskKIKNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 RASIGFVPQ--KALLFSGSIEENLRYGKENATHDELEvaaASACATEFINKLEESYQYnLTQGATNLSGGQKQRVSIARA 486
Cdd:PRK13631 115 RRRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSY-LERSPFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEA-TIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERSEVY 564
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
.
gi 1265247244 565 Q 565
Cdd:PRK13631 271 N 271
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
335-552 |
5.28e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 97.29 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVK--TYDLQKLRASI 412
Cdd:cd03268 1 LKTNDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQknIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 ---GFVPQKallfsgSIEENLR-----YGKENATHDE-LEVAAASACATEFINKleesyqynltqgatnLSGGQKQRVSI 483
Cdd:cd03268 79 eapGFYPNL------TARENLRllarlLGIRKKRIDEvLDVVGLKDSAKKKVKG---------------FSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 484 ARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD--ADKILVLDNGELVGNG 552
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQkvADRIGIINKGKLIEEG 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
339-558 |
5.75e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 339 NVSYSYTK-NNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGI------DVKTYDLQKLRAS 411
Cdd:PRK14246 12 NISRLYLYiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYG-KENATHDELEVAAASACATEFINKLEESYQyNLTQGATNLSGGQKQRVSIARALVR 489
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
335-569 |
6.36e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.15 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG--IDVKTYDLQKLRASI 412
Cdd:PRK13636 6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQKA--LLFSGSIEENLRYGKENATHDELEVAaasacaTEFINKLEESYQYNLTQGATN-LSGGQKQRVSIARALVR 489
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVR------KRVDNALKRTGIEHLKDKPTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALKTKYKGT-TTLLIASKISSIMD--ADKILVLDNGELVGNGTHEQLLERSEVYQE 566
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIATHDIDIVPlyCDNVFVMKEGRVILQGNPKEVFAEKEMLRK 238
|
...
gi 1265247244 567 IYL 569
Cdd:PRK13636 239 VNL 241
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
335-570 |
7.02e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 7.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD-----QGEICIDGIDV--KTYDLQK 407
Cdd:PRK14239 6 LQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQKALLFSGSIEENLRYG------KENATHDEL--EVAAASACATEFINKLEESyqynltqgATNLSGGQKQ 479
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAveKSLKGASIWDEVKDRLHDS--------ALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 480 RVSIARALVRKPPILILDDSTSAVDAKSEATIQT---ALKTKYkgtTTLLI------ASKISsimdaDKILVLDNGELVG 550
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEEtllGLKDDY---TMLLVtrsmqqASRIS-----DRTGFFLDGDLIE 227
|
250 260
....*....|....*....|.
gi 1265247244 551 -NGTHEQLLERSEVYQEIYLS 570
Cdd:PRK14239 228 yNDTKQMFMNPKHKETEDYIS 248
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
60-497 |
1.24e-22 |
|
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: 101.80 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 60 LLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAKI-----ETFssnnrDSFGTGKLLTIVTNDITSIQSAmtmtl 134
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRIlaaplERL-----ERIGAARLLAALTEDVRTISQA----- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 135 rvLVRGPLLFMGSIIIVFVTA------RELFPILLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVI 208
Cdd:COG4615 122 --FVRLPELLQSVALVLGCLAylawlsPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKEL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 209 K-------AYVRQKYE--IAQFGSVNTNLTKINIRAVQLISLMMpiimLVVSGGIVAtLWIGGEKVFNGTLrVGAILAFI 279
Cdd:COG4615 200 KlnrrrrrAFFDEDLQptAERYRDLRIRADTIFALANNWGNLLF----FALIGLILF-LLPALGWADPAVL-SGFVLVLL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 280 nYLniiLMSLMSISMVFIQIARAFPSADRVQQV---LNTEVDIISAANAIEPEKIEGNIEFKNVSYSYTKNNE---YVLK 353
Cdd:COG4615 274 -FL---RGPLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegFTLG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFsgsieENLrYG 433
Cdd:COG4615 350 PIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRL-LG 423
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 434 KENATHDELevaaasacATEFINKLEESYQYNLTQGA---TNLSGGQKQRVSIARALVRKPPILILD 497
Cdd:COG4615 424 LDGEADPAR--------ARELLERLELDHKVSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFD 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
337-557 |
1.75e-22 |
|
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: 102.68 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 337 FKNVSYSYTKnneyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEIcidgidvktydlqKLRASIGFVP 416
Cdd:TIGR01271 431 FSNFSLYVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------------KHSGRISFSP 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 417 QKALLFSGSIEENLRYGkenATHDELE-VAAASACA-TEFINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:TIGR01271 494 QTSWIMPGTIKDNIIFG---LSYDEYRyTSVIKACQlEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLY 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 495 ILDDSTSAVDAKSEATI-QTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQL 557
Cdd:TIGR01271 571 LLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
335-516 |
2.21e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.25 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIGF 414
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYG--KENATHDELEVAAASACATEfinKLEESYQYNLTQgatnLSGGQKQRVSIARALVRKP 491
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAFGlrMQKTPAAEITPRVMEALRMV---QLEEFAQRKPHQ----LSGGQQQRVAIARAVVNKP 163
|
170 180
....*....|....*....|....*
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALK 516
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELK 188
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
335-558 |
4.05e-22 |
|
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: 95.92 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPR-LYDVDQGEICIDGIDVKTYDLQKLRASIG 413
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FV-PQKALLFS--------------GSIEenlRYgkENATHDELEVAAASACATEFINKLEESYQynltqgatNLSGGQK 478
Cdd:COG1119 82 LVsPALQLRFPrdetvldvvlsgffDSIG---LY--REPTDEQRERARELLELLGLAHLADRPFG--------TLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 479 QRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMDA-DKILVLDNGELVGNGTHE 555
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
...
gi 1265247244 556 QLL 558
Cdd:COG1119 229 EVL 231
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
335-523 |
5.58e-22 |
|
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: 92.99 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYsYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklRASIGF 414
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLRYgkenATHDELevaaasacatefinkleesyqynltqgatnlSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03223 69 LPQRPYLPLGTLREQLIY----PWDDVL-------------------------------SGGEQQRLAFARLLLHKPKFV 113
|
170 180
....*....|....*....|....*....
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKTkyKGTT 523
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE--LGIT 140
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-552 |
6.65e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 94.28 E-value: 6.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIqKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGI----DVKTYDLQKLRASIGFVPQKALLFSG-SIEE 428
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLRYGKENATHDELEVAAASACATEFINKLEESYQYNLtqgatnlSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSE 508
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQL-------SGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1265247244 509 ATIQTALKTKYK--GTTTLLIASKISSI-MDADKILVLDNGELVGNG 552
Cdd:cd03297 168 LQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-527 |
7.73e-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: 94.42 E-value: 7.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICID----GIDVKTYD----LQKLRASIGFVPQ----- 417
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASpreiLALRRRTIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 418 ---KALLFsgsIEENLRygkenatHDELEVAAASACATEFINKLeesyqyNLTQG------ATnLSGGQKQRVSIARALV 488
Cdd:COG4778 106 prvSALDV---VAEPLL-------ERGVDREEARARARELLARL------NLPERlwdlppAT-FSGGEQQRVNIARGFI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1265247244 489 RKPPILILDDSTSAVDAKSEAT----IQTAlktKYKGTTTLLI 527
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVvvelIEEA---KARGTAIIGI 208
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
335-550 |
8.85e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.94 E-value: 8.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSY--TKnneyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD-LQKLRAS 411
Cdd:COG1129 5 LEMRGISKSFggVK----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYGKENATHDELEVAAASACATEFINKLEESYqyNLTQGATNLSGGQKQRVSIARALVRK 490
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLGREPRRGGLIDWRAMRRRARELLARLGLDI--DPDTPVGDLSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 491 PPILILDDSTSAVDAKsEA----TIQTALKTkyKGTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:COG1129 159 ARVLILDEPTASLTER-EVerlfRIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-536 |
9.71e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVdQGEICIDG--------IDVKTYDLQ 406
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRASIGFVPQKALLFSGSIEENLRYG-KENATHDELEVAAASACATEFINkLEESYQYNLTQGATNLSGGQKQRVSIAR 485
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvKIVGWRPKLEIDDIVESALKDAD-LWDEIKHKIHKSALDLSGGQQQRLCIAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 486 ALVRKPPILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIAS----KISSIMD 536
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlRLRSELTMVIVShnlhQVSRLSD 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
351-584 |
1.13e-21 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 94.72 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDlqklRASIG----FvpQKALLFS 423
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglPPHR----IARLGiartF--QNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 G-SIEENLRYGKENATHDEL------------EVAAASACATEFINKLE-ESYQYNLtqgATNLSGGQKQRVSIARALVR 489
Cdd:COG0411 93 ElTVLENVLVAAHARLGRGLlaallrlprarrEEREARERAEELLERVGlADRADEP---AGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 490 KPPILILDDSTSAVDAK-SEATIQT--ALKtKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERSEVyQ 565
Cdd:COG0411 170 EPKLLLLDEPAAGLNPEeTEELAELirRLR-DERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRADPRV-I 247
|
250
....*....|....*....
gi 1265247244 566 EIYLsqggnlhkeGGEEHA 584
Cdd:COG0411 248 EAYL---------GEEAAA 257
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-557 |
1.17e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.23 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY---VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV--KTYD--LQK 407
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthKTKDkyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQ--KALLFSGSIEENLRYGKENATHDELEVAAASacateFINKLEESYQYN-LTQGATNLSGGQKQRVSIA 484
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
335-551 |
1.25e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.03 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY--VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKL---- 408
Cdd:PRK10535 5 LELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 RASIGFVPQKALLFSG-SIEENLRYgkeNATHDELEVAAASACATEFINK--LEESYQYNLTQgatnLSGGQKQRVSIAR 485
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNVEV---PAVYAGLERKQRLLRAQELLQRlgLEDRVEYQPSQ----LSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 486 ALVRKPPILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMDADKILVLDNGELVGN 551
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
337-551 |
1.93e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 337 FKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklRASIGFVP 416
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 417 QKALLFSG-SIEENLRYGKENATHDELEVAAASAC----------ATEFINKLEESYQYNLTQGA--------------- 470
Cdd:COG0488 68 QEPPLDDDlTVLDTVLDGDAELRALEAELEELEAKlaepdedlerLAELQEEFEALGGWEAEARAeeilsglgfpeedld 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 471 ---TNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKtKYKGttTLLIaskIS---SIMD--ADKILV 542
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK-NYPG--TVLV---VShdrYFLDrvATRILE 221
|
250
....*....|..
gi 1265247244 543 LDNGELV---GN 551
Cdd:COG0488 222 LDRGKLTlypGN 233
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
335-552 |
2.04e-21 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 92.56 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyvlKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:cd03298 1 VRLDKIRFSYGEQP----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 vpQKALLFSG-SIEENLRYG-----KENATHDE-LEVAAASACATEFINKLEESyqynltqgatnLSGGQKQRVSIARAL 487
Cdd:cd03298 77 --QENNLFAHlTVEQNVGLGlspglKLTAEDRQaIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNG 552
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
12-309 |
2.70e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 94.47 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 12 KPYMFFAIIgplFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDI 91
Cdd:cd18540 1 KKLLILLII---LMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 92 RKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLL 171
Cdd:cd18540 78 RKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 172 AIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVS 251
Cdd:cd18540 158 VSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGS 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 252 GGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18540 238 IATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
354-504 |
4.37e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.41 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRASIGFV---PQKAL----LFS 423
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELRPLRRRMQMVfqdPYASLnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 GSIEENLRYgKENATHDELEVAAASACAT-----EFINKL--EesyqynltqgatnLSGGQKQRVSIARALVRKPPILIL 496
Cdd:COG4608 116 DIIAEPLRI-HGLASKAERRERVAELLELvglrpEHADRYphE-------------FSGGQRQRIGIARALALNPKLIVC 181
|
....*...
gi 1265247244 497 DDSTSAVD 504
Cdd:COG4608 182 DEPVSALD 189
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
354-575 |
4.77e-21 |
|
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: 94.78 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG---------IDVKTYdlqklRASIGFVPQKALLFSG 424
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargIFLPPH-----RRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 -SIEENLRYGKENATHDELEVAAASACATEFINKLeesyqynLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAV 503
Cdd:COG4148 92 lSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHL-------LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 504 DAKSEATI---------QTALKTKYkgtttlliaskISSIMD-----ADKILVLDNGELVGNGTHEQLLERSEVYQEIYL 569
Cdd:COG4148 165 DLARKAEIlpylerlrdELDIPILY-----------VSHSLDevarlADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGG 233
|
....*.
gi 1265247244 570 SQGGNL 575
Cdd:COG4148 234 EEAGSV 239
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
335-552 |
8.63e-21 |
|
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: 90.80 E-value: 8.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKlrasIGF 414
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYgkeNATHDELEVAAASACATEFINKLE-ESYQYnltQGATNLSGGQKQRVSIARALVRKPP 492
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVY---LAQLKGLKKEEARRRIDEWLERLElSEYAN---KRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNG 552
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
345-517 |
9.73e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.93 E-value: 9.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 345 TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDvDQGEICIDGIDVKTYDLQKL---RASIGFVPQKA-- 419
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPns 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 420 -----LLFSGSIEENLR--YGKENATHDELEVAAAsacATEFINKLEESYQYnltqgATNLSGGQKQRVSIARALVRKPP 492
Cdd:PRK15134 374 slnprLNVLQIIEEGLRvhQPTLSAAQREQQVIAV---MEEVGLDPETRHRY-----PAEFSGGQRQRIAIARALILKPS 445
|
170 180
....*....|....*....|....*
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKT 517
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKS 470
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
334-557 |
1.94e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 93.22 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 334 NIEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVktydlQKLRA--- 410
Cdd:PRK10851 2 SIEIANIKKSF--GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHArdr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 411 SIGFVPQKALLFSG-SIEENLRYG-KENATHDELEVAAASACATEFINKLEESYQYNltQGATNLSGGQKQRVSIARALV 488
Cdd:PRK10851 75 KVGFVFQHYALFRHmTVFDNIAFGlTVLPRRERPNAAAIKAKVTQLLEMVQLAHLAD--RYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 489 RKPPILILDDSTSAVDAKSEATIQTALK---TKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQL 557
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
351-560 |
2.39e-20 |
|
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: 94.75 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLA----KLLPRLYDVDQGEICIDGIDVKTYDLQKLRA----SIGFV---PQKA 419
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIfqePMTS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 420 L--LFSgsIE----ENLRygkenaTHDELEVAAASACATEFinkLEE-----------SY--QynltqgatnLSGGQKQR 480
Cdd:COG4172 105 LnpLHT--IGkqiaEVLR------LHRGLSGAAARARALEL---LERvgipdperrldAYphQ---------LSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDakseATIQT-------ALKTKYkGTTTLLI------ASKIssimdADKILVLDNGE 547
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALD----VTVQAqildllkDLQREL-GMALLLIthdlgvVRRF-----ADRVAVMRQGE 234
|
250
....*....|...
gi 1265247244 548 LVGNGTHEQLLER 560
Cdd:COG4172 235 IVEQGPTAELFAA 247
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
352-558 |
2.54e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.56 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKL----RASIGFVPQK-ALLFSGSI 426
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 427 EENLRYGKenathdELEVAAASACATEFINKLEESYQYNLTQGATN-LSGGQKQRVSIARALVRKPPILILDDSTSAVDA 505
Cdd:PRK10070 124 LDNTAFGM------ELAGINAEERREKALDALRQVGLENYAHSYPDeLSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 506 KSEATIQ---TALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK10070 198 LIRTEMQdelVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-504 |
2.87e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.77 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSytKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK10247 8 LQLQNVGYL--AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLRYGKEnATHDELEVAAASACATEFinKLEESYqynLTQGATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPWQ-IRNQQPDPAIFLDDLERF--ALPDTI---LTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170
....*....|
gi 1265247244 495 ILDDSTSAVD 504
Cdd:PRK10247 160 LLDEITSALD 169
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
335-558 |
3.37e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 89.64 E-value: 3.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtknnEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK10771 2 LKLTDITWLY----HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 vpQKALLFSG-SIEENLRYG-----KENAT-HDELEVAAASACATEFINKLeesyqynltqgATNLSGGQKQRVSIARAL 487
Cdd:PRK10771 78 --QENNLFSHlTVAQNIGLGlnpglKLNAAqREKLHAIARQMGIEDLLARL-----------PGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKTK-YKGTTTLLIASKisSIMDADKI----LVLDNGELVGNGTHEQLL 558
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSH--SLEDAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-547 |
3.67e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.12 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNneYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklRASIGF 414
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQkallfsgsieenlrygkenathdelevaaasacatefinkleesyqynltqgatnLSGGQKQRVSIARALVRKPPIL 494
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 495 ILDDSTSAVDAKSEATIQTALKtKYKGttTLLIASK----ISSImdADKILVLDNGE 547
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALK-EYPG--TVILVSHdryfLDQV--ATKIIELEDGK 144
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
335-571 |
3.81e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 90.19 E-value: 3.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD--------LQ 406
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRASIGFVPQKALLFSGsieenlRYGKENATHDELEV-----AAASACATEFINKL-----EESYqynltqgATNLSGG 476
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPH------RTVLENIIEGPVIVkgepkEEATARARELLAKVglagkETSY-------PRRLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 477 QKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIAS-KISSIMD-ADKILVLDNGELVGNGTH 554
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVThEMSFARDvADRAIFMDQGRIVEQGPA 228
|
250 260
....*....|....*....|..
gi 1265247244 555 EQLL-----ERSEVYQEIYLSQ 571
Cdd:PRK11264 229 KALFadpqqPRTRQFLEKFLLQ 250
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
23-309 |
4.27e-20 |
|
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: 90.68 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 23 LFMVLEVAMDLIQPTIMQHIIDVGIANRD----LNYVIKMGLLmigAAALGLVGGL--GCMMYstkAAVNFATDIRKDVF 96
Cdd:cd18572 3 VFLVVAALSELAIPHYTGAVIDAVVADGSreafYRAVLLLLLL---SVLSGLFSGLrgGCFSY---AGTRLVRRLRRDLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 97 A-----KIETFssnnrDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELfpillVVVPILLL 171
Cdd:cd18572 77 RsllrqDIAFF-----DATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRL-----TLLAFITV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 172 AIILIASKASGTF-----KKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPII 246
Cdd:cd18572 147 PVIALITKVYGRYyrklsKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVN 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 247 MLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18572 227 TLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-549 |
7.76e-20 |
|
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: 7.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIdGIDVKtydlqklrasIGF 414
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG--SIEENLRYGKENAThdELEVAAASACateFINKLEESYQYnltqgATNLSGGQKQRVSIARALVRKPP 492
Cdd:COG0488 383 FDQHQEELDPdkTVLDELRDGAPGGT--EQEVRGYLGR---FLFSGDDAFKP-----VGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKTkYKGttTLLIASK----ISSImdADKILVLDNGELV 549
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDD-FPG--TVLLVSHdryfLDRV--ATRILEFEDGGVR 508
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
335-557 |
9.22e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 9.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLK---DISFSIQKGEKVGIIGSTGSGKSTL-----AKLLPRLYDV-------------DQGEI 393
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFiehlnALLLPDTGTIewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 394 CIDGIDVKTYDLQK------LRASIGFVPQKA--LLFSGSIEENLRYGKENATHDELEvaaASACATEFIN--KLEESYq 463
Cdd:PRK13651 83 VLEKLVIQKTRFKKikkikeIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSMGVSKEE---AKKRAAKYIElvGLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 464 ynLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYK-GTTTLLIASKISSIMD-ADKIL 541
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVLEwTKRTI 236
|
250
....*....|....*..
gi 1265247244 542 VLDNGELVGNG-THEQL 557
Cdd:PRK13651 237 FFKDGKIIKDGdTYDIL 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
334-555 |
1.06e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.53 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 334 NIEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG------IDVKTYDLQK 407
Cdd:COG4161 2 SIQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQKALLFSG-SIEENLrygkenaTHDELEV-----AAASACATEFINKLEesyqynLTQGAT----NLSGGQ 477
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHlTVMENL-------IEAPCKVlglskEQAREKAMKLLARLR------LTDKADrfplHLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 478 KQRVSIARALVRKPPILILDDSTSAVDakSEATIQTA---LKTKYKGTTTLLI------ASKISSimdadKILVLDNGEL 548
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALD--PEITAQVVeiiRELSQTGITQVIVthevefARKVAS-----QVVYMEKGRI 219
|
....*..
gi 1265247244 549 VGNGTHE 555
Cdd:COG4161 220 IEQGDAS 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
335-578 |
1.59e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 88.74 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYT-------KNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQK 407
Cdd:COG4167 5 LEVRNLSKTFKyrtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQKAllfSGSIEENLRYG-------KENATHDELEVAaasacatEFINK-------LEESYQYNLTQgatnL 473
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEERE-------ERIFAtlrlvglLPEHANFYPHM----L 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 474 SGGQKQRVSIARALVRKPPILILDDSTSAVDA--KSEAT-----IQTALKTKYKGTTTLL-IASKISsimdaDKILVLDN 545
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMsvRSQIInlmleLQEKLGISYIYVSQHLgIVKHIS-----DKVLVMHQ 225
|
250 260 270
....*....|....*....|....*....|....*
gi 1265247244 546 GELVGNGTHEQLLE--RSEVYQEIYLSQGGNLHKE 578
Cdd:COG4167 226 GEVVEYGKTAEVFAnpQHEVTKRLIESHFGEALTA 260
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-309 |
1.62e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 89.55 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 18 AIIGPLFMVLEVAMDLIQPTIMQHIIDV----------------GIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYST 81
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAvfngeasflplvpaslGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 82 kAAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPI 161
Cdd:cd18565 81 -FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 162 LLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISL 241
Cdd:cd18565 160 ALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 242 MMPIIMLVVSGGIVATLWIGGEKVFNG------TLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18565 240 FFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
347-509 |
1.74e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 347 NNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvKTYDLQKLRASIGFV-PQKALLFSGS 425
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLgHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 IEENLRYGKENATHDELEVAAAsACATEFINKLEESYQYnltqgatnLSGGQKQRVSIARALVRKPPILILDDSTSAVDA 505
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAA-LEAVGLAPLAHLPFGY--------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
....
gi 1265247244 506 KSEA 509
Cdd:PRK13539 161 AAVA 164
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-549 |
1.78e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 87.33 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 334 NIEFKNVSYSYTKNNEYV--LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD---QGEICIDGIDVKTYDLQKl 408
Cdd:cd03234 3 VLPWWDVGLKAKNWNKYAriLNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQK- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 raSIGFVPQKALLFSG-SIEENLRYGKENATHDEL---------EVAAASACATEFI-NKLeesyqynltqgATNLSGGQ 477
Cdd:cd03234 82 --CVAYVRQDDILLPGlTVRETLTYTAILRLPRKSsdairkkrvEDVLLRDLALTRIgGNL-----------VKGISGGE 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 478 KQRVSIARALVRKPPILILDDSTSAVDAKSE-ATIQTALKTKYKGTTTLL-IASKISSIMDA-DKILVLDNGELV 549
Cdd:cd03234 149 RRRVSIAVQLLWDPKVLILDEPTSGLDSFTAlNLVSTLSQLARRNRIVILtIHQPRSDLFRLfDRILLLSSGEIV 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
351-552 |
1.85e-19 |
|
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: 87.77 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIdVKTYDLQKLRASIGFV-PQKA-LLFSGSIEE 428
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfGQKTqLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLRYGKENATHDELEvaaasacATEFINKLEESYQYN--LTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAK 506
Cdd:cd03267 115 SFYLLAAIYDLPPAR-------FKKRLDELSELLDLEelLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265247244 507 SEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNG 552
Cdd:cd03267 188 AQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
335-558 |
2.14e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.15 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK11231 3 LRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYGKEN--------ATHDE--LEVAAASACATEFINKLeesyqynltqgATNLSGGQKQRVSI 483
Cdd:PRK11231 81 LPQHHLTPEGiTVRELVAYGRSPwlslwgrlSAEDNarVNQAMEQTRINHLADRR-----------LTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 484 ARALVRKPPILILDDSTSAVDAKSEATIQT---ALKTKYKGTTTLL----IASKIssimdADKILVLDNGELVGNGTHEQ 556
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRlmrELNTQGKTVVTVLhdlnQASRY-----CDHLVVLANGHVMAQGTPEE 224
|
..
gi 1265247244 557 LL 558
Cdd:PRK11231 225 VM 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-567 |
3.98e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 333 GNIEFKNVSYSYTKNNEY---VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV-----KTYD 404
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 405 LQKLRASIGFVPQ--KALLFSGSIEENLRYGKENATHDELEVAAASACATEFInKLEESYqynLTQGATNLSGGQKQRVS 482
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 483 IARALVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLE 559
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFErlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIFS 240
|
....*...
gi 1265247244 560 RSEVYQEI 567
Cdd:PRK13645 241 NQELLTKI 248
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
335-553 |
4.29e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNE--------------------YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEIC 394
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 395 IDG-----IDVKTydlqklrasiGFVPQkallFSGsiEENLR-----YGKENATHDEL--EVAAASACAtEFIN---Kle 459
Cdd:COG1134 85 VNGrvsalLELGA----------GFHPE----LTG--RENIYlngrlLGLSRKEIDEKfdEIVEFAELG-DFIDqpvK-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 460 esyqynltqgatNLSGGQKQRVSIARALVRKPPILILDDSTSAVDA----KSEAtiqtALKTKYKGTTTLLIAS-KISSI 534
Cdd:COG1134 146 ------------TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLA----RIRELRESGRTVIFVShSMGAV 209
|
250 260
....*....|....*....|
gi 1265247244 535 MD-ADKILVLDNGELVGNGT 553
Cdd:COG1134 210 RRlCDRAIWLEKGRLVMDGD 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
335-559 |
5.23e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.12 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIGF 414
Cdd:PRK11607 20 LEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYGKEnatHDELEVAAASACATEFINKLEesYQYNLTQGATNLSGGQKQRVSIARALVRKPPI 493
Cdd:PRK11607 96 MFQSYALFPHmTVEQNIAFGLK---QDKLPKAEIASRVNEMLGLVH--MQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 494 LILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLE 559
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
335-505 |
5.68e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 88.62 E-value: 5.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKlrASIGF 414
Cdd:PRK11432 7 VVLKNITKRFGSNT--VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG-SIEENLRYG--KENATHDELEVAAASACATEFINKLEESYqynltqgATNLSGGQKQRVSIARALVRKP 491
Cdd:PRK11432 83 VFQSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRY-------VDQISGGQQQRVALARALILKP 155
|
170
....*....|....
gi 1265247244 492 PILILDDSTSAVDA 505
Cdd:PRK11432 156 KVLLFDEPLSNLDA 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
334-548 |
6.14e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.93 E-value: 6.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 334 NIEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIG 413
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQK-ALLFSGSIEENLRYGKENATHDELEVAaasacatEFINKLEESYQYN--LTQGATNLSGGQKQRVSIARALVRK 490
Cdd:PRK11000 79 MVFQSyALYPHLSVAENMSFGLKLAGAKKEEIN-------QRVNQVAEVLQLAhlLDRKPKALSGGQRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 491 PPILILDDSTSAVDA--KSEATIQTA-LKTKYKGTTTLLIASKISSIMDADKILVLDNGEL 548
Cdd:PRK11000 152 PSVFLLDEPLSNLDAalRVQMRIEISrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
351-581 |
6.82e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 91.38 E-value: 6.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDgidvktydlqklrASIGFVPQKALLFSGSIEEN- 429
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNi 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 430 LRYGKENAT--HDELEVAAASACATEFINKLEESyqynLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAK- 506
Cdd:PTZ00243 742 LFFDEEDAArlADAVRVSQLEADLAQLGGGLETE----IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHv 817
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 507 SEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQLLeRSEVYQEiyLSQGGNLHKEGGE 581
Cdd:PTZ00243 818 GERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYAT--LAAELKENKDSKE 889
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
350-552 |
1.09e-18 |
|
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: 85.28 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 350 YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQklrasIGFVPQkallFSGsiEEN 429
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG-----GGFNPE----LTG--REN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 430 LR-----YGKENATHDELEvaaasacatEFI---NKLEESYQYNLtqgaTNLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:cd03220 105 IYlngrlLGLSRKEIDEKI---------DEIiefSELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 502 AVDAKSEATIQTALKTKYKGTTTLLIAS-KISSIMD-ADKILVLDNGELVGNG 552
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTVILVShDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-575 |
1.20e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.33 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDL-QKLRASIGFVPQKALLFSG-SIEE 428
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLRYGKEnaTHDELEVAAASACATEFINKLEESY-QYNLTQgatNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKS 507
Cdd:PRK10895 98 NLMAVLQ--IRDDLSAEQREDRANELMEEFHIEHlRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 508 EATIQTALK-TKYKGTTTLLIASKISSIMDA-DKILVLDNGELVGNGTHEQLLERSEVyQEIYLSQGGNL 575
Cdd:PRK10895 173 VIDIKRIIEhLRDSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEILQDEHV-KRVYLGEDFRL 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
335-504 |
1.21e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQK-ALLFSGSIEENLRYGKEN-----ATHDE-----LEVAAASACATEFINkleesyqynltQGATNLSGGQKQRVSI 483
Cdd:PRK09536 82 VPQDtSLSFEFDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFAD-----------RPVTSLSGGERQRVLL 150
|
170 180
....*....|....*....|.
gi 1265247244 484 ARALVRKPPILILDDSTSAVD 504
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLD 171
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
335-555 |
2.15e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.68 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG--------IDVKtyDLQ 406
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDK--AIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRASIGFVPQKALLFSG-SIEENLRYGKENAThdELEVAAASACATEFINKLEesyqynLTQGAT----NLSGGQKQRV 481
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHlTVQQNLIEAPCRVL--GLSKDQALARAEKLLERLR------LKPYADrfplHLSGGQQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 482 SIARALVRKPPILILDDSTSAVDAKSEATI--------QTALkTKYKGTTTLLIASKISSimdadKILVLDNGELVGNGT 553
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIvsiirelaETGI-TQVIVTHEVEVARKTAS-----RVVYMENGHIVEQGD 224
|
..
gi 1265247244 554 HE 555
Cdd:PRK11124 225 AS 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
352-550 |
2.16e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD-LQKLRASIGFVPQKALLFSG-SIEEN 429
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 430 LRYGKENATHDELEVAAASAcatefinKLEE-SYQYNL----TQGATNLSGGQKQRVSIARALVRKPPILILDDSTsAV- 503
Cdd:COG3845 101 IVLGLEPTKGGRLDRKAARA-------RIRElSERYGLdvdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPT-AVl 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265247244 504 -DAKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:COG3845 173 tPQEADELFEILRRLAAEGKSIIFITHKLREVMAiADRVTVLRRGKVVG 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-550 |
2.45e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRAS-IGFVPQ----KALLFSGS 425
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEdrlgRGLVPDMS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 IEENL---RYGKEN-ATHDELEVAAASACATEFINKleesyqYNL-TQG----ATNLSGGQKQRVSIARALVRKPPILIL 496
Cdd:COG3845 353 VAENLilgRYRRPPfSRGGFLDRKAIRAFAEELIEE------FDVrTPGpdtpARSLSGGNQQKVILARELSRDPKLLIA 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 497 DDSTSAVDAKSEATIQTAL-KTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:COG3845 427 AQPTRGLDVGAIEFIHQRLlELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVG 482
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
335-548 |
3.82e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.72 E-value: 3.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGF 414
Cdd:PRK10522 323 LELRNVTFAYQDNG-FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIeenlryGKENATHDELEVAAasacateFINKLEESYQYNLTQGA---TNLSGGQKQRVSIARALVRKP 491
Cdd:PRK10522 402 VFTDFHLFDQLL------GPEGKPANPALVEK-------WLERLKMAHKLELEDGRisnLKLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTAL--KTKYKGTTTLLIASKISSIMDADKILVLDNGEL 548
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLlpLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-560 |
5.15e-18 |
|
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: 87.17 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRL--YDVDQGEI------------------- 393
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 394 ------C-----------IDGIDVKTYDLQKlRASIGFVPQKALLFSGSIEENLRygkeNATHD-ELEVAAASACATEFI 455
Cdd:TIGR03269 79 gepcpvCggtlepeevdfWNLSDKLRRRIRK-RIAIMLQRTFALYGDDTVLDNVL----EALEEiGYEGKEAVGRAVDLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 456 NKLEESYQynLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGT-TTLLIASKISSI 534
Cdd:TIGR03269 154 EMVQLSHR--ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEV 231
|
250 260
....*....|....*....|....*...
gi 1265247244 535 MD--ADKILVLDNGELVGNGTHEQLLER 560
Cdd:TIGR03269 232 IEdlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-549 |
7.30e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.60 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVS---YSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDlqkl 408
Cdd:COG1101 2 LELKNLSktfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 RAS-IGFVPQKALL---FSGSIEEN------------LRYGKENATHDELEvaaasacatEFINKLEESYQYNLTQGATN 472
Cdd:COG1101 78 RAKyIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFR---------ELLATLGLGLENRLDTKVGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 473 LSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTalKTKY----KGTTTLLIASKISsimDA----DKILVLD 544
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE--LTEKiveeNNLTTLMVTHNME---QAldygNRLIMMH 223
|
....*
gi 1265247244 545 NGELV 549
Cdd:COG1101 224 EGRII 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
338-569 |
1.58e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 338 KNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDL-QKLRASIGFVP 416
Cdd:COG1137 7 ENLVKSYGKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhKRARLGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 417 QKALLFSG-SIEENLRygkenAThdeLEVAAASAcaTEFINKLEE-----SYQYNLTQGATNLSGGQKQRVSIARALVRK 490
Cdd:COG1137 85 QEASIFRKlTVEDNIL-----AV---LELRKLSK--KEREERLEElleefGITHLRKSKAYSLSGGERRRVEIARALATN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 491 PPILILDDSTSAVDAKSEATIQTALKT-KYKG-----T-----TTLLIaskissimdADKILVLDNGELVGNGTHEQLLE 559
Cdd:COG1137 155 PKFILLDEPFAGVDPIAVADIQKIIRHlKERGigvliTdhnvrETLGI---------CDRAYIISEGKVLAEGTPEEILN 225
|
250
....*....|
gi 1265247244 560 RSEVyQEIYL 569
Cdd:COG1137 226 NPLV-RKVYL 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-564 |
1.86e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKlRASIGF 414
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQ-KALLFSGSIEENLR-----YGKENAThdeleVAAASACATEFInKLEESYQYNLTQgatnLSGGQKQRVSIARALV 488
Cdd:PRK13537 85 VPQfDNLDPDFTVRENLLvfgryFGLSAAA-----ARALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 489 RKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD--ADKILVLDNGELVGNGTHEQLLERS----- 561
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErlCDRLCVIEEGRKIAEGAPHALIESEigcdv 234
|
....
gi 1265247244 562 -EVY 564
Cdd:PRK13537 235 iEIY 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-562 |
1.92e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.20 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNneYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQ-----GEICIDGIDVKTYDLQ--K 407
Cdd:PRK14267 5 IETVNLRVYYGSN--HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDpiE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQKALLFSG-SIEEN----LRYGKENATHDELE--VAAASACATefinkLEESYQYNLTQGATNLSGGQKQR 480
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNvaigVKLNGLVKSKKELDerVEWALKKAA-----LWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDAKSEATIQT---ALKTKYkgTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQL 557
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEEllfELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
....*
gi 1265247244 558 LERSE 562
Cdd:PRK14267 236 FENPE 240
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
335-563 |
2.04e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.85 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLL---PRlydVDQGEICIDGIDVKTYDLQK-LRA 410
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLcgdPR---ATSGRIVFDGKDITDWQTAKiMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 411 SIGFVPQKALLFSG-SIEENLRYGKENATHDELEVAAASAcaTEFINKLEESYqynlTQGATNLSGGQKQRVSIARALVR 489
Cdd:PRK11614 81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHERR----IQRAGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 490 KPPILILDDSTSAVdakSEATIQTALKT----KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERSEV 563
Cdd:PRK11614 155 QPRLLLLDEPSLGL---APIIIQQIFDTieqlREQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
352-558 |
2.55e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 2.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQK-LRASIGFVPQK----ALLFSGSI 426
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 427 EEN-----LRYGKENATHdeLEVAAASACATEFInKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:PRK10762 348 KENmsltaLRYFSRAGGS--LKHADEQQAVSDFI-RLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 502 AVD--AKSEaTIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVG-----NGTHEQLL 558
Cdd:PRK10762 425 GVDvgAKKE-IYQLINQFKAEGLSIILVSSEMPEVLGmSDRILVMHEGRISGeftreQATQEKLM 488
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
350-511 |
3.46e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 350 YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktYDLQKLRAS---------IGFVPQ-KA 419
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNG-----QPMSKLSSAakaelrnqkLGFIYQfHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 420 LLFSGSIEEN----LRYGKEN---ATHDELEVAAASAcatefinkLEESYQYNltqgATNLSGGQKQRVSIARALVRKPP 492
Cdd:PRK11629 98 LLPDFTALENvampLLIGKKKpaeINSRALEMLAAVG--------LEHRANHR----PSELSGGERQRVAIARALVNNPR 165
|
170
....*....|....*....
gi 1265247244 493 ILILDDSTSAVDAKSEATI 511
Cdd:PRK11629 166 LVLADEPTGNLDARNADSI 184
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
335-515 |
4.49e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 81.45 E-value: 4.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEY--VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDlqklrASI 412
Cdd:COG4525 4 LTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQK-ALLFSGSIEENLRYGKENAThdeLEVAAASACATEFINK--LEESYQYNLTQgatnLSGGQKQRVSIARALVR 489
Cdd:COG4525 79 GVVFQKdALLPWLNVLDNVAFGLRLRG---VPKAERRARAEELLALvgLADFARRRIWQ----LSGGMRQRVGIARALAA 151
|
170 180
....*....|....*....|....*.
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTAL 515
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELL 177
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
352-550 |
1.09e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD--QGEICIDGIDVKTYDLQKL-RASIGFVPQKALLFSG-SIE 427
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGatNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKS 507
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVG--NLGLGQQQLVEIAKALNKQARLLILDEPTASLTESE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265247244 508 EATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:PRK13549 179 TAVLLDIIRDlKAHGIACIYISHKLNEVKAiSDTICVIRDGRHIG 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
338-548 |
1.36e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.72 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 338 KNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEIcIDGidvkTYDLQKLRASIGFVPQ 417
Cdd:PRK11247 16 NAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 418 KA-LLFSGSIEEN----LRYGKENATHDELEVAAASACATEFinkleesyqynltqgATNLSGGQKQRVSIARALVRKPP 492
Cdd:PRK11247 89 DArLLPWKKVIDNvglgLKGQWRDAALQALAAVGLADRANEW---------------PAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKIS-SIMDADKILVLDNGEL 548
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
335-517 |
1.48e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNneYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDV-----DQGEICIDGIDV--KTYDLQK 407
Cdd:PRK14243 11 LRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 408 LRASIGFVPQKALLFSGSIEENLRYGKE----NATHDELEVAAASACA--TEFINKLEESyqynltqgATNLSGGQKQRV 481
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSLRQAAlwDEVKDKLKQS--------GLSLSGGQQQRL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1265247244 482 SIARALVRKPPILILDDSTSAVDAKSEATIQTALKT 517
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHE 196
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
335-560 |
1.77e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.15 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtydlQKLRASIGF 414
Cdd:COG4152 2 LELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQ-KALLFSGSIEENLRY-----GkenathdeLEVAAASACATEFINKLE-ESYQYNLTQgatNLSGGQKQRVSIARAL 487
Cdd:COG4152 76 LPEeRGLYPKMKVGEQLVYlarlkG--------LSKAEAKRRADEWLERLGlGDRANKKVE---ELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLiaskiSS-IMD-----ADKILVLDNGELVGNGTHEQLLER 560
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRElAAKGTTVIF-----SShQMElveelCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
352-583 |
1.94e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 80.52 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLL-----PrlydvDQGEICIDGID-VKtyDLQKLRASIGFV-PQKA-LLFS 423
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvP-----TSGEVRVLGYVpFK--RRKEFARRIGVVfGQRSqLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 GSIEENLR-----YGKENATHDE-LEvaaasacatEFINKLE-ESYqynLTQGATNLSGGQKQRVSIARALVRKPPILIL 496
Cdd:COG4586 111 LPAIDSFRllkaiYRIPDAEYKKrLD---------ELVELLDlGEL---LDTPVRQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 497 DDSTSAVDAKSEATIQTALKT--KYKGTTTLLiaskISSIMD-----ADKILVLDNGELVGNGTHEQLLER--------- 560
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEynRERGTTILL----TSHDMDdiealCDRVIVIDHGRIIYDGSLEELKERfgpyktivl 254
|
250 260
....*....|....*....|....*
gi 1265247244 561 --SEVYQEIYLSQGGNLHKEGGEEH 583
Cdd:COG4586 255 elAEPVPPLELPRGGEVIEREGNRV 279
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
334-506 |
2.27e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 80.66 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 334 NIEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtyDLQKLRASIG 413
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQ-VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN--ELEPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQK-ALLFSGSIEENLRYGKENATHDELEVAAASACATEfINKLEESYQYNLTQgatnLSGGQKQRVSIARALVRKPP 492
Cdd:PRK11650 80 MVFQNyALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAAR-ILELEPLLDRKPRE----LSGGQRQRVAMGRAIVREPA 154
|
170
....*....|....
gi 1265247244 493 ILILDDSTSAVDAK 506
Cdd:PRK11650 155 VFLFDEPLSNLDAK 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
351-531 |
2.38e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.97 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDlqklrASIGFVPQ-KALLFSGSIEEN 429
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQnEGLLPWRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 430 LRYGKENATHDELEVAAAsacATEFINK--LEESYQYNLTQgatnLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKS 507
Cdd:PRK11248 91 VAFGLQLAGVEKMQRLEI---AHQMLKKvgLEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*.
gi 1265247244 508 EATIQTALKTKYKGT--TTLLIASKI 531
Cdd:PRK11248 164 REQMQTLLLKLWQETgkQVLLITHDI 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
349-544 |
3.38e-16 |
|
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: 77.53 E-value: 3.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 349 EYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG--IDVKTYDLQKLRASIGFVPQ-KALLfsgS 425
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpLDFQRDSIARGLLYLGHAPGiKTTL---S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 IEENLRYGKENATHDELEvaaaSACATEFINKLEESyqynltqGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDA 505
Cdd:cd03231 90 VLENLRFWHADHSDEQVE----EALARVGLNGFEDR-------PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1265247244 506 KSEATIQTALKTKYKGTTTLLIASKISSIMDADKILVLD 544
Cdd:cd03231 159 AGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELD 197
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
335-551 |
3.64e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.99 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRAS 411
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKA-LLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLtqgatNLSGGQKQRVSIARALVRK 490
Cdd:PRK10908 81 IGMIFQDHhLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 491 PPILILDDSTSAVD-AKSEATIQTALKTKYKGTTTLLIASKISSIMDAD-KILVLDNGELVGN 551
Cdd:PRK10908 156 PAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHGG 218
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
351-568 |
4.18e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLFSGSIEENL 430
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 431 -------------RYGKENatHDELEVAAASACATEFINKLEESyqynltqgatnLSGGQKQRVSIARALVRKPPILILD 497
Cdd:PRK10575 106 vaigrypwhgalgRFGAAD--REKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 498 DSTSAVDAKSE----ATIQTAlkTKYKGTTTLLIASKISsiMDA---DKILVLDNGELVGNGTHEQLLeRSEVYQEIY 568
Cdd:PRK10575 173 EPTSALDIAHQvdvlALVHRL--SQERGLTVIAVLHDIN--MAArycDYLVALRGGEMIAQGTPAELM-RGETLEQIY 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
346-583 |
4.48e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 346 KNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtydlQKLRAS-IGFVPQKALL--- 421
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVPQSEEVdws 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 422 FSGSIEENL---RYG-----KENATHDELEVAAASAcateFINKLEESYQYnltqgATNLSGGQKQRVSIARALVRKPPI 493
Cdd:PRK15056 93 FPVLVEDVVmmgRYGhmgwlRRAKKRDRQIVTAALA----RVDMVEFRHRQ-----IGELSGGQKKRVFLARAIAQQGQV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 494 LILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMDADKILVLDNGELVGNGTHEQL-----LER--SEVYQ 565
Cdd:PRK15056 164 ILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTftaenLELafSGVLR 243
|
250
....*....|....*...
gi 1265247244 566 EIYLSqggnlhkeGGEEH 583
Cdd:PRK15056 244 HVALN--------GSEES 253
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-560 |
5.08e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 5.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD-----QGEICIDGIDVKTYDLQKLR 409
Cdd:PRK14247 4 IEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 ASIGFVPQ-KALLFSGSIEENLRYG-KEN---ATHDELEVAAASACATEfinKLEESYQYNLTQGATNLSGGQKQRVSIA 484
Cdd:PRK14247 82 RRVQMVFQiPNPIPNLSIFENVALGlKLNrlvKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLI------ASKISsimdaDKILVLDNGELVGNGTHEQLL 558
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVthfpqqAARIS-----DYVAFLYKGQIVEWGPTREVF 233
|
..
gi 1265247244 559 ER 560
Cdd:PRK14247 234 TN 235
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
21-309 |
5.13e-16 |
|
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: 78.83 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 21 GPLFMVLEVAMDLIQPTIMQHIIDVGI---------ANRDLNYVIkMGLLMIGaaalgLVGGLGCMMYS---TKAAVNFA 88
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTnhsgsggeeALRALNQAV-LILLGVV-----LIGSIATFLRSwlfTLAGERVV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 89 TDIRKDVFAKIE----TFSSNNRdsfgTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLV 164
Cdd:cd18780 75 ARLRKRLFSAIIaqeiAFFDVTR----TGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 165 VVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFG-SVNTNLtKINIRAVQLISLMM 243
Cdd:cd18780 151 VVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSeKINESY-LLGKKLARASGGFN 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 244 PIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18780 230 GFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
350-511 |
6.53e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 6.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 350 YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKT---YDLQKLRASIGFVPQKA------- 419
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspGKLQALRRDIQFIFQDPyasldpr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 420 LLFSGSIEENLRygkenaTHDELEVAAASACATEFINKL----EESYQYnltqgATNLSGGQKQRVSIARALVRKPPILI 495
Cdd:PRK10261 418 QTVGDSIMEPLR------VHGLLPGKAAAARVAWLLERVgllpEHAWRY-----PHEFSGGQRQRICIARALALNPKVII 486
|
170
....*....|....*.
gi 1265247244 496 LDDSTSAVDAKSEATI 511
Cdd:PRK10261 487 ADEAVSALDVSIRGQI 502
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
335-557 |
9.45e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 9.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidVKTYDLQKLRA---S 411
Cdd:PRK15439 12 LCARSISKQYSGVE--VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG--NPCARLTPAKAhqlG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYG--KENATHDELEvaaasacatefiNKLEE-SYQYNLTQGATNLSGGQKQRVSIARAL 487
Cdd:PRK15439 88 IYLVPQEPLLFPNlSVKENILFGlpKRQASMQKMK------------QLLAAlGCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 488 VRKPPILILDDSTSAVD-AKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
352-546 |
9.77e-16 |
|
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: 76.74 E-value: 9.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLrasigFVPQK-ALLFSGSIEENL 430
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNySLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 431 RYGKENATHDelevaaasACATEFINKLEESYQY-NLTQGA----TNLSGGQKQRVSIARALVRKPPILILDDSTSAVDA 505
Cdd:TIGR01184 76 ALAVDRVLPD--------LSKSERRAIVEEHIALvGLTEAAdkrpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1265247244 506 KSEATIQTALKTKYK--GTTTLLIASKI-SSIMDADKILVLDNG 546
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
348-522 |
1.65e-15 |
|
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: 79.59 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 348 NEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPrlydvdqgeicidGIDvKTYDLQKLRA---SIGFVPQKALL--- 421
Cdd:TIGR03719 17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFNGEARPQpgiKVGYLPQEPQLdpt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 422 --FSGSIEE---------------NLRYGKENATHD-------ELEVAAASACATEFINKLEESYQ-YNLTQG---ATNL 473
Cdd:TIGR03719 83 ktVRENVEEgvaeikdaldrfneiSAKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDaLRCPPWdadVTKL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265247244 474 SGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKtKYKGT 522
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ-EYPGT 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
351-504 |
1.70e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV----------KTYD---LQKLRASIGFVPQ 417
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADknqLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 418 KALLFSG-SIEENLRYGKENATHdeLEVAAASACATEFINK--LEESYQynlTQGATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVLG--LSKQEARERAVKYLAKvgIDERAQ---GKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170
....*....|
gi 1265247244 495 ILDDSTSAVD 504
Cdd:PRK10619 175 LFDEPTSALD 184
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
352-546 |
3.21e-15 |
|
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: 75.06 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLakLLPRLYDVD--QGEI----CIDGIDVKTYDLQKLRASIGFVPQKALLFSGS 425
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQtlEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 IEENLRYGkeNATHDELEVAAASACATE-FINKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVD 504
Cdd:cd03290 95 VEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265247244 505 AK-SEATIQTALKT--KYKGTTTLLIASKISSIMDADKILVLDNG 546
Cdd:cd03290 173 IHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
339-560 |
4.39e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 4.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 339 NVSYSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG----------IDVKTYDLQKL 408
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 R----ASIGFVPQKAL-----LFS--GSIEENLRYgKENATHDElevaaASACATEFIN--KLEESyQYNLTQGATNLSG 475
Cdd:PRK10261 99 RhvrgADMAMIFQEPMtslnpVFTvgEQIAESIRL-HQGASREE-----AMVEAKRMLDqvRIPEA-QTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 476 GQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTT--TLLIASKISSIMD-ADKILVLDNGELVGNG 552
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
....*...
gi 1265247244 553 THEQLLER 560
Cdd:PRK10261 252 SVEQIFHA 259
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
352-560 |
4.63e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.54 E-value: 4.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD---LQKLRASIGFV---------PQKA 419
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVfqnpygslnPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 420 LlfsGSI-EENLrygkenATHDELEVAAASACATEFINKL---EESYQ-YnltqgATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:PRK11308 111 V---GQIlEEPL------LINTSLSAAERREKALAMMAKVglrPEHYDrY-----PHMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 495 ILDDSTSAVDAKSEATI-------QTALKTKYkgtttLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLER 560
Cdd:PRK11308 177 VADEPVSALDVSVQAQVlnlmmdlQQELGLSY-----VFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-559 |
4.86e-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: 77.92 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNEYVLK---DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICI----DGIDV-KTYDLQ 406
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMtKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 407 KLRAS--IGFVPQKALLFS-GSIEENLrygkENATHDEL--EVAAASACATEFINKLEESYQYN-LTQGATNLSGGQKQR 480
Cdd:TIGR03269 360 RGRAKryIGILHQEYDLYPhRTVLDNL----TEAIGLELpdELARMKAVITLKMVGFDEEKAEEiLDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 481 VSIARALVRKPPILILDDSTSAVDAKSEATI-QTALKTKYKGTTTLLIaskISSIMD-----ADKILVLDNGELVGNGTH 554
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEMEQTFII---VSHDMDfvldvCDRAALMRDGKIVKIGDP 512
|
....*
gi 1265247244 555 EQLLE 559
Cdd:TIGR03269 513 EEIVE 517
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
351-559 |
4.86e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 4.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLL---PRlYDVDQGEICIDGID--------------------------VK 401
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDilelspderaragiflafqypveipgVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 402 TYDLqkLRASIGFVPQKALlfsgSIEENLRYGKENAthDELEVAAasacatEFINKleesyqyNLTQGatnLSGGQKQRV 481
Cdd:COG0396 94 VSNF--LRTALNARRGEEL----SAREFLKLLKEKM--KELGLDE------DFLDR-------YVNEG---FSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 482 SIARALVRKPPILILD--DSTSAVDakseatiqtALKT--------KYKGTTTLLIA--SKISSIMDADKILVLDNGELV 549
Cdd:COG0396 150 EILQMLLLEPKLAILDetDSGLDID---------ALRIvaegvnklRSPDRGILIIThyQRILDYIKPDFVHVLVDGRIV 220
|
250
....*....|
gi 1265247244 550 GNGTHEQLLE 559
Cdd:COG0396 221 KSGGKELALE 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
351-515 |
5.95e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.55 E-value: 5.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRAS--IGFVPQ-KALLfsgSIE 427
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlyLGHLPGlKPEL---SAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLRYgkENATHDELEVAAASACATEFINKLEESyqynltqGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKS 507
Cdd:TIGR01189 92 ENLHF--WAAIHGGAQRTIEDALAAVGLTGFEDL-------PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
....*...
gi 1265247244 508 EATIQTAL 515
Cdd:TIGR01189 163 VALLAGLL 170
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
351-559 |
6.07e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 73.72 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLL---PRlYDVDQGEICIDGIDVKtyDL---QKLRASIGFVPQKALLFSG 424
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghPK-YEVTEGEILFKGEDIT--DLppeERARLGIFLAFQYPPEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 -SIEENLRYgkenathdelevaaasacatefINKleesyqynltqgatNLSGGQKQRVSIARALVRKPPILILDDSTSAV 503
Cdd:cd03217 92 vKNADFLRY----------------------VNE--------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 504 DAKSEATIQTALKTKYKGTTTLLIAS---KISSIMDADKILVLDNGELVGNGTHEQLLE 559
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIIThyqRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
351-543 |
1.46e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.27 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklRASIGFVPQKALL---FSGSIE 427
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLRYG--------KENATHDELEVAAASAC--ATEFINK-LEEsyqynltqgatnLSGGQKQRVSIARALVRKPPILIL 496
Cdd:NF040873 76 DLVAMGrwarrglwRRLTRDDRAAVDDALERvgLADLAGRqLGE------------LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265247244 497 DDSTSAVDAKSEATIQTALKTKY-KGTTTLLIASKISSIMDADKILVL 543
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
353-550 |
1.62e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 353 KDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYD-LQKLRASIGFVP----QKALLFSGSIE 427
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPedrqSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 EN------------LRYGKENATHDELEVAAASACAtefinkleesyqyNLTQGATNLSGGQKQRVSIARALVRKPPILI 495
Cdd:PRK15439 360 WNvcalthnrrgfwIKPARENAVLERYRRALNIKFN-------------HAEQAARTLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 496 LDDSTSAVDAKSEATIQTALKTKYK-GTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIEQmADRVLVMHQGEISG 483
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
53-309 |
1.66e-14 |
|
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: 74.43 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 53 NYVIKMGLLMIGAAALGLVGgLGCMMYstkAAVNFATDIRKDVFAK-----IETFssnnrDSFGTGKLLTIVTNDITSIQ 127
Cdd:cd18577 48 KYALYFVYLGIGSFVLSYIQ-TACWTI---TGERQARRIRKRYLKAllrqdIAWF-----DKNGAGELTSRLTSDTNLIQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 128 SAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRV 207
Cdd:cd18577 119 DGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 208 IKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILM 287
Cdd:cd18577 199 VKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAF 278
|
250 260
....*....|....*....|..
gi 1265247244 288 SLMSISMVFIQIARAFPSADRV 309
Cdd:cd18577 279 SLGQIAPNLQAFAKARAAAAKI 300
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
346-559 |
2.83e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 2.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 346 KNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLP--RLYDVD-QGEICIDGIDVktyDLQKLRASIGFVPQKALLF 422
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrSPKGVKgSGSVLLNGMPI---DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 423 -SGSIEENLRY-------------GKENATHDELEVAAASACATEFINkleesyQYNLTQGatnLSGGQKQRVSIARALV 488
Cdd:TIGR00955 112 pTLTVREHLMFqahlrmprrvtkkEKRERVDEVLQALGLRKCANTRIG------VPGRVKG---LSGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 489 RKPPILILDDSTSAVDAKSEAT-IQTALKTKYKGTTTLL-IASKISSIMDA-DKILVLDNGELVGNGTHEQLLE 559
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSvVQVLKGLAQKGKTIICtIHQPSSELFELfDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-571 |
4.10e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 348 NEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG--IDVKTYDLQKLRASIGFVPQ--KALLFS 423
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQdpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 GSIEENLRYGKENATHDELEVAAASACATEFINKleesyQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAV 503
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDA-----QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 504 DAKSEATIQTALKTKYKGTTTLLIAS-KISSIMD-ADKILVLDNGELVGNGTHEQLLERSEVYQEIYLSQ 571
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISShDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQAGLTQ 237
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
351-568 |
4.13e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKALLfSGSIEENL 430
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATT-PGDITVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 431 RYGKENATHDEL--------EVAAASACATEFINKLEesyqynlTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSA 502
Cdd:PRK10253 101 LVARGRYPHQPLftrwrkedEEAVTKAMQATGITHLA-------DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 503 VDAKSEATIQTALK--TKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLErSEVYQEIY 568
Cdd:PRK10253 174 LDISHQIDLLELLSelNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVT-AELIERIY 241
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
327-559 |
4.23e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 327 EPEKI-EGNIEFKNVS-YSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYD-VDQGEICIDGIDVKTY 403
Cdd:PRK13549 251 EPHTIgEVILEVRNLTaWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 404 D-LQKLRASIGFVPqkallfsgsiEENLRYG-------KENAT---------HDELEVAAASACATEFINKLEESYQyNL 466
Cdd:PRK13549 331 NpQQAIAQGIAMVP----------EDRKRDGivpvmgvGKNITlaaldrftgGSRIDDAAELKTILESIQRLKVKTA-SP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 467 TQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIqtalktkYK--------GTTTLLIASKISSIMD-A 537
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEI-------YKlinqlvqqGVAIIVISSELPEVLGlS 472
|
250 260
....*....|....*....|....*..
gi 1265247244 538 DKILVLDNGELVG-----NGTHEQLLE 559
Cdd:PRK13549 473 DRVLVMHEGKLKGdlinhNLTQEQVME 499
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
335-504 |
1.21e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDgidvktydlQKLRasIGF 414
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSG---SIEENLRYgKENATHDELEVAAASACATEFINkleesyqynltQGATNLSGGQKQRVSIARALVRKP 491
Cdd:PRK09544 72 VPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLID-----------APMQKLSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 1265247244 492 PILILDDSTSAVD 504
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
337-552 |
1.34e-13 |
|
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: 69.98 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 337 FKNVSY--SYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTL----AKLLPRLYDVDqGEICIDGIDVKTyDLQKLRA 410
Cdd:cd03233 6 WRNISFttGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkalANRTEGNVSVE-GDIHYNGIPYKE-FAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 411 SIGFVPQKALLFSG-SIEENLRYgkenathdelevaAASACATEFINKleesyqynltqgatnLSGGQKQRVSIARALVR 489
Cdd:cd03233 84 EIIYVSEEDVHFPTlTVRETLDF-------------ALRCKGNEFVRG---------------ISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKISSIMDA--DKILVLDNGELVGNG 552
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASDEIYDlfDKVLVLYEGRQIYYG 202
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
343-557 |
2.14e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.43 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 343 SYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQ---GEICIDGIDVK-----TYDLQKLRASIGF 414
Cdd:PRK09984 11 AKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQregrlARDIRKSRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQK-ALLFSGSIEENLRYGKENAThdelevAAASACATEFINKLEESYQYNLT---------QGATNLSGGQKQRVSIA 484
Cdd:PRK09984 91 IFQQfNLVNRLSVLENVLIGALGST------PFWRTCFSWFTREQKQRALQALTrvgmvhfahQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 485 RALVRKPPILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKIS-SIMDADKILVLDNGELVGNGTHEQL 557
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
352-565 |
2.30e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTL----AKLLPrlydvDQGEICIDGIDVKTYDLQKL---RAsigFVPQK-ALLFS 423
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLlarmAGLLP-----GQGEILLNGRPLSDWSAAELarhRA---YLSQQqSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 GSIEENLRYGKEnATHDELEVAAASACATEFInKLEESYQYNLTQgatnLSGGQKQRVSIARALVRKPP-------ILIL 496
Cdd:COG4138 84 MPVFQYLALHQP-AGASSEAVEQLLAQLAEAL-GLEDKLSRPLTQ----LSGGEWQRVRLAAVLLQVWPtinpegqLLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 497 DDSTSAVDAKSEATIQTALKTkykgtttlLIASKISSIM----------DADKILVLDNGELVGNGTHEQLLER---SEV 563
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLRE--------LCQQGITVVMsshdlnhtlrHADRVWLLKQGKLVASGETAEVMTPenlSEV 229
|
..
gi 1265247244 564 YQ 565
Cdd:COG4138 230 FG 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
351-558 |
2.96e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.51 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDV-----DQGEICIDGIDVKTY-DLQKLRASIGFVPQKALLFSG 424
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 SIEENLRYG---KENATHDELEvAAASACATEFinKLEESYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:PRK14271 116 SIMDNVLAGvraHKLVPRKEFR-GVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 502 AVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
327-559 |
2.98e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.16 E-value: 2.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 327 EPEKIEGNI-EFKNVS-YSYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD-QGEICIDG--IDVK 401
Cdd:TIGR02633 249 EPHEIGDVIlEARNLTcWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 402 TyDLQKLRASIGFVPQ----KALLFSGSIEENLRYG--KENATHDELEVAAASACATEFINKLE-ESYQYNLTQGatNLS 474
Cdd:TIGR02633 329 N-PAQAIRAGIAMVPEdrkrHGIVPILGVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKvKTASPFLPIG--RLS 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 475 GGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTAL-KTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNG 552
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLInQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDF 485
|
250
....*....|..
gi 1265247244 553 -----THEQLLE 559
Cdd:TIGR02633 486 vnhalTQEQVLA 497
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
351-558 |
3.07e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.43 E-value: 3.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLA----KLLPR---LYDvdQGEICIDGIDVKTYDLQKLRASIGfvPQKALLFS 423
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTAlsilRLLPSppvVYP--SGDIRFHGESLLHASEQTLRGVRG--NKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 ---------GSIEENLRygKENATHDELEVAAASAcatEFINKLEesyQYNLTQGAT-------NLSGGQKQRVSIARAL 487
Cdd:PRK15134 100 epmvslnplHTLEKQLY--EVLSLHRGMRREAARG---EILNCLD---RVGIRQAAKrltdyphQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALKTKYK--GTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
352-558 |
4.04e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKAllfSGSIEENLR 431
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 432 YGKENATHDELEVAAASACATEFINklEESYQYNLTQGATN-----LSGGQKQRVSIARALVRKPPILILDDSTSAVDAK 506
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPEQREKQII--ETLRQVGLLPDHASyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 507 SEAT-IQTALKTKYKGTTTLLIASKISSIMD--ADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK15112 184 MRSQlINLMLELQEKQGISYIYVTQHLGMMKhiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
336-548 |
9.34e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.58 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 336 EFKNVsysyTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKStlaKLLPRLYDVDQ---GEICIDGIDVKT---YDLQKL- 408
Cdd:PRK09700 267 EVRNV----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKragGEIRLNGKDISPrspLDAVKKg 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 409 -------RASIGFVPQKALLFSGSIEENLRYGKENAT------HDELEVAAASacatefiNKLEESYQYNLTQGATNLSG 475
Cdd:PRK09700 340 mayitesRRDNGFFPNFSIAQNMAISRSLKDGGYKGAmglfheVDEQRTAENQ-------RELLALKCHSVNQNITELSG 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 476 GQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTAL-KTKYKGTTTLLIASKISSIMDA-DKILVLDNGEL 548
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMrQLADDGKVILMVSSELPEIITVcDRIAVFCEGRL 487
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
355-571 |
9.77e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 355 ISFSIQKGEKVGIIGSTGSGKSTL----AKLLPrlydvDQGEICIDGIDVKTYDLQKL---RASigFVPQKALLFSGSIE 427
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLlarmAGLLP-----GSGSIQFAGQPLEAWSAAELarhRAY--LSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLrygkenATHdeLEVAAASACATEFINKLEESYQYN--LTQGATNLSGGQKQRVSIARALVRKPP-------ILILDD 498
Cdd:PRK03695 88 QYL------TLH--QPDKTRTEAVASALNEVAEALGLDdkLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 499 STSAVDAKSEATIQTALKTkykgtttlLIASKISSIM----------DADKILVLDNGELVGNGtheqllERSEVYQEIY 568
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSE--------LCQQGIAVVMsshdlnhtlrHADRVWLLKQGKLLASG------RRDEVLTPEN 225
|
...
gi 1265247244 569 LSQ 571
Cdd:PRK03695 226 LAQ 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
352-550 |
1.15e-12 |
|
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: 70.24 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD--QGEICIDGIDVKTYDLQKL-RASIGFVPQK-ALLFSGSIE 427
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQElTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLRYGKE-----NATHDELEVAAASACATEFinKLEESyqyNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSA 502
Cdd:TIGR02633 97 ENIFLGNEitlpgGRMAYNAMYLRAKNLLREL--QLDAD---NVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1265247244 503 VDAK-SEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:TIGR02633 172 LTEKeTEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVA 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
368-553 |
1.20e-12 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.20 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 368 IGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGFVPQKALLFSG-SIEENLRYgkenatHDELEVAA 446
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILF------YAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 447 ASACATEFINKLEES-YQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALkTKYKGTTTL 525
Cdd:TIGR01257 1035 WEEAQLEMEAMLEDTgLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL-LKYRSGRTI 1113
|
170 180 190
....*....|....*....|....*....|
gi 1265247244 526 LIASKISSIMD--ADKILVLDNGELVGNGT 553
Cdd:TIGR01257 1114 IMSTHHMDEADllGDRIAIISQGRLYCSGT 1143
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-557 |
2.31e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.32 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 355 ISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLrASIGFVP--QKALLF-SGSIEENL- 430
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENLl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 431 ----RYGKENATHDELEVAAASACATEfinKLEESYQY----NLTQ----GATNLSGGQKQRVSIARALVRKPPILILDD 498
Cdd:PRK11300 103 vaqhQQLKTGLFSGLLKTPAFRRAESE---ALDRAATWlervGLLEhanrQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 499 STSAVDAKSEATIQ---TALKTKYkGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:PRK11300 180 PAAGLNPKETKELDeliAELRNEH-NVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-522 |
2.45e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPrlydvdqgeicidGIDvKTYD----LQKlRASIGFVPQKALL----- 421
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KEFEgearPAP-GIKVGYLPQEPQLdpekt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 422 FSGSIEE---------------NLRYGKENATHDEL--EVAA-----ASACATEFINKLEesyqynltQGA--------- 470
Cdd:PRK11819 87 VRENVEEgvaevkaaldrfneiYAAYAEPDADFDALaaEQGElqeiiDAADAWDLDSQLE--------IAMdalrcppwd 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 471 ---TNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKtKYKGT 522
Cdd:PRK11819 159 akvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLH-DYPGT 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
354-513 |
3.48e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 65.60 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIdvktyDLQKLRASigfvPQKALLFSG--------- 424
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-----PIRRQRDE----YHQDLLYLGhqpgiktel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 SIEENLRYgkenathdeleVAAASACATEF--INKLEesyQYNLtQG-----ATNLSGGQKQRVSIARALVRKPPILILD 497
Cdd:PRK13538 90 TALENLRF-----------YQRLHGPGDDEalWEALA---QVGL-AGfedvpVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170
....*....|....*.
gi 1265247244 498 DSTSAVDAKSEATIQT 513
Cdd:PRK13538 155 EPFTAIDKQGVARLEA 170
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
351-548 |
4.09e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.96 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQ---KLRA-SIGFVPQKALLF-SGS 425
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAkHVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 426 IEEN------LRYGKENATHDElevaaasacATEFINKLeeSYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDS 499
Cdd:PRK10584 105 ALENvelpalLRGESSRQSRNG---------AKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 500 TSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMDADKILVLDNGEL 548
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSlnREHGTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
339-538 |
4.15e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 339 NVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTyDLQKLRASIGFVPQK 418
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 419 AllfsgSIEENLRYgKENATHDeLEVAAASACATEFINKLEESYQYNLTQGAtnLSGGQKQRVSIARALVRKPPILILDD 498
Cdd:PRK13540 83 S-----GINPYLTL-RENCLYD-IHFSPGAVGITELCRLFSLEHLIDYPCGL--LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1265247244 499 STSAVDAKSEATIQTALKT-KYKGTTTLLIASKISSIMDAD 538
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
353-557 |
4.47e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 4.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 353 KDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV---KTYDLQKLRASIGFVPQKAL------LFS 423
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPLaslnprMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 GSI-EENLRYGKENATHDEL--EVAAASA---CATEFINKLEESYqynltqgatnlSGGQKQRVSIARALVRKPPILILD 497
Cdd:PRK15079 118 GEIiAEPLRTYHPKLSRQEVkdRVKAMMLkvgLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 498 DSTSAVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQlqREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
335-546 |
6.84e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 64.57 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSY--TKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYD--VDQGEICIDGIDVKtydlQKLRA 410
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 411 SIGFVPQKALLFSGS-IEENLRYgkenathdelevaaaSACATEfinkleesyqynltqgatnLSGGQKQRVSIARALVR 489
Cdd:cd03232 80 STGYVEQQDVHSPNLtVREALRF---------------SALLRG-------------------LSVEQRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 490 KPPILILDDSTSAVDAKSEATIQTAL-KTKYKGTTTLL-IASKISSIMDA-DKILVLDNG 546
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLkKLADSGQAILCtIHQPSASIFEKfDRLLLLKRG 185
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
352-546 |
1.01e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 67.51 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD--QGEICIDGIDVKTYDlqkLRAS----IGFVPQK-ALLFSG 424
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKD---IRDSealgIVIIHQElALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 SIEENLRYGKENATHDELEVAAASACATEFINK--LEESYQynlTQgATNLSGGQKQRVSIARALVRKPPILILDDSTSA 502
Cdd:NF040905 94 SIAENIFLGNERAKRGVIDWNETNRRARELLAKvgLDESPD---TL-VTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1265247244 503 V-DAKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNG 546
Cdd:NF040905 170 LnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDG 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
355-561 |
1.45e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 355 ISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDG--IDVKTyDLQKLRASIGFVP----QKALLFSGSIEE 428
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIRAGIMLCPedrkAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 N---------------LRYGKENAThdelevaaasacATEFINKLEESYQyNLTQGATNLSGGQKQRVSIARALVRKPPI 493
Cdd:PRK11288 351 NinisarrhhlragclINNRWEAEN------------ADRFIRSLNIKTP-SREQLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 494 LILDDSTSAVD--AKSEatIQTALktkYK----GTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERS 561
Cdd:PRK11288 418 ILLDEPTRGIDvgAKHE--IYNVI---YElaaqGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQ 487
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
354-504 |
2.70e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKL---------RASIGFV---PQKALL 421
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVhqhPRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 422 FS----GSIEENL------RYGK--ENATH--DELEVAAASacatefINKLEESYqynltqgatnlSGGQKQRVSIARAL 487
Cdd:PRK11701 104 MQvsagGNIGERLmavgarHYGDirATAGDwlERVEIDAAR------IDDLPTTF-----------SGGMQQRLQIARNL 166
|
170
....*....|....*..
gi 1265247244 488 VRKPPILILDDSTSAVD 504
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLD 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-552 |
2.79e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDlQKLRAS--I 412
Cdd:PRK09700 6 ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQlgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GFVPQK-ALLFSGSIEENLRYGKENATH----DELEVAAASACATEFINKLeeSYQYNLTQGATNLSGGQKQRVSIARAL 487
Cdd:PRK09700 83 GIIYQElSVIDELTVLENLYIGRHLTKKvcgvNIIDWREMRVRAAMMLLRV--GLKVDLDEKVANLSISHKQMLEIAKTL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 488 VRKPPILILDDSTSAV-DAKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNG 552
Cdd:PRK09700 161 MLDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
335-558 |
4.85e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.30 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEicidgidVKTYDlqklRASIGF 414
Cdd:PRK15064 320 LEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-------VKWSE----NANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQ-KALLFSGsiEENL-----RYGKENatHDELEVAAAsacatefINKLEESyQYNLTQGATNLSGGQKQRVSIARALV 488
Cdd:PRK15064 387 YAQdHAYDFEN--DLTLfdwmsQWRQEG--DDEQAVRGT-------LGRLLFS-QDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 489 RKPPILILDDSTSAVDAKSEATIQTALKtKYKGttTLLIASK----ISSImdADKILVLDNGELVG-NGTHEQLL 558
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALE-KYEG--TLIFVSHdrefVSSL--ATRIIEITPDGVVDfSGTYEEYL 524
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
349-549 |
5.46e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 5.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 349 EYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtydlqklrasigFVPQKALLfsgsieE 428
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ------------FGREASLI------D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLryGKENATHDELEVAAAS--ACATEFINKLEEsyqynltqgatnLSGGQKQRVSIARALVRKPPILILDDSTSAVDAk 506
Cdd:COG2401 105 AI--GRKGDFKDAVELLNAVglSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR- 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 507 seatiQTALKTKYK-------GTTTLLIASKISSIMDA---DKILVLDNGELV 549
Cdd:COG2401 170 -----QTAKRVARNlqklarrAGITLVVATHHYDVIDDlqpDLLIFVGYGGVP 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
367-504 |
9.78e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 9.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 367 IIGSTGSGKSTLAKLLPRLYDVDQGEICIDG---IDV-KTYDLQKLRASIGFVPQKALLFSG-SIEENLRYG---KENAT 438
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLFPHyKVRGNLRYGmakSMVAQ 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 439 HDELeVAAASacatefINKLEESYqynltqgATNLSGGQKQRVSIARALVRKPPILILDDSTSAVD 504
Cdd:PRK11144 109 FDKI-VALLG------IEPLLDRY-------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
352-506 |
1.47e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKtydLQKLRASIG-----------FVPQKal 420
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR---FASTTAALAagvaiiyqelhLVPEM-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 421 lfsgSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGatNLSGGQKQRVSIARALVRKPPILILDDST 500
Cdd:PRK11288 95 ----TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLK--YLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
....*.
gi 1265247244 501 SAVDAK 506
Cdd:PRK11288 169 SSLSAR 174
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-566 |
1.55e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 63.66 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLA-KLLPRLYDVD-QGEICIDG--IDVKTYDlQKLRASIGFV----PQKALLF 422
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRNiSGTVFKDGkeVDVSTVS-DAIDAGLAYVtedrKGYGLNL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 423 SGSIEENL---------RYGKENAtHDELEVAaasacatefinkleESYQYNL-------TQGATNLSGGQKQRVSIARA 486
Cdd:NF040905 354 IDDIKRNItlanlgkvsRRGVIDE-NEEIKVA--------------EEYRKKMniktpsvFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 487 LVRKPPILILDDSTSAVD--AKSEA-TIQTALKTKYKGttTLLIASKISSIMD-ADKILVLDNGELVGNgtheqlLERSE 562
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDvgAKYEIyTIINELAAEGKG--VIVISSELPELLGmCDRIYVMNEGRITGE------LPREE 490
|
....
gi 1265247244 563 VYQE 566
Cdd:NF040905 491 ASQE 494
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
354-504 |
1.63e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQkLRASIGFVPQKallFS--G--SIEEN 429
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA-TRRRVGYMSQA---FSlyGelTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 430 LrygkenATHDEL-EVAAASAcaTEFINKLEEsyQYNLTQGATNLSG----GQKQRVSIARALVRKPPILILDDSTSAVD 504
Cdd:NF033858 360 L------ELHARLfHLPAAEI--AARVAEMLE--RFDLADVADALPDslplGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-504 |
1.71e-10 |
|
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: 61.66 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 358 SIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVkTYDLQKLRASigfvpqkallFSGSIEENLRYGKENA 437
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKAD----------YEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 438 THDelevaaaSACATEFIN--KLEESYQYNLtqgaTNLSGGQKQRVSIARALVRKPPILILDDSTSAVD 504
Cdd:cd03237 90 YTH-------PYFKTEIAKplQIEQILDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
15-309 |
1.92e-10 |
|
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: 62.05 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 15 MFFAIIGPLFmvlEVAMDLIQPTIMQHIIDVGIANRDL---NYVIKMGLLMIGAAALGLVGGLGCMMYST----KAAVNF 87
Cdd:cd18554 1 IIITIVIGLV---RFGIPLLLPLILKYIVDDVIQGSSLtldEKVYKLFTIIGIMFFIFLILRPPVEYYRQyfaqWIANKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 88 ATDIRKDVFAKIETFS----SNNRdsfgTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPILL 163
Cdd:cd18554 78 LYDIRKDLFDHLQKLSlryyANNR----SGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 164 VVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMM 243
Cdd:cd18554 154 VIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTF 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 244 PIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18554 234 SAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
354-557 |
2.55e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.05 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 354 DISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVD---QGEICIDG---IDVKTYDLQKLRASigfvpQKALLFSG--- 424
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGreiLNLPEKELNKLRAE-----QISMIFQDpmt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 425 SIEENLRYGKENAT----HDELEVAAASACATEFIN--KLEESYQyNLTQGATNLSGGQKQRVSIARALVRKPPILILDD 498
Cdd:PRK09473 109 SLNPYMRVGEQLMEvlmlHKGMSKAEAFEESVRMLDavKMPEARK-RMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1265247244 499 STSAVDAKSEATIQT---ALKTKYkGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:PRK09473 188 PTTALDVTVQAQIMTllnELKREF-NTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
335-547 |
2.61e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 63.26 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtknNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEIcIDGIDVkTYDLQKLRASigf 414
Cdd:COG1245 342 VEYPDLTKSY---GGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKI-SYKPQYISPD--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 vpqkallFSGSIEENLRygkeNATHDELEvaaASACATEFINKL--EESYQYNLtqgaTNLSGGQKQRVSIARALVRKPP 492
Cdd:COG1245 414 -------YDGTVEEFLR----SANTDDFG---SSYYKTEIIKPLglEKLLDKNV----KDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSI-MDADKILVLDnGE 547
Cdd:COG1245 476 LYLLDEPSAHLDVEQRLAVAKAIRrfAENRGKTAMVVDHDIYLIdYISDRLMVFE-GE 532
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
343-504 |
3.04e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 343 SYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPqkALLF 422
Cdd:PRK13543 18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP--GLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 423 SGSIEENLRYgkENATHD-ELEVAAASACATEFINKLEESYqynltqgATNLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:PRK13543 96 DLSTLENLHF--LCGLHGrRAKQMPGSALAIVGLAGYEDTL-------VRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
...
gi 1265247244 502 AVD 504
Cdd:PRK13543 167 NLD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
336-529 |
4.59e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 336 EFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEI-CIDGIDVKTYDlqKLRASIGf 414
Cdd:PRK11147 321 EMENVNYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhCGTKLEVAYFD--QHRAELD- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 vPQKallfsgSIEENLRYGKEnathdELEVAAASACATEFINKLEESYQYNLTQgATNLSGGQKQRVSIARALVRKPPIL 494
Cdd:PRK11147 396 -PEK------TVMDNLAEGKQ-----EVMVNGRPRHVLGYLQDFLFHPKRAMTP-VKALSGGERNRLLLARLFLKPSNLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265247244 495 ILDDSTSAVDakseatIQT-----ALKTKYKGttTLLIAS 529
Cdd:PRK11147 463 ILDEPTNDLD------VETlelleELLDSYQG--TVLLVS 494
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
335-547 |
4.73e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 4.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtknNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEIcidGIDVK-TYDLQKLRASig 413
Cdd:PRK13409 341 VEYPDLTKKL---GDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKiSYKPQYIKPD-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 fvpqkallFSGSIEENLRYGKENathdelevAAASACATEFINKL--EESYQYNLtqgaTNLSGGQKQRVSIARALVRKP 491
Cdd:PRK13409 413 --------YDGTVEDLLRSITDD--------LGSSYYKSEIIKPLqlERLLDKNV----KDLSGGELQRVAIAACLSRDA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 492 PILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSI-MDADKILVLDnGE 547
Cdd:PRK13409 473 DLYLLDEPSAHLDVEQRLAVAKAIRriAEEREATALVVDHDIYMIdYISDRLMVFE-GE 530
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
185-309 |
4.88e-10 |
|
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: 60.92 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 185 KKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATLWIGGEK 264
Cdd:cd18570 170 REVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYL 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1265247244 265 VFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18570 250 VIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
353-560 |
5.40e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.10 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 353 KDISFSIQKGEKVGIIGSTGSGKS----TLAKLLPRLYDVDQGEICIDGIDVKTYDLQ-KLRASIGFVPQKAL-----LF 422
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRgRKIATIMQNPRSAFnplhtMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 423 SGSIEENLRYGKENAthDELEVAAASACATEFINKLEESYQYNLtqgatnlSGGQKQRVSIARALVRKPPILILDDSTSA 502
Cdd:PRK10418 100 THARETCLALGKPAD--DATLTAALEAVGLENAARVLKLYPFEM-------SGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 503 VDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLER 560
Cdd:PRK10418 171 LDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
351-553 |
6.29e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLL---------PRLYDVdQGEICIDGIDVKTYD---LQKLRASIGFVPQK 418
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggaPRGARV-TGDVTLNGEPLAAIDaprLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 419 ALLFsgSIEE--------NLRYGKENATHD------ELEVAAASACAtefinkleesyqynlTQGATNLSGGQKQRVSIA 484
Cdd:PRK13547 95 AFAF--SAREivllgrypHARRAGALTHRDgeiawqALALAGATALV---------------GRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 485 RAL---------VRKPPILILDDSTSAVDAKSE----ATIQTALKTKYKGTTTLLIASKISSiMDADKILVLDNGELVGN 551
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAH 236
|
..
gi 1265247244 552 GT 553
Cdd:PRK13547 237 GA 238
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
347-560 |
7.12e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 7.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 347 NNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLL---PRlYDVDQGEICIDGIDVKTYDLQKlRASIGFVpqkaLLFS 423
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghPA-YKILEGDILFKGESILDLEPEE-RAHLGIF----LAFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 GSIE-------ENLR--YgkeNATHDELEVAAASACA-TEFIN------KLEESY-QYNLTQGatnLSGGQKQRVSIARA 486
Cdd:CHL00131 92 YPIEipgvsnaDFLRlaY---NSKRKFQGLPELDPLEfLEIINeklklvGMDPSFlSRNVNEG---FSGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 487 LVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD---ADKILVLDNGELVGNGTHE--QLLER 560
Cdd:CHL00131 166 ALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDyikPDYVHVMQNGKIIKTGDAElaKELEK 244
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
335-516 |
2.54e-09 |
|
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: 60.15 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSyTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklRASIGF 414
Cdd:TIGR00954 452 IKFENIPLV-TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFY 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQKALLFSGSIEENLRYG------KENATHDELEVAAASACATEFInkLEESYQYNLTQGATN-LSGGQKQRVSIARAL 487
Cdd:TIGR00954 520 VPQRPYMTLGTLRDQIIYPdssedmKRRGLSDKDLEQILDNVQLTHI--LEREGGWSAVQDWMDvLSGGEKQRIAMARLF 597
|
170 180
....*....|....*....|....*....
gi 1265247244 488 VRKPPILILDDSTSAVDAKSEATIQTALK 516
Cdd:TIGR00954 598 YHKPQFAILDECTSAVSVDVEGYMYRLCR 626
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
341-562 |
2.87e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 341 SYSYTKnneyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGiDVKTYDLQK--LRASIG----F 414
Cdd:PRK11147 12 SFSDAP----LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVARLQQdpPRNVEGtvydF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VpqkallfSGSIEENLRYGKEnatHDELEVAAASACATEFINKL---------------EESYQYNLTQ-------GATN 472
Cdd:PRK11147 87 V-------AEGIEEQAEYLKR---YHDISHLVETDPSEKNLNELaklqeqldhhnlwqlENRINEVLAQlgldpdaALSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 473 LSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTkYKGtTTLLIA---SKISSImdADKILVLDNGELV 549
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQG-SIIFIShdrSFIRNM--ATRIVDLDRGKLV 232
|
250
....*....|....
gi 1265247244 550 G-NGTHEQLLERSE 562
Cdd:PRK11147 233 SyPGNYDQYLLEKE 246
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
335-504 |
5.22e-09 |
|
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: 58.79 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIdGIDVKtydlqklrasIGF 414
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 415 VPQ--KALLFSGSIEENLRYGkenatHDELEVAAASACATEFINkleesyQYNLTQG-----ATNLSGGQKQRVSIARAL 487
Cdd:TIGR03719 390 VDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPSRAYVG------RFNFKGSdqqkkVGQLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 1265247244 488 VRKPPILILDDSTSAVD 504
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
335-562 |
6.93e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.08 E-value: 6.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYsyTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKL---RAS 411
Cdd:PRK11831 8 VDMRGVSF--TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 412 IGFVPQKALLFSG-SIEENLRYGKENATHdelevAAASACATEFINKLEESYqynlTQGATN-----LSGGQKQRVSIAR 485
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPLREHTQ-----LPAPLLHSTVMMKLEAVG----LRGAAKlmpseLSGGMARRAALAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 486 ALVRKPPILILDDS-------TSAVDAKSEATIQTALktkykGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:PRK11831 157 AIALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSAL-----GVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
....*
gi 1265247244 558 LERSE 562
Cdd:PRK11831 232 QANPD 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
356-576 |
1.02e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 356 SFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICID---GIDVKTYDLQKLRASIGFVPQKALLFSGsiEENlrY 432
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshITRLSFEQLQKLVSDEWQRNNTDMLSPG--EDD--T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 433 GKENATHDELEVAAASAC---ATEF-INKLeesyqynLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSE 508
Cdd:PRK10938 99 GRTTAEIIQDEVKDPARCeqlAQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 509 ATIQTALKT-KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLLERSEVYQEIYLSQGGNLH 576
Cdd:PRK10938 172 QQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQALVAQLAHSEQLEGVQ 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
328-564 |
1.23e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 328 PEKI----EGNIEFKNVsysyTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTY 403
Cdd:PRK10982 240 PDKEnkpgEVILEVRNL----TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNH 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 404 DLQKL-----------RASIGFVPQKALLFSGSIEENLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTqgatN 472
Cdd:PRK10982 316 NANEAinhgfalvteeRRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQIG----S 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 473 LSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATI-QTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAG 471
|
250
....*....|....*....
gi 1265247244 551 -----NGTHEQLLERSEVY 564
Cdd:PRK10982 472 ivdtkTTTQNEILRLASLH 490
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
355-558 |
2.55e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.96 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 355 ISFSIQKGEKVGIIGSTGSGKSTLAKLLPRL----YDVDQGEICIDGIDVKTYDLQKLRASIGF-------VPQKALLFS 423
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGHnvsmifqEPQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 424 GSIEENLRYGKENATHDE---LEVAAASACATEFINK--------LEESYQYNLTQGatnlsggQKQRVSIARALVRKPP 492
Cdd:PRK15093 106 ERVGRQLMQNIPGWTYKGrwwQRFGWRKRRAIELLHRvgikdhkdAMRSFPYELTEG-------ECQKVMIAIALANQPR 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 493 ILILDDSTSAVDAKSEATIQTALK--TKYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQLL 558
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTrlNQNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
351-546 |
4.45e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.04 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLP-RLYDVD-QGEICIDGIDVKTYDLQKlrasIGFVPQKALLFSG-SIE 427
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILKR----TGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLRYGK-----ENATHDELEVAAASACATEFINKLEESYQYN-LTQGatnLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:PLN03211 159 ETLVFCSllrlpKSLTKQEKILVAESVISELGLTKCENTIIGNsFIRG---ISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1265247244 502 AVDAKSE-ATIQTALKTKYKGTTTLLIASKISSIMDA--DKILVLDNG 546
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEG 283
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
355-557 |
8.56e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 355 ISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVdQGEICIDGIDVKTYDLQKL-----RASIGfvPQKALLFSGSIEE- 428
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGQDLQRIsekerRNLVG--AEVAMIFQDPMTSl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 429 NLRYGKENATHDELEVAAASACATEFINKLEESYQYNLTQGAT-------NLSGGQKQRVSIARALVRKPPILILDDSTS 501
Cdd:PRK11022 103 NPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASrldvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 502 AVDAKSEATIQTALKT--KYKGTTTLLIASKISSIMD-ADKILVLDNGELVGNGTHEQL 557
Cdd:PRK11022 183 ALDVTIQAQIIELLLElqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
335-504 |
1.46e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.75 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNneYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDV-KTYDLQKLRASIG 413
Cdd:NF033858 2 ARLEGVSHRYGKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMaDARHRRAVCPRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 414 FVPQ---KALLFSGSIEENLR-----YGkenatHDELEVAAAsacatefINKLEESyqynlTqG--------ATNLSGGQ 477
Cdd:NF033858 80 YMPQglgKNLYPTLSVFENLDffgrlFG-----QDAAERRRR-------IDELLRA-----T-GlapfadrpAGKLSGGM 141
|
170 180
....*....|....*....|....*..
gi 1265247244 478 KQRVSIARALVRKPPILILDDSTSAVD 504
Cdd:NF033858 142 KQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
24-309 |
2.04e-07 |
|
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: 52.70 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 24 FMVLEVAMDLIQPTIMQHIIDvGIA-NRDL----NYVIKMGLLMIGAA-ALGLVGGLgcmmySTKAAVNFATDIRKDVFA 97
Cdd:cd18784 4 FLLAAAVGEIFIPYYTGQVID-GIViEKSQdkfsRAIIIMGLLAIASSvAAGIRGGL-----FTLAMARLNIRIRNLLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 98 KIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELfpillVVVPILLLAIILIA 177
Cdd:cd18784 78 SIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQL-----SLVTLIGLPLIAIV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 178 SKASGTF-----KKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSG 252
Cdd:cd18784 153 SKVYGDYykklsKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1265247244 253 GIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18784 233 LTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
23-309 |
4.73e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 51.72 E-value: 4.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 23 LFMVLEVAMDLIQPTIMQHIIDV--GIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAKIE 100
Cdd:cd18579 4 LLKLLEDLLSLAQPLLLGLLISYlsSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 101 TFSSNNRDSFGTGKLLTIVTNDITSIQSAMtMTLRVLVRGPLL----------------FMGSIIIVFVTArelfpillv 164
Cdd:cd18579 84 RLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQiivalyllyrllgwaaLAGLGVLLLLIP--------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 165 vvpilllAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAY------------VRQKyEIAQfgsvntnLTKIN 232
Cdd:cd18579 154 -------LQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYawekpflkrieeLRKK-ELKA-------LRKFG 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1265247244 233 -IRAVQL-ISLMMPIIMLVVSggIVATLWIGgekvfnGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18579 219 yLRALNSfLFFSTPVLVSLAT--FATYVLLG------NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
304-507 |
5.15e-07 |
|
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: 53.09 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 304 PSADRVQQVLNTEVDIISAANAIEPEKIEgniEFKNVsysYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLP 383
Cdd:TIGR01257 1913 PIFDEDDDVAEERQRIISGGNKTDILRLN---ELTKV---YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLT 1986
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 384 RLYDVDQGEICIDGIDVKTyDLQKLRASIGFVPQ-KAL--LFSGSIEENLRYGKENATHDELEVAA----ASACATEFIN 456
Cdd:TIGR01257 1987 GDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfDAIddLLTGREHLYLYARLRGVPAEEIEKVAnwsiQSLGLSLYAD 2065
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1265247244 457 KLEESYqynltqgatnlSGGQKQRVSIARALVRKPPILILDDSTSAVDAKS 507
Cdd:TIGR01257 2066 RLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
351-546 |
5.24e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 351 VLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRlyDVDQGEICIDGidVKTYDlqklraSIG---FVPQKallfsgsiE 427
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEG--VITYD------GITpeeIKKHY--------R 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLRYGKENATH-------DELEVAAAsaCAT-----------EFINKLEE--------SYQYNLTQG---ATNLSGGQK 478
Cdd:TIGR00956 138 GDVVYNAETDVHfphltvgETLDFAAR--CKTpqnrpdgvsreEYAKHIADvymatyglSHTRNTKVGndfVRGVSGGER 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1265247244 479 QRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTkykgTTTLLIASKISSIMDA--------DKILVLDNG 546
Cdd:TIGR00956 216 KRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKT----SANILDTTPLVAIYQCsqdayelfDKVIVLYEG 287
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
335-395 |
5.47e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 5.47e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 335 IEFKNVSYSYtknNEYVL-KDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICI 395
Cdd:PRK11819 325 IEAENLSKSF---GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
361-547 |
7.13e-07 |
|
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: 48.91 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 361 KGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTYDLQKLRASIGFVPQKAllfsgsieenlrygkenathd 440
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKA--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 441 elevaaasacatefinkleesyqynltqgatNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQ-------T 513
Cdd:smart00382 60 -------------------------------SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlL 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1265247244 514 ALKTKYKGTTTLLIASKISSIMDA------DKILVLDNGE 547
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLIL 148
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
352-550 |
9.36e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 9.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 352 LKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGIDVKTY---DLQKlrASIGFVPQKA-LLFSGSIE 427
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpkSSQE--AGIGIIHQELnLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 428 ENLRYGKENATH----DELEVAAAsacATEFINKLeeSYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAV 503
Cdd:PRK10762 98 ENIFLGREFVNRfgriDWKKMYAE---ADKLLARL--NLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1265247244 504 -DAKSEATIQTALKTKYKGTTTLLIASKISSIMD-ADKILVLDNGELVG 550
Cdd:PRK10762 173 tDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFIA 221
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
335-560 |
3.67e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.63 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYTKNNeyVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLP--RLYDVDQGEICIDGIDVKTYDLQKlRASI 412
Cdd:PRK09580 2 LSIKDLHVSVEDKA--ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 413 GF---------VP--QKALLFSGSIEENLRYgKENATHDELEVAAASACATEFINKLEESYQYNLTQGatnLSGGQKQRV 481
Cdd:PRK09580 79 GIfmafqypveIPgvSNQFFLQTALNAVRSY-RGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG---FSGGEKKRN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 482 SIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD---ADKILVLDNGELVGNGTH---E 555
Cdd:PRK09580 155 DILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDFtlvK 234
|
....*
gi 1265247244 556 QLLER 560
Cdd:PRK09580 235 QLEEQ 239
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
350-534 |
5.59e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 5.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 350 YVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEICIDGidvktydlqklrasigfvpQKALLFSGSIEEN 429
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------------------SAALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 430 LRYGKENATHDELEVAAASACATEFINKLEESYQYN--LTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAK- 506
Cdd:PRK13545 99 QLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGkfIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTf 178
|
170 180
....*....|....*....|....*...
gi 1265247244 507 SEATIQTALKTKYKGTTTLLIASKISSI 534
Cdd:PRK13545 179 TKKCLDKMNEFKEQGKTIFFISHSLSQV 206
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
316-504 |
1.66e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 316 EVDIISAANAIEPEkiEGNIEFKNVSYSYtkNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLL----PRLYDVD-- 389
Cdd:PRK10938 244 EPDEPSARHALPAN--EPRIVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhPQGYSNDlt 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 390 -------QGEICIDgidvktydlqkLRASIGFVPQ------------KALLFSG---SIeenlryGKENATHDELEVAAA 447
Cdd:PRK10938 320 lfgrrrgSGETIWD-----------IKKHIGYVSSslhldyrvstsvRNVILSGffdSI------GIYQAVSDRQQKLAQ 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1265247244 448 sacatEFINKLeesyqyNLTQGATN-----LSGGQKQRVSIARALVRKPPILILDDSTSAVD 504
Cdd:PRK10938 383 -----QWLDIL------GIDKRTADapfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
362-506 |
2.28e-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: 46.21 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 362 GEKVGIIGSTGSGKSTLAKLL-----PRLYDVDqGEICIDGIdVKTY---DLQ---------KLRASIG--FVPQKALLF 422
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILagklkPNLGKFD-DPPDWDEI-LDEFrgsELQnyftkllegDVKVIVKpqYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 423 SGSIEENLRYGKENATHDELevaaasacatefINKLEesYQYNLTQGATNLSGGQKQRVSIARALVRKPPILILDDSTSA 502
Cdd:cd03236 104 KGKVGELLKKKDERGKLDEL------------VDQLE--LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
....
gi 1265247244 503 VDAK 506
Cdd:cd03236 170 LDIK 173
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
463-557 |
2.38e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 463 QYNLTQGA----TNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALKTKYKGTTTLLIASKISSIMD-- 536
Cdd:NF000106 131 RFSLTEAAgraaAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEql 210
|
90 100
....*....|....*....|.
gi 1265247244 537 ADKILVLDNGELVGNGTHEQL 557
Cdd:NF000106 211 AHELTVIDRGRVIADGKVDEL 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
335-512 |
2.69e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 335 IEFKNVSYSYtKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLLPRLYDVDQGEIC--------------IDGIDV 400
Cdd:PLN03073 509 ISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 401 KTYDL------------QKLRASIGfvpqkallfSGSIEENLrygkenathdelevaaasacatefinKLEESYqynltq 468
Cdd:PLN03073 588 SSNPLlymmrcfpgvpeQKLRAHLG---------SFGVTGNL--------------------------ALQPMY------ 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1265247244 469 gatNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKS-EATIQ 512
Cdd:PLN03073 627 ---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
52-319 |
6.10e-05 |
|
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: 45.14 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 52 LNYVIKMGLLMIGAAALGLVGGLGCMMYSTKAAVNFATDIRKDVFAKI-----ETFssnNRDSFGTGKLLTIVTNDITSI 126
Cdd:cd18578 48 RSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAIlrqdiAWF---DDPENSTGALTSRLSTDASDV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 127 QSAMTMTLRVLVRGPLLFMGSIIIVFVTAREL---------FpillvvvpilLLAIILIASKASGTF-KKVQEALDKVNT 196
Cdd:cd18578 125 RGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLalvglatvpL----------LLLAGYLRMRLLSGFeEKNKKAYEESSK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 197 KLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAIL 276
Cdd:cd18578 195 IASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFF 274
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1265247244 277 -AFinylNIILMSLMSISMVFI---QIARAFPSADRVQQVLNTEVDI 319
Cdd:cd18578 275 iVF----MALIFGAQSAGQAFSfapDIAKAKAAAARIFRLLDRKPEI 317
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
320-516 |
1.60e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 320 ISAANAIEPEK------IEGNIEFKNVSY-----------SYTKNNEYVLKDISFSIQKGEKVGIIGSTGSGKSTLAKLL 382
Cdd:PLN03140 847 LEAANGVAPKRgmvlpfTPLAMSFDDVNYfvdmpaemkeqGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVL 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 383 P--RLYDVDQGEICIDGIDVKtydlQKLRASI-GFVPQ-----------KALLFSGSieenLRYGKENATHDELEvaaas 448
Cdd:PLN03140 927 AgrKTGGYIEGDIRISGFPKK----QETFARIsGYCEQndihspqvtvrESLIYSAF----LRLPKEVSKEEKMM----- 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1265247244 449 acateFINKLEESYQY-NLTQ------GATNLSGGQKQRVSIARALVRKPPILILDDSTSAVDAKSEATIQTALK 516
Cdd:PLN03140 994 -----FVDEVMELVELdNLKDaivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVR 1063
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
466-557 |
7.98e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 466 LTQGATNLSGGQKQRVSIARALVRK---PPILILDDSTSAV---DAKSEATIQTALKTkyKGTTTLLIASKISSIMDADK 539
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVD--KGNTVVVIEHNLDVIKTADY 900
|
90 100
....*....|....*....|....
gi 1265247244 540 ILVL------DNGELVGNGTHEQL 557
Cdd:TIGR00630 901 IIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
47-281 |
1.00e-03 |
|
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: 41.30 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 47 IANRD-----LNYVIKMGLLMIGAAALGLVGGlgCMMYSTKAAVNfaTDIRKDVFA-----KIETFSSNnrdsfGTGKLL 116
Cdd:cd18589 26 IMNKDapeafTAAITVMSLLTIASAVSEFVCD--LIYNITMSRIH--SRLQGLVFAavlrqEIAFFDSN-----QTGDIV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 117 TIVTNDIT----SIQSAMTMTLRVLVRGPLLF----MGSIIIVFVTARELfpillvvvpilllAIILIASKASGTF---- 184
Cdd:cd18589 97 SRVTTDTEdmseSLSENLSLLMWYLARGLFLFifmlWLSPKLALLTALGL-------------PLLLLVPKFVGKFqqsl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 185 -KKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIR-----AVQLISLMMPIIMLVVsgGIvatL 258
Cdd:cd18589 164 aVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKeaaayAVSMWTSSFSGLALKV--GI---L 238
|
250 260
....*....|....*....|...
gi 1265247244 259 WIGGEKVFNGTLRVGAILAFINY 281
Cdd:cd18589 239 YYGGQLVTAGTVSSGDLVTFVLY 261
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
86-309 |
1.07e-03 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 41.38 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 86 NFATDIRKDVFAKIE----TFSSNNRdsfgTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPI 161
Cdd:cd18574 72 RVAARLRNDLFSSLLrqdiAFFDTHR----TGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 162 LLVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISL 241
Cdd:cd18574 148 LLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGI 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1265247244 242 MMPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAILAFINYLNIILMSLMSISMVFIQIARAFPSADRV 309
Cdd:cd18574 228 FQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
198-278 |
1.49e-03 |
|
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: 40.95 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 198 LQENLSGVRVIKA-----YVRQKYE--IAQFGSVNTNLTKINIRAVQLISLMMPIIMLVVsggivatLWIGGEKVFNGTL 270
Cdd:cd18588 183 LVETVTGIETVKSlavepQFQRRWEelLARYVKASFKTANLSNLASQIVQLIQKLTTLAI-------LWFGAYLVMDGEL 255
|
....*...
gi 1265247244 271 RVGAILAF 278
Cdd:cd18588 256 TIGQLIAF 263
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
189-278 |
2.18e-03 |
|
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: 40.26 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 189 EALDKVNTKLQENLSGVRVIKA-----YVRQKYEIAQFGSVNTN--LTKINIRAVQLISLMMPIIMlvvsggiVATLWIG 261
Cdd:cd18566 174 RADERRQNFLIETLTGIHTIKAmamepQMLRRYERLQANAAYAGfkVAKINAVAQTLGQLFSQVSM-------VAVVAFG 246
|
90
....*....|....*..
gi 1265247244 262 GEKVFNGTLRVGAILAF 278
Cdd:cd18566 247 ALLVINGDLTVGALIAC 263
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
16-276 |
3.20e-03 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 39.95 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 16 FFAIIG----PLFMVL---------EVAMDLIQPTIMQHIIDVGIANRDLNYVIKMGLLMIGAAALGLVGGLGCMMYSTK 82
Cdd:cd18558 6 LCAIIHggllPAFMVIfgdmtdsftNGGMTNITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 83 AAVNFATDIRKDVFAKIETFSSNNRDSFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSIIIVFVTARELFPIL 162
Cdd:cd18558 86 AAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 163 LVVVPILLLAIILIASKASGTFKKVQEALDKVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRAVQLISLM 242
Cdd:cd18558 166 LAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNIS 245
|
250 260 270
....*....|....*....|....*....|....
gi 1265247244 243 MPIIMLVVSGGIVATLWIGGEKVFNGTLRVGAIL 276
Cdd:cd18558 246 MGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVL 279
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
13-299 |
3.23e-03 |
|
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: 39.80 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 13 PYMFFAIIgpLFMVLEVAMDLIQPTIMQHIIDVGIANRDLNYvikmgLLMIGAAALGLVGGLGCMMY-----STKAAVNF 87
Cdd:cd18555 1 KKLLISIL--LLSLLLQLLTLLIPILTQYVIDNVIVPGNLNL-----LNVLGIGILILFLLYGLFSFlrgyiIIKLQTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 88 ATDIRKDVFAK-----------------IETFSSNN--RDsFGTGKLLTIVTNDITSIQSAMTMTLRVLVRGPLLFMGSI 148
Cdd:cd18555 74 DKSLMSDFFEHllklpysffenrssgdlLFRANSNVyiRQ-ILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 149 IIVFVTareLFpillvvvpilllaiiliaskasgTFKKVQEALDK---VNTKLQ----ENLSGVRVIKA----------- 210
Cdd:cd18555 153 LIVLLL---LL-----------------------TRKKIKKLNQEeivAQTKVQsyltETLYGIETIKSlgsekniykkw 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 211 ---YVRQKYEIAQFGSVNTNLTKINiravQLISLMMPIIMLvvsggivatlWIGGEKVFNGTLRVGAILAFINYLNIILM 287
Cdd:cd18555 207 enlFKKQLKAFKKKERLSNILNSIS----SSIQFIAPLLIL----------WIGAYLVINGELTLGELIAFSSLAGSFLT 272
|
330
....*....|..
gi 1265247244 288 SLMSISMVFIQI 299
Cdd:cd18555 273 PIVSLINSYNQF 284
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
345-553 |
3.34e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.52 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 345 TKNNeyvLKDISFSIQKGEKVGIIGSTGSGKSTL---------------AKLLPRLYDVDQGEICIDGIDVKTYDLqklr 409
Cdd:cd03271 7 RENN---LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlypalarrlhlKKEQPGNHDRIEGLEHIDKVIVIDQSP---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 410 asIGFVPQ-------KAL-----LFSGSI------EENL--RYgKENATHDELEVAAASAcaTEFI-------NKLEESY 462
Cdd:cd03271 80 --IGRTPRsnpatytGVFdeireLFCEVCkgkrynRETLevRY-KGKSIADVLDMTVEEA--LEFFenipkiaRKLQTLC 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 463 Q----Y-NLTQGATNLSGGQKQRVSIARALVRKPP---ILILDDSTSAVDAKSEATIQTALKT-KYKGTTTLLIASKISS 533
Cdd:cd03271 155 DvglgYiKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDV 234
|
250 260
....*....|....*....|....*.
gi 1265247244 534 IMDADKILVL------DNGELVGNGT 553
Cdd:cd03271 235 IKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
193-281 |
3.46e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 39.75 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1265247244 193 KVNTKLQENLSGVRVIKAYVRQKYEIAQFGSVNTNLTKINIRaVQLISLMMPIIMLVVSG-GIVATLWIGGEKVFNGTLR 271
Cdd:cd18567 178 KEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIR-LQRLQILFSAANGLLFGlENILVIYLGALLVLDGEFT 256
|
90
....*....|
gi 1265247244 272 VGAILAFINY 281
Cdd:cd18567 257 VGMLFAFLAY 266
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
364-387 |
8.99e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 37.39 E-value: 8.99e-03
|
| |
