|
Name |
Accession |
Description |
Interval |
E-value |
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1-593 |
0e+00 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 1006.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 1 MRKSRHHQDNTPVEFSWRSVKSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDSLEqvnDGLTSIIAVPVTLV 80
Cdd:COG5265 5 RAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALL---SGAAALLVVPVGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 81 LLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIVP 160
Cdd:COG5265 82 LAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 161 TLLEILFVVAIFFHQYGLNFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYES 240
Cdd:COG5265 162 TLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 241 QRYDEELALWETARRKNRLTLFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYRE 320
Cdd:COG5265 242 RRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 321 IKGSLANIEKMFELLERVPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLV 400
Cdd:COG5265 322 IRQALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 401 KLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLP 480
Cdd:COG5265 402 RLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 481 KKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADK 560
Cdd:COG5265 482 DGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADE 561
|
570 580 590
....*....|....*....|....*....|...
gi 2261045687 561 IIVMHQGEIVETGNHQQLLLANGRYAKMWAMQQ 593
Cdd:COG5265 562 ILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-593 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 580.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 14 EFSWRSVKSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDSLeqVNDGLTSIIAvpvTLVLLYGLLRFFNVIL 93
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL--LAGGDLSALL---LLLLLLLGLALLRALL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 94 GEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIVPTLLEILFVVAIFF 173
Cdd:COG1132 78 SYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 174 HQYGLnFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETA 253
Cdd:COG1132 158 VIDWR-LALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 254 RRKNRLTLFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKMFE 333
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 334 LLERVPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGS 413
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 414 IEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLK 493
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 494 LSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETG 573
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|
gi 2261045687 574 NHQQLLLANGRYAKMWAMQQ 593
Cdd:COG1132 557 THEELLARGGLYARLYRLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-593 |
3.87e-156 |
|
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: 464.69 E-value: 3.87e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 18 RSVKSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDSLeQVNDGLTSIIavpvTLVLLYGLLRFFNVILGEIR 97
Cdd:COG2274 142 FGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRV-LPNQDLSTLW----VLAIGLLLALLFEGLLRLLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 98 DTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLS---RDMERgtsgI-SFLMRFMVFNIVPTLLEILFVVAIFF 173
Cdd:COG2274 217 SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLAsrfRDVES----IrEFLTGSLLTALLDLLFVLIFLIVLFF 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 174 hqYGLNFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETA 253
Cdd:COG2274 293 --YSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 254 RRKNRLTLFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKMFE 333
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 334 LLERVPKVTDKKQAKELNIGDGTISFKDVRFEYDP-SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSG 412
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 413 SIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGL 492
Cdd:COG2274 531 RILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 493 KLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVET 572
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570 580
....*....|....*....|.
gi 2261045687 573 GNHQQLLLANGRYAKMWAMQQ 593
Cdd:COG2274 691 GTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
37-331 |
5.85e-151 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 435.77 E-value: 5.85e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSLeqvNDGLTSIIAVPVTLVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKL 116
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDAL---SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 117 FDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIVPTLLEILFVVAIFFHQYGLNFALITLGSIVLYIGFTA 196
Cdd:cd18582 78 FRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYVAFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 197 YATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGLNSGQALIIASAM 276
Cdd:cd18582 158 KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 277 TSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKM 331
Cdd:cd18582 238 TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
357-592 |
1.01e-139 |
|
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: 405.08 E-value: 1.01e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIV 436
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILI 516
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 517 FDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQ 592
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
18-592 |
4.48e-123 |
|
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: 375.19 E-value: 4.48e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 18 RSVKSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVD------SLEQVNDGLTSIIAVpvTLVLLYG-LLRFFN 90
Cdd:TIGR02204 4 RPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDhgfskdSSGLLNRYFAFLLVV--ALVLALGtAARFYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 91 VIlgeirdtlfgRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGL-SRDMERGT-------SGISFLMRFMVfnIVPTL 162
Cdd:TIGR02204 82 VT----------WLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVvSRLTTDTTllqsvigSSLSMALRNAL--MCIGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 163 LEILFVVAIffhqyglNFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQR 242
Cdd:TIGR02204 150 LIMMFITSP-------KLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 243 YDEEL-ALWETARRKNRLTLFgLNSGQALIIASAMTSMLLLAANGVVAKEM---TLGDFVLINAFMMqlfMPLNFLGFVY 318
Cdd:TIGR02204 223 FGGAVeKAYEAARQRIRTRAL-LTAIVIVLVFGAIVGVLWVGAHDVIAGKMsagTLGQFVFYAVMVA---GSIGTLSEVW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 319 REIKGSLANIEKMFELLERVPKVTDKKQAKELNI-GDGTISFKDVRFEY--DPSRPILKGINFTINSGEKLAVVGESGSG 395
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVpLRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 396 KSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDF 475
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 476 VQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTI 555
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
570 580 590
....*....|....*....|....*....|....*..
gi 2261045687 556 VDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQ 592
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
21-592 |
2.84e-120 |
|
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: 367.50 E-value: 2.84e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 21 KSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDgLTSIIAVP---VTLVLLYGLLRFFNvilgeir 97
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRD-RSVLWWVPlvvIGLAVLRGICSFVS------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 98 DTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGG-LSR---DMERGTSGISFLMRFMVfnivptlLEILFVVAIFF 173
Cdd:TIGR02203 75 TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTlLSRitfDSEQVASAATDAFIVLV-------RETLTVIGLFI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 174 HQYGLNFALiTLGSIVLY--IGFTAYATEWRTKYI-REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDeelalw 250
Cdd:TIGR02203 148 VLLYYSWQL-TLIVVVMLpvLSILMRRVSKRLRRIsKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFD------ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 251 etaRRKNRLTLFGLNSGQA---------LIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREI 321
Cdd:TIGR02203 221 ---AVSNRNRRLAMKMTSAgsisspitqLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPM 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 322 KGSLANIEKMFELLERVPKVTDKKQAKELNIGDgtISFKDVRFEYDP-SRPILKGINFTINSGEKLAVVGESGSGKSTLV 400
Cdd:TIGR02203 298 QRGLAAAESLFTLLDSPPEKDTGTRAIERARGD--VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 401 KLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNP-NADDDQVWQAIKHAHLYDFVQDL 479
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKL 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 480 PKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDAD 559
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
570 580 590
....*....|....*....|....*....|...
gi 2261045687 560 KIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQ 592
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
357-589 |
2.53e-117 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 347.68 E-value: 2.53e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDP-SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPIL 515
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMW 589
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-583 |
7.92e-112 |
|
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: 345.59 E-value: 7.92e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 21 KSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDGLTSIIAVPVTLVLLYgLLRFfnvILGEIRDTL 100
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVL-LLRA---LLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 101 FGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGI-SFLMRFM--VFN--IVPtlleILFVVAIFFhq 175
Cdd:COG4988 82 AFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALdGYFARYLpqLFLaaLVP----LLILVAVFP-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 176 ygLNF--ALITLGSIVLYIGFTAyATEWRTKYIREAN-QADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEElalwet 252
Cdd:COG4988 156 --LDWlsGLILLVTAPLIPLFMI-LVGKGAAKASRRQwRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEA------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 253 ARRKNRLTL----FGLNSGQAL-IIASAMTSML-LLAANGVVAKEMTLGD--FVLINAfmMQLFMPLNFLGFVYREIKGS 324
Cdd:COG4988 227 SEDFRKRTMkvlrVAFLSSAVLeFFASLSIALVaVYIGFRLLGGSLTLFAalFVLLLA--PEFFLPLRDLGSFYHARANG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 325 LANIEKMFELLERVPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLF 404
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 405 RFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQ 484
Cdd:COG4988 385 GFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 485 TVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVM 564
Cdd:COG4988 465 TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVL 544
|
570
....*....|....*....
gi 2261045687 565 HQGEIVETGNHQQLLLANG 583
Cdd:COG4988 545 DDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
18-590 |
7.24e-111 |
|
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: 343.29 E-value: 7.24e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 18 RSVKSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFI---LkeIVDSLEQvndGLTSIIAVPVTLVLLYGLLR------- 87
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALsgwL--IAAAALA---PPILNLFVPIVGVRAFAIGRtvfryle 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 88 --------FfnVILGEIRDTLFGRVTERAMRRVGlklfdHLHNLDLdfhLNRqtggLSRDMERgtsgisfLMRFMVFNIV 159
Cdd:COG4987 76 rlvshdatL--RLLADLRVRLYRRLEPLAPAGLA-----RLRSGDL---LNR----LVADVDA-------LDNLYLRVLL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 160 PTL--LEILFVVAIFFHQYGLNFALITLGSIVLYIGFTAYATEWRTK-YIREANQADSSSNSRAIDSLLNYETVKYFNNE 236
Cdd:COG4987 135 PLLvaLLVILAAVAFLAFFSPALALVLALGLLLAGLLLPLLAARLGRrAGRRLAAARAALRARLTDLLQGAAELAAYGAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 237 QYESQRYDE-ELALWETARRKNRLTLFGlNSGQALIIASAMTSMLLLAANGVVAKEMT---LGDFVLINAFMMQLFMPLN 312
Cdd:COG4987 215 DRALARLDAaEARLAAAQRRLARLSALA-QALLQLAAGLAVVAVLWLAAPLVAAGALSgplLALLVLAALALFEALAPLP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 313 fLGFVYREikGSLANIEKMFELLERVPKVTDKKQAKELNiGDGTISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGE 391
Cdd:COG4987 294 -AAAQHLG--RVRAAARRLNELLDAPPAVTEPAEPAPAP-GGPSLELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 392 SGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAH 471
Cdd:COG4987 370 SGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 472 LYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHR 551
Cdd:COG4987 450 LGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
570 580 590
....*....|....*....|....*....|....*....
gi 2261045687 552 LSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWA 590
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
357-592 |
1.63e-110 |
|
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: 330.66 E-value: 1.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYdPSRP---ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:cd03249 1 IEFKNVSFRY-PSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPP 513
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQ 592
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
355-583 |
1.36e-107 |
|
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: 322.64 E-value: 1.36e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMG 434
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPI 514
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 515 LIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANG 583
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-588 |
3.19e-103 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 323.84 E-value: 3.19e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 26 YLMEHKSRV-VLALICLVLAKVAIVGlPFILKEIVDSLEqvndGLTSIIAvpvtLVLLYGLLRFFNVILGEIRDTLFGRV 104
Cdd:PRK13657 13 YLGAEKRLGiLLAVANVLLAAATFAE-PILFGRIIDAIS----GKGDIFP----LLAAWAGFGLFNIIAGVLVARHADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 105 TERamRRVGL--KLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFL-MRFMVFNIVpTLLEILFVVAI-FFHQYGLNF 180
Cdd:PRK13657 84 AHR--RRLAVltEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwLEFMREHLA-TLVALVVLLPLaLFMNWRLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 181 ALITLGsiVLYIGFTAYATEwRTKYI-REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQrydeelALWETARRKNR- 258
Cdd:PRK13657 161 VLVVLG--IVYTLITTLVMR-KTKDGqAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQ------ALRDIADNLLAa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 259 ----LTLFGLNSGQALIIAS-AMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFL-GFVyREIKGSLANIEKMF 332
Cdd:PRK13657 232 qmpvLSWWALASVLNRAASTiTMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVvAFI-NQVFMAAPKLEEFF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 333 ELLERVPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSG 412
Cdd:PRK13657 311 EVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 413 SIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGL 492
Cdd:PRK13657 391 RILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGR 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 493 KLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVET 572
Cdd:PRK13657 471 QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVES 550
|
570
....*....|....*.
gi 2261045687 573 GNHQQLLLANGRYAKM 588
Cdd:PRK13657 551 GSFDELVARGGRFAAL 566
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
15-594 |
3.76e-101 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 321.69 E-value: 3.76e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 15 FSWrsvksLIPYLMEHKS--RVVLaLICLVLAKVAIVGlPFILKEIVDSLeQVNDGLTSIIAVPVTLVLLygllRFFNVI 92
Cdd:TIGR01846 127 FSW-----FIPAIIRYRKqfREVL-LISLALQLFALVT-PLLFQVVIDKV-LVHRGLSTLSVLALAMLAV----AIFEPA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 93 LGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGL---SRDMERgtsgisfLMRFMVFNIVPTLLEILFVV 169
Cdd:TIGR01846 195 LGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTvarVRELEQ-------IRNFLTGSALTVVLDLLFVV 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 170 ---AIFFHqYGLNFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEE 246
Cdd:TIGR01846 268 vflAVMFF-YSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 247 LALWetARRKNRLTLFGLNSGQALIIASAMTSMLLL--AANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGS 324
Cdd:TIGR01846 347 LAAY--VAASFRVTNLGNIAGQAIELIQKLTFAILLwfGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQT 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 325 LANIEKMFELLERvPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRP-ILKGINFTINSGEKLAVVGESGSGKSTLVKLL 403
Cdd:TIGR01846 425 GIALERLGDILNS-PTEPRSAGLAALPELRGAITFENIRFRYAPDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLL 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 404 FRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKE 483
Cdd:TIGR01846 504 QRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGY 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 484 QTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIV 563
Cdd:TIGR01846 584 NTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIV 663
|
570 580 590
....*....|....*....|....*....|.
gi 2261045687 564 MHQGEIVETGNHQQLLLANGRYAKMWAMQQD 594
Cdd:TIGR01846 664 LEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
37-331 |
2.90e-99 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 303.76 E-value: 2.90e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSLeqvNDGLTSIIAVPVTLVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKL 116
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNAL---TLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 117 FDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIVPTLLEILFVVAIFFHQYGLNFALITLGSIVLYIGFTA 196
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 197 YATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGLNSGQALIIASAM 276
Cdd:cd18560 158 KVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 277 TSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKM 331
Cdd:cd18560 238 TLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-592 |
5.10e-94 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 300.01 E-value: 5.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 16 SWRSVKSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDsleqvnDGLTS-----IIAVPVTLVLLYGLLRFFN 90
Cdd:PRK11176 9 TWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLD------DGFGKadrsvLKWMPLVVIGLMILRGITS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 91 VILGEIRDTLFGRVTERaMRRvglKLFDHLHNLDLDFHLNRQTGGL-SR---DMERGTSGISFLMrfmvFNIVPTLLEI- 165
Cdd:PRK11176 83 FISSYCISWVSGKVVMT-MRR---RLFGHMMGMPVSFFDKQSTGTLlSRityDSEQVASSSSGAL----ITVVREGASIi 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 166 -LFVVaIFFHQYGLNFALITLGSIVlyigftAYATEWRTKYIREANQADSSS----NSRAIDSLLNYETVKYFNNEQYES 240
Cdd:PRK11176 155 gLFIM-MFYYSWQLSLILIVIAPIV------SIAIRVVSKRFRNISKNMQNTmgqvTTSAEQMLKGHKEVLIFGGQEVET 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 241 QRYDeelalwetaRRKNRLTLFGLN--SGQAL------IIAS-AMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPL 311
Cdd:PRK11176 228 KRFD---------KVSNRMRQQGMKmvSASSIsdpiiqLIASlALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 312 NFLGFVYREIKGSLANIEKMFELLERVPKVTDKKqaKELNIGDGTISFKDVRFEYdPSR--PILKGINFTINSGEKLAVV 389
Cdd:PRK11176 299 KSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGK--RVIERAKGDIEFRNVTFTY-PGKevPALRNINFKIPAGKTVALV 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 390 GESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYG-NPNADDDQVWQAIK 468
Cdd:PRK11176 376 GRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAAR 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 469 HAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVI 548
Cdd:PRK11176 456 MAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI 535
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2261045687 549 AHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQ 592
Cdd:PRK11176 536 AHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-588 |
7.84e-91 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 295.09 E-value: 7.84e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 23 LIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDSLeqVNDGLTSIIAVPVTLVLLYGLLRFFnviLGEIRDTLFG 102
Cdd:TIGR00958 152 LLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTL--GGDKGPPALASAIFFMCLLSIASSV---SAGLRGGSFN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 103 RVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFMVFNIVPTL--LEILFVVAIFFHQYGLNF 180
Cdd:TIGR00958 227 YTMARINLRIREDLFRSLLRQDLGFFDENKTGEL---TSRLSSDTQTMSRSLSLNVNVLLrnLVMLLGLLGFMLWLSPRL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 181 ALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLT 260
Cdd:TIGR00958 304 TMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 261 LFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKMFELLERVPK 340
Cdd:TIGR00958 384 YAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPN 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 341 VTDKKQAKELNIgDGTISFKDVRFEY--DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS 418
Cdd:TIGR00958 464 IPLTGTLAPLNL-EGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDG 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 419 VNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGE 498
Cdd:TIGR00958 543 VPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQ 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 499 KQRVAIARTILKRPPILIFDEATSSLDSGSEQailaALQEI--AKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQ 576
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESrsRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
|
570
....*....|..
gi 2261045687 577 QLLLANGRYAKM 588
Cdd:TIGR00958 699 QLMEDQGCYKHL 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
357-568 |
1.95e-83 |
|
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: 258.08 E-value: 1.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFNDSIFENIrygnpnadddqvwqaikhahlydfvqdlpkkeqtvvgerglkLSGGEKQRVAIARTILKRPPIL 515
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGE 568
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
38-331 |
2.36e-83 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 262.95 E-value: 2.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 38 LICLVLAKVAIVGLPFILKEIVDSLEQVNDglTSIIAVPVTLVLLYGLLRFFNV-------ILGEIRDTLFGRVTERAMR 110
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLTPDSA--DSPLAFPWALILLYVFLKFLQGggsgsvgLLSNLRSFLWIPVQQFTTR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIVPTLLEIlfVVAIFFHQYGLN--FALITLGSI 188
Cdd:cd18581 80 EISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADI--IIAIIYFAIAFNpwFGLIVFVTM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 VLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGLNSGQ 268
Cdd:cd18581 158 ALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQ 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 269 ALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKM 331
Cdd:cd18581 238 NLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDMENM 300
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
357-592 |
1.27e-82 |
|
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: 258.57 E-value: 1.27e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRP-ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPIL 515
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQ 592
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
355-574 |
8.11e-82 |
|
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: 255.88 E-value: 8.11e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDP-SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:cd03244 1 GDIEFKNVSLRYRPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFNDSIFENIrygNPN--ADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKR 511
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNL---DPFgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 512 PPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGN 574
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
26-588 |
3.02e-79 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 261.36 E-value: 3.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 26 YLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDgltsiiaVPVTLVLLYGLlRFFNVILGEIRDTLFGRVT 105
Cdd:TIGR01192 13 YLNVHKNRVLLIVIANITLAAITIAEPILFGRIIDAISSKSD-------VLPTLALWAGF-GVFNTIAYVLVAREADRLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 106 ERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFL-MRFMVFNIVPTLLEILFVVAIFFHQYGLNFALIT 184
Cdd:TIGR01192 85 HGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLwLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 185 LGSIVLYIGFTAYAtewRTKYIREANQADSSSNSRAI-DSLLNYETVKYFNN---EQYESQRYDEELALWETARrknrLT 260
Cdd:TIGR01192 165 LGILYILIAKLVMQ---RTKNGQAAVEHHYHNVFKHVsDSISNVSVVHSYNRieaETSALKQFTNNLLSAQYPV----LD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 261 LFGLNSGQALIIAS-AMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKMFELLERVP 339
Cdd:TIGR01192 238 WWALASGLNRMASTiSMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 340 KVTDKKQAKELNIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSV 419
Cdd:TIGR01192 318 QREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 420 NIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEK 499
Cdd:TIGR01192 398 DINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGER 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 500 QRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:TIGR01192 478 QRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELI 557
|
....*....
gi 2261045687 580 LANGRYAKM 588
Cdd:TIGR01192 558 QKDGRFYKL 566
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-588 |
1.48e-77 |
|
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: 259.67 E-value: 1.48e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 11 TPVEFSWRSVKSLIPYLMEHKSRVVLALICLVLAKVAIVGLPFILKEIVDS-LEQVNDGLTSIIAVpvTLVLLYgllrFF 89
Cdd:TIGR01193 135 KPIKEKENSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTyIPHKMMGTLGIISI--GLIIAY----II 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 90 NVILGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVfnivpTL---LEIL 166
Cdd:TIGR01193 209 QQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTIL-----SLfldMWIL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 167 FVVAIFFHQYGLNFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEE 246
Cdd:TIGR01193 284 VIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 247 LALWETARRKNRLTLFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPL-NFLGFVYREIKGSL 325
Cdd:TIGR01193 364 FGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLeNIINLQPKLQAARV 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 326 ANiEKMFELLERVPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFR 405
Cdd:TIGR01193 444 AN-NRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVG 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 406 FYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGN-PNADDDQVWQAIKHAHLYDFVQDLPKKEQ 484
Cdd:TIGR01193 523 FFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQ 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 485 TVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIaKGHTSLVIAHRLSTIVDADKIIVM 564
Cdd:TIGR01193 603 TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVL 681
|
570 580
....*....|....*....|....
gi 2261045687 565 HQGEIVETGNHQQLLLANGRYAKM 588
Cdd:TIGR01193 682 DHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
329-593 |
2.38e-77 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 256.18 E-value: 2.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 329 EKMFELLERvPKVTDKKQAKELNigDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYD 408
Cdd:PRK10790 316 ERVFELMDG-PRQQYGNDDRPLQ--SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 409 VTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNpNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVG 488
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 489 ERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGE 568
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
250 260
....*....|....*....|....*
gi 2261045687 569 IVETGNHQQLLLANGRYAKMWAMQQ 593
Cdd:PRK10790 552 AVEQGTHQQLLAAQGRYWQMYQLQL 576
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
33-564 |
8.05e-73 |
|
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: 242.58 E-value: 8.05e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 33 RVVLALICL--VLAKVAIVGLPFILKEIVDSLEQVNDGLTSIIAVPVTLVLLYgLLRFfnvilgeirdtLFGRVTERAMR 110
Cdd:TIGR02857 2 RRALALLALlgVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVL-LLRA-----------LLGWLQERAAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RVGLK--------LFDHLHNLDLDFHLNRQTGGLSRDMERGTSGI-SFLMRFMVFNIVPTLLEILFVVAIFFHQygLNFA 181
Cdd:TIGR02857 70 RAAAAvksqlrerLLEAVAALGPRWLQGRPSGELATLALEGVEALdGYFARYLPQLVLAVIVPLAILAAVFPQD--WISG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 182 LITLGSIVLYIGFTAYaTEWRTKYIREANQADSSSNSRA-IDSLLNYETVKYFNNEQYESQrydeelALWETARRKNRLT 260
Cdd:TIGR02857 148 LILLLTAPLIPIFMIL-IGWAAQAAARKQWAALSRLSGHfLDRLRGLPTLKLFGRAKAQAA------AIRRSSEEYRERT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 261 LfglnsgQALIIASAMTSML-LLAANGV-----------VAKEMTL--GDFVLINAfmMQLFMPLNFLGFVYREIKGSLA 326
Cdd:TIGR02857 221 M------RVLRIAFLSSAVLeLFATLSValvavyigfrlLAGDLDLatGLFVLLLA--PEFYLPLRQLGAQYHARADGVA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 327 NIEKMFELLERVPKVT-DKKQAKELNigDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFR 405
Cdd:TIGR02857 293 AAEALFAVLDAAPRPLaGKAPVTAAP--ASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 406 FYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQT 485
Cdd:TIGR02857 371 FVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDT 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 486 VVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVM 564
Cdd:TIGR02857 451 PIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
355-573 |
1.00e-71 |
|
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: 229.78 E-value: 1.00e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:cd03245 1 GRIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPP 513
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETG 573
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
38-331 |
7.41e-70 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 227.41 E-value: 7.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 38 LICLVLAKVAIVGLPFILKEIVDSLEQVNDgltsiiAVPVTLVLLYGLLRFFN--VILGEIRDTLFGRVTERAMRRVGLK 115
Cdd:cd18583 2 FLCLLAERVLNVLVPRQLGIIVDSLSGGSG------KSPWKEIGLYVLLRFLQsgGGLGLLRSWLWIPVEQYSYRALSTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 116 LFDHLHNLDLDFHLNRQTGGLSRDMERGTSgISFLMRFMVFNIVPTLLEILFVVAIFFHQYGLNFALITLGSIVLYIGFT 195
Cdd:cd18583 76 AFNHVMNLSMDFHDSKKSGEVLKAIEQGSS-INDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLYVWST 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 196 AYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGLNSGQALIIASA 275
Cdd:cd18583 155 IKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLILTLG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 276 MTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKM 331
Cdd:cd18583 235 LLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
235-589 |
1.63e-69 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 235.10 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 235 NEQYESQRYDEELALWETARRKNRLTlfGLnsGQALIIAS---AMTSMLLLAANGVVAKEMTlGDFVLINAFM----MQL 307
Cdd:PRK11160 219 EDRYRQQLEQTEQQWLAAQRRQANLT--GL--SQALMILAnglTVVLMLWLAAGGVGGNAQP-GALIALFVFAalaaFEA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 308 FMPLnflGFVYREIKGSLANIEKMFELLERVPKVTDKKQAKeLNIGDGTISFKDVRFEY-DPSRPILKGINFTINSGEKL 386
Cdd:PRK11160 294 LMPV---AGAFQHLGQVIASARRINEITEQKPEVTFPTTST-AAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKV 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 387 AVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQA 466
Cdd:PRK11160 370 ALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEV 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 467 IKHAHLYDFVQDlPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSL 546
Cdd:PRK11160 450 LQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVL 528
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2261045687 547 VIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMW 589
Cdd:PRK11160 529 MITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
207-593 |
1.83e-68 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 231.91 E-value: 1.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 207 REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELAlwETARRKNRLTLFGLNSGQALIIASAMTSmlLLAANG 286
Cdd:PRK10789 166 KLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAE--DTGKKNMRVARIDARFDPTIYIAIGMAN--LLAIGG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 287 ----VVAKEMTLGDfvlINAFMMQL-FM--PLNFLGFVYREIKGSLANIEKMFELLERVPKVTDKKQAkeLNIGDGTISF 359
Cdd:PRK10789 242 gswmVVNGSLTLGQ---LTSFVMYLgLMiwPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEP--VPEGRGELDV 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQ 438
Cdd:PRK10789 317 NIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 DTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFD 518
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 519 EATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQQ 593
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQ 551
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
68-579 |
1.03e-64 |
|
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: 221.93 E-value: 1.03e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 68 GLTSIIAVpvtLVLLYGLLRFfnvilgeIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLsRDMERgtsgi 147
Cdd:COG4618 61 MLTLLALG---LYAVMGLLDA-------VRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQAL-RDLDT----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 148 sfLMRFMVFNIVPTLLEI----LFVVAIF-FHQYglnFALITLGSIVLYIGFtAYATEWRT-KYIREANQADSSSNSRAI 221
Cdd:COG4618 125 --LRQFLTGPGLFALFDLpwapIFLAVLFlFHPL---LGLLALVGALVLVAL-ALLNERLTrKPLKEANEAAIRANAFAE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 222 DSLLNYETVkyfnneqyESQRYDEELA-LWETARRKNRLTLFGLNSGQALIiaSAMT---------SMLLLAANGVVAKE 291
Cdd:COG4618 199 AALRNAEVI--------EAMGMLPALRrRWQRANARALALQARASDRAGGF--SALSkflrlllqsAVLGLGAYLVIQGE 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 292 MTLGdfvlinafMMqlfmplnflgfvyreIKGS------LANIE------KMF-----------ELLERVPKVTDKKQAK 348
Cdd:COG4618 269 ITPG--------AM---------------IAASilmgraLAPIEqaiggwKQFvsarqayrrlnELLAAVPAEPERMPLP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 349 ELNigdGTISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQ 427
Cdd:COG4618 326 RPK---GRLSVENLTVVPPGSkRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 428 SLRKHMGIVPQDTVLFNDSIFENI-RYGNPnaDDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIAR 506
Cdd:COG4618 403 ELGRHIGYLPQDVELFDGTIAENIaRFGDA--DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 507 TILKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
354-569 |
1.04e-64 |
|
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: 211.56 E-value: 1.04e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 354 DGTISFKDVRFEYD--PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRK 431
Cdd:cd03248 9 KGIVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 432 HMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKR 511
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 512 PPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEI 569
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-552 |
1.58e-64 |
|
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: 220.70 E-value: 1.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 23 LIPYLMEHKSRVVLALICLVLAKVAIVGLPFI---LkeIVDSLEQ--VNDGLTSIIAVPvTLVLLYGLLRFFNVILGEir 97
Cdd:TIGR02868 4 ILPLLKPRRRRLALAVLLGALALGSAVALLGVsawL--ISRAAEMppVLYLSVAAVAVR-AFGIGRAVFRYLERLVGH-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 98 DTLFgrvteRAMRRVGLKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFMVFNIVP----TLLEILFVVAIFF 173
Cdd:TIGR02868 79 DAAL-----RSLGALRVRVYERLARQALAGRRRLRRGDL---LGRLGADVDALQDLYVRVIVPagvaLVVGAAAVAAIAV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 174 HQYGlnfALITLGSIVLYIGFTA-YATEWRTKYIREANQADSSSNSRAIDSLLNY--ETVKYFNNEQYESQRYDEELALW 250
Cdd:TIGR02868 151 LSVP---AALILAAGLLLAGFVApLVSLRAARAAEQALARLRGELAAQLTDALDGaaELVASGALPAALAQVEEADRELT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 251 ETARRKNRLTLFGlNSGQALIIASAMTSMLLLAANGVVAKEM---TLGDFVLINafmMQLFMPLNFLGFVYREIKGSLAN 327
Cdd:TIGR02868 228 RAERRAAAATALG-AALTLLAAGLAVLGALWAGGPAVADGRLapvTLAVLVLLP---LAAFEAFAALPAAAQQLTRVRAA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 328 IEKMFELLERVPKVTDKKQAKELNIGDG--TISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFR 405
Cdd:TIGR02868 304 AERIVEVLDAAGPVAEGSAPAAGAVGLGkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 406 FYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQT 485
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDT 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 486 VVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRL 552
Cdd:TIGR02868 464 VLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
295-594 |
1.16e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 211.63 E-value: 1.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 295 GDFVLINA--FmmqlFMPLNFLGFVYREIKGSLANIEKMFELLErVPKVTDKKQAKELNIGDG-TISFKD-VRFEYDPSR 370
Cdd:PRK11174 290 GFFVLILApeF----YQPLRDLGTFYHAKAQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPvTIEAEDlEILSPDGKT 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 371 pILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRF--YdvtSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIF 448
Cdd:PRK11174 365 -LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGS 528
Cdd:PRK11174 441 DNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 529 EQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKMWAMQQD 594
Cdd:PRK11174 521 EQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
354-573 |
3.65e-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: 193.78 E-value: 3.65e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 354 DGTISFKDVRFEYDPSRP-ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKH 432
Cdd:cd03369 4 HGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 433 MGIVPQDTVLFNDSIFENI-RYGNpnADDDQVWQAIKhahlydfvqdlpkkeqtvVGERGLKLSGGEKQRVAIARTILKR 511
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 512 PPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETG 573
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
357-569 |
6.13e-52 |
|
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: 175.87 E-value: 6.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFNDSIFENIrygnpnadddqvwqaikhahlydfvqdlpkkeqtvvgerglkLSGGEKQRVAIARTILKRPPIL 515
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVDADKIIVMHQGEI 569
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
357-579 |
1.57e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 176.75 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIV 436
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIKHA----HLYDFVQDLPkkeqtvvgergLKLSGGEKQRVAIARTI 508
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEAlelvGLEHLADRPP-----------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIA-HRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
262-568 |
3.59e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 187.54 E-value: 3.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 262 FGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGdfVLINAFMMQLFMPlNFlgfvyREIKGSLANIEKMFELLERVPKV 341
Cdd:PTZ00265 297 FGFWYGTRIIISDLSNQQPNNDFHGGSVISILLG--VLISMFMLTIILP-NI-----TEYMKSLEATNSLYEIINRKPLV 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 342 TDKKQAKEL-NIGdgTISFKDVRFEYDPSR--PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI-D 417
Cdd:PTZ00265 369 ENNDDGKKLkDIK--KIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInD 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 418 SVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYG----------------NPNA----------------------- 458
Cdd:PTZ00265 447 SHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDsqenknkrnscrakcagdlndms 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 459 ------------------DDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:PTZ00265 527 nttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 521 TSSLDSGSEQAILAALQEIaKGH---TSLVIAHRLSTIVDADKIIVMHQGE 568
Cdd:PTZ00265 607 TSSLDNKSEYLVQKTINNL-KGNenrITIIIAHRLSTIRYANTIFVLSNRE 656
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-587 |
3.97e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 187.54 E-value: 3.97e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 72 IIAVPVTLVLLYGLLRFFNVILGE-IRDTLFGRVTERAMRRvGLKLFDHLHNLD--LDFHLNRQTGGLSRDMergTSGIS 148
Cdd:PTZ00265 872 ILVIAIAMFISETLKNYYNNVIGEkVEKTMKRRLFENILYQ-EISFFDQDKHAPglLSAHINRDVHLLKTGL---VNNIV 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 149 FLMRFMVFNIVPTLLEILF---VVAIFFHQYGLNFALITLGSIVlyigftAYATEWRTKYIREANQADSSSNSRAI---- 221
Cdd:PTZ00265 948 IFTHFIVLFLVSMVMSFYFcpiVAAVLTGTYFIFMRVFAIRARL------TANKDVEKKEINQPGTVFAYNSDDEIfkdp 1021
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 222 -----DSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLT---LFGLN-SGQALIIASAMTSMLLLAANGVVakem 292
Cdd:PTZ00265 1022 sfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVnsmLWGFSqSAQLFINSFAYWFGSFLIRRGTI---- 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 293 tlgdfvLINAFMMQLFMPLnFLGFV---YREIKGSLAN----IEKMFELLERVPKVTDKKQA----KELNIGDGTISFKD 361
Cdd:PTZ00265 1098 ------LVDDFMKSLFTFL-FTGSYagkLMSLKGDSENaklsFEKYYPLIIRKSNIDVRDNGgiriKNKNDIKGKIEIMD 1170
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 362 VRFEY--DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDV------------------------------ 409
Cdd:PTZ00265 1171 VNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnv 1250
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 410 ------------------------TSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDQVWQ 465
Cdd:PTZ00265 1251 gmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKR 1330
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 466 AIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GH 543
Cdd:PTZ00265 1331 ACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDK 1410
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 2261045687 544 TSLVIAHRLSTIVDADKIIVMHQ----GEIVET-GNHQQLLLA-NGRYAK 587
Cdd:PTZ00265 1411 TIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVqDGVYKK 1460
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
324-588 |
3.97e-48 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 181.47 E-value: 3.97e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 324 SLAniEKMFELLERVPKVTDKKQAKELNIGD----------GTISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGES 392
Cdd:PLN03130 1197 SLA--ENSLNAVERVGTYIDLPSEAPLVIENnrpppgwpssGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRT 1274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 393 GSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIRYGNPNADDDqVWQAIKHAHL 472
Cdd:PLN03130 1275 GAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDAD-LWESLERAHL 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 473 YDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRL 552
Cdd:PLN03130 1354 KDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRL 1433
|
250 260 270
....*....|....*....|....*....|....*..
gi 2261045687 553 STIVDADKIIVMHQGEIVETGNHQQLLL-ANGRYAKM 588
Cdd:PLN03130 1434 NTIIDCDRILVLDAGRVVEFDTPENLLSnEGSAFSKM 1470
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
358-568 |
5.91e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 166.49 E-value: 5.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 358 SFKDVRFEY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIV 436
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQ--DTVLFNDSIFENI-----RYGNPNADDDQ-VWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIARTI 508
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVafgleNLGLPEEEIEErVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGE 568
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
323-579 |
1.79e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 173.94 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 323 GSLANIEKMFELLERVPKVTDKKQAKELNIGDGT--ISFKDVRFEYDPSRP----ILKGINFTINSGEKLAVVGESGSGK 396
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 397 STLVKLLFRFYDVTSGSIEIDSVNIKTVTQQS---LRKHMGIVPQD---------TVLfnDSIFE---NIRYGNPNADDD 461
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQDpysslnprmTVG--DIIAEplrLHGLLSRAERRE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 462 QVWQAIKHAHL-YDFVQDLPkkeqtvvGErglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSgSEQA-ILAALQEI 539
Cdd:COG1123 383 RVAELLERVGLpPDLADRYP-------HE----LSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQAqILNLLRDL 450
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2261045687 540 AK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG1123 451 QRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
302-588 |
2.54e-45 |
|
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: 172.82 E-value: 2.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 302 AFMMQLFMPLNFLGFVYREIKGSLANIEKMFELLE---RVPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRP-ILKGIN 377
Cdd:TIGR00957 1227 SYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSEtekEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDLDlVLRHIN 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 378 FTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENIrygNP- 456
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPf 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 457 -NADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAA 535
Cdd:TIGR00957 1384 sQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQST 1463
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 536 LQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAKM 588
Cdd:TIGR00957 1464 IRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
357-573 |
3.67e-45 |
|
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: 159.59 E-value: 3.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDP---SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---R 430
Cdd:cd03257 2 LEVKNLSVSFPTgggSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 KHMGIVPQD---------TVLfnDSIFENIRYGNPNADDdqvwQAIKHAHLYDFVQ-DLPKKeqtVVGERGLKLSGGEKQ 500
Cdd:cd03257 82 KEIQMVFQDpmsslnprmTIG--EQIAEPLRIHGKLSKK----EARKEAVLLLLVGvGLPEE---VLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 501 RVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
357-573 |
1.02e-44 |
|
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: 156.70 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVtQQSLRKHMGI 435
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFNDSIFENIrygnpnadddqvwqaikhahlydfvqdlpkkeqtvvgerGLKLSGGEKQRVAIARTILKRPPIL 515
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETG 573
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
373-522 |
2.45e-44 |
|
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: 154.73 E-value: 2.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFND-SIFENI 451
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 452 RYG------NPNADDDQVWQAIKHAHLYDFvqdlpkkEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATS 522
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEKLGLGDL-------ADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
355-579 |
5.06e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 169.00 E-value: 5.06e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:PLN03232 1233 GSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFNDSIFENIRYGNPNADDDqVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPP 513
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSK 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:PLN03232 1392 ILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
357-569 |
1.84e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 154.20 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIV 436
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFNDSIFENI----RYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEqtvvgerglkLSGGEKQRVAIARTILKRP 512
Cdd:COG4619 80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPVER----------LSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 513 PILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAH------RLstivdADKIIVMHQGEI 569
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
357-571 |
6.15e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 153.28 E-value: 6.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQS---LRKHM 433
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFND-SIFENIRYG------NPNADDDQVWQAIKHAHLYDFVQDLPkkeqtvvgergLKLSGGEKQRVAIAR 506
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 507 TILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIA-HRLStIVDA--DKIIVMHQGEIVE 571
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLE-LVDRmpKRVLELEDGRLVR 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
357-578 |
6.29e-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: 153.49 E-value: 6.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRpILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDV-----TSGSIEIDSVNIKT--VTQQSL 429
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQDTVLFNDSIFENIRYG-------NPNADDDQVWQAIKHAHLYDFVQDLPKkeqtvvgerGLKLSGGEKQRV 502
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLH---------ALGLSGGQQQRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 503 AIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAH------RLstivdADKIIVMHQGEIVETGNHQ 576
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFGPTE 225
|
..
gi 2261045687 577 QL 578
Cdd:cd03260 226 QI 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
357-579 |
6.69e-43 |
|
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: 154.43 E-value: 6.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIV 436
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVL-FNDSIFENIRYG---------NPNADDDQ-VWQAIKHAHLYDFvqdlpkKEQTVvgergLKLSGGEKQRVAIA 505
Cdd:COG1120 81 PQEPPApFGLTVRELVALGryphlglfgRPSAEDREaVEEALERTGLEHL------ADRPV-----DELSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHrlstivD-------ADKIIVMHQGEIVETGNHQ 576
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLH------DlnlaaryADRLVLLKDGRIVAQGPPE 223
|
...
gi 2261045687 577 QLL 579
Cdd:COG1120 224 EVL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
357-581 |
1.96e-42 |
|
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: 152.35 E-value: 1.96e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSR---PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---R 430
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 KHMGIVPQDTVLFND-SIFENIRYGNPNADDDQVWQAIKHAHLYDFVqDLPKKEQTVVGErglkLSGGEKQRVAIARTIL 509
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELV-GLEDKADAYPAQ----LSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
357-583 |
2.75e-42 |
|
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: 152.97 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDsvNIKTVTQQSL---RKH 432
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENLweiRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 433 MGIVPQD--------TVLfNDSIF--ENIryGNPNaddDQVWQAIKHA----HLYDFVQDLPKKeqtvvgerglkLSGGE 498
Cdd:TIGR04520 79 VGMVFQNpdnqfvgaTVE-DDVAFglENL--GVPR---EEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 499 KQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVDADKIIVMHQGEIVETG--- 573
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpr 221
|
250
....*....|...
gi 2261045687 574 ---NHQQLLLANG 583
Cdd:TIGR04520 222 eifSQVELLKEIG 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
358-568 |
4.79e-42 |
|
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: 148.55 E-value: 4.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 358 SFKDVRFEYdPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVP 437
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 438 QdtvlfndsifenirygnpnadddqvwqaikhahlydfvqdlpkkeqtvvgerglkLSGGEKQRVAIARTILKRPPILIF 517
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 518 DEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDA-DKIIVMHQGE 568
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
357-571 |
7.16e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.58 E-value: 7.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEY---DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---- 429
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQDTVLFND-SIFENI----RYGNPNADDDQVW--QAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRV 502
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENValplLLAGVSRKERRERarELLERVGLGDRLDHRPSQ-----------LSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 503 AIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVDADKIIVMHQGEIVE 571
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
357-579 |
7.20e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.98 E-value: 7.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQsLRKHMGIV 436
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFND-SIFENIR-----YGNPNADDDQ-VWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTIL 509
Cdd:COG1131 79 PQEPALYPDlTVRENLRffarlYGLPRKEARErIDELLELFGLTDAADRKVGT-----------LSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
357-569 |
2.72e-41 |
|
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: 148.79 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEY---DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---- 429
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQDTVLFND-SIFENIRY-----GNPNADD-DQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRV 502
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERrERAEELLERVGLGDRLNHYPSE-----------LSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 503 AIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVDADKIIVMHQGEI 569
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
355-580 |
8.45e-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: 148.90 E-value: 8.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFNDSIFENIrygNP--NADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKR 511
Cdd:cd03288 98 SIILQDPILFSGSIRFNL---DPecKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 512 PPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLL 580
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
357-568 |
1.32e-40 |
|
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: 146.46 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSR----PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIdsvniktvtqqslRKH 432
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 433 MGIVPQDTVLFNDSIFENIRYGNPnADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRP 512
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 513 PILIFDEATSSLDSGSEQAIL--AALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGE 568
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIFenCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
360-570 |
1.36e-40 |
|
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: 146.25 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKtvtQQSLRKHMGIVPQD 439
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 T--VLFNDSIFENIRYGNPNADDD--QVWQAIKHAHLYDFVQDLPkkeqtvvgergLKLSGGEKQRVAIARTILKRPPIL 515
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIV 570
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
357-578 |
2.37e-40 |
|
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: 146.88 E-value: 2.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ---QSLRKHM 433
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFND-SIFENIRYgnP----NADDDQVWQAIKHAHLyDFVqDLPKKEQTVVGErglkLSGGEKQRVAIARTI 508
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAF--PlrehTRLSEEEIREIVLEKL-EAV-GLRGAEDLYPAE----LSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 509 LKRPPILIFDEATSSLD---SGSEQAILAALQEiAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:cd03261 152 ALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKK-ELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
370-579 |
9.26e-40 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 145.72 E-value: 9.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQD---------T 440
Cdd:COG1124 18 VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyaslhprhT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 441 VlfNDSIFENIR-YGNPNADDdQVWQAIKHAHLY-DFVQDLPkkEQtvvgerglkLSGGEKQRVAIARTILKRPPILIFD 518
Cdd:COG1124 98 V--DRILAEPLRiHGLPDREE-RIAELLEQVGLPpSFLDRYP--HQ---------LSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 519 EATSSLDSgSEQA-ILAALQEI--AKGHTSLVIAHRLStIVD--ADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG1124 164 EPTSALDV-SVQAeILNLLKDLreERGLTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLL 227
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
350-579 |
9.31e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 146.29 E-value: 9.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 350 LNIGDGTISFKDVRFEYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQS 428
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 429 LRKHMGIVPQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIKHAHLYDFVQDLPKKEQtvvgergLKLSGGEKQRVAI 504
Cdd:PRK13632 81 IRKKIGIIFQnpDNQFIGATVEDDIAFGleNKKVPPKKMKDIIDDLAKKVGMEDYLDKEP-------QNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 505 ARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIA--HRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
357-579 |
1.09e-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: 151.98 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDP-SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVT---SGSIEIDSVNIKTVTQQSLRKH 432
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 433 MGIVPQD--TVLFNDSIFENIRYG------NPNADDDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAI 504
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 505 ARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
357-579 |
1.12e-39 |
|
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: 145.12 E-value: 1.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVT---QQSLRKHM 433
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFND-SIFENIRYGnpnadddqvwqaikhahLYDFvQDLPKKE-QTVVGER----GLK---------LSGGE 498
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFP-----------------LREH-TDLSEAEiRELVLEKlelvGLPgaadkmpseLSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 499 KQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNH 575
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
....
gi 2261045687 576 QQLL 579
Cdd:COG1127 227 EELL 230
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
34-311 |
1.82e-39 |
|
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: 145.48 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDGLTSIIAVpvtLVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVG 113
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNV---YSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 114 LKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIVPTLLEILFVVAIFFHqYGLNFALITLGSIVLYIG 193
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFY-YGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 194 FTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGLNSGQALIIA 273
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 2261045687 274 SAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPL 311
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
357-578 |
6.95e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 143.25 E-value: 6.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDV-----TSGSIEIDSVNI--KTVTQQSL 429
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDIydPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQDTVLFNDSIFENIRYG------NPNAD-DDQVWQAIKHAHLYDFVQD-LpkkeqtvvGERGLKLSGGEKQR 501
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSElDEIVEESLRKAALWDEVKDrL--------KKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 502 VAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAH------RLStivdaDKIIVMHQGEIVETGNH 575
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPT 237
|
...
gi 2261045687 576 QQL 578
Cdd:COG1117 238 EQI 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
357-569 |
1.07e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.54 E-value: 1.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVtqqslRKHMGIV 436
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQ-------------DTVLFNdsifeniRYGN-------PNADDDQVWQAIKHAHLYDFvqdlpKKEQtvVGErglkLSG 496
Cdd:COG1121 81 PQraevdwdfpitvrDVVLMG-------RYGRrglfrrpSRADREAVDEALERVGLEDL-----ADRP--IGE----LSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 497 GEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEI 569
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
357-588 |
1.18e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.62 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQD-------TVLFNDSIF--ENIryGNPNAD-DDQVWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIA 505
Cdd:PRK13635 86 VFQNpdnqfvgATVQDDVAFglENI--GVPREEmVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAALQEI--AKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANG 583
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
....*
gi 2261045687 584 RYAKM 588
Cdd:PRK13635 233 MLQEI 237
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
34-329 |
6.02e-38 |
|
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: 141.92 E-value: 6.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLEqVNDGLTSIIAVPVTLVLLYGLLRFFNVIlgeiRDTLFGRVTERAMRRVG 113
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVI-PAGDLSLLLWIALLLLLLALLRALLSYL----RRYLAARLGQRVVFDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 114 LKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRF---MVFNIVPTLLEILFVVAIFFHqygLNF--ALITLGSI 188
Cdd:cd07346 76 RDLFRHLQRLSLSFFDRNRTGDL---MSRLTSDVDAVQNLvssGLLQLLSDVLTLIGALVILFY---LNWklTLVALLLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 VLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGLNSGQ 268
Cdd:cd07346 150 PLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 269 ALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIE 329
Cdd:cd07346 230 GLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLE 290
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
356-570 |
7.30e-38 |
|
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: 138.45 E-value: 7.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDPS-----RPILKGINFTINSGEKLAVVGESGSGKSTLVKLL--FRFYDVTSGSIEIDSVNIKtvtQQS 428
Cdd:cd03213 3 TLSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 429 LRKHMGIVPQDTVLF-NDSIFENIRYgnpnadddqvwqaikHAHLydfvqdlpkkeqtvvgeRGLklSGGEKQRVAIART 507
Cdd:cd03213 80 FRKIIGYVPQDDILHpTLTVRETLMF---------------AAKL-----------------RGL--SGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIV--DADKIIVMHQGEIV 570
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVI 191
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
357-579 |
1.24e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 139.36 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTVTQQSLRKHMG 434
Cdd:COG1126 2 IEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDgeDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLFND-SIFENIRYGnpnadddQVWqaikhahlydfVQDLPKKEQTVVGER-----GL---------KLSGGEK 499
Cdd:COG1126 81 MVFQQFNLFPHlTVLENVTLA-------PIK-----------VKKMSKAEAEERAMEllervGLadkadaypaQLSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 500 QRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQ 577
Cdd:COG1126 143 QRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKeGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEE 222
|
..
gi 2261045687 578 LL 579
Cdd:COG1126 223 FF 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
357-574 |
5.12e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 140.60 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYD-PSRPI--LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---R 430
Cdd:COG1135 2 IELENLSKTFPtKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 KHMGIVPQDtvlFN--DS--IFENIRY-----GNPNADDDQvwqaiKHAHLYDFVqDLPKKEQTVVGErglkLSGGEKQR 501
Cdd:COG1135 82 RKIGMIFQH---FNllSSrtVAENVALpleiaGVPKAEIRK-----RVAELLELV-GLSDKADAYPSQ----LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 502 VAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
357-573 |
1.06e-36 |
|
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: 136.11 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQslRKHMGIV 436
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLF-NDSIFENIRYG-----NPNAD-DDQVWQAIKHAHLYDFVQDLPkkeqtvvgergLKLSGGEKQRVAIARTIL 509
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGlklrgVPKAEiRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
357-570 |
2.96e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKH---M 433
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQD-------TVLFN--------DSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQdlpkkeqtvvgERGLKLSGGE 498
Cdd:COG3638 83 GMIFQQfnlvprlSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAY-----------QRADQLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 499 KQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRlstiVD-----ADKIIVMHQGEIV 570
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQ----VDlarryADRIIGLRDGRVV 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
360-573 |
3.73e-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: 133.33 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQd 439
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 tvlfndsifenirygnpnadddqvwqAIKHAHLYDFVqdlpkkeqtvvgERGLK-LSGGEKQRVAIARTILKRPPILIFD 518
Cdd:cd03214 81 --------------------------ALELLGLAHLA------------DRPFNeLSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 519 EATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
357-569 |
4.14e-36 |
|
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: 132.91 E-value: 4.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTvTQQSLRKHMGIV 436
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFND-SIFENirygnpnadddqvwqaikhahlydfvqdlpkkeqtvvgergLKLSGGEKQRVAIARTILKRPPIL 515
Cdd:cd03230 79 PEEPSLYENlTVREN-----------------------------------------LKLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEI 569
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
357-569 |
4.15e-36 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 134.19 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPsRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTVTQQSLRKHMG 434
Cdd:cd03262 1 IEIKNLHKSFGD-FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglKLTDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLF-NDSIFENIRYGnpnadddQVWqaikhahlydfVQDLPKKEQTVVGERGLK--------------LSGGEK 499
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLA-------PIK-----------VKGMSKAEAEERALELLEkvgladkadaypaqLSGGQQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 500 QRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEI 569
Cdd:cd03262 142 QRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
357-579 |
4.69e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 137.49 E-value: 4.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILK---GINFTINSGEKLAVVGESGSGKSTLVKLLFRFYD---VTSGSIEIDSVNIKTVTQQSLR 430
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 ----KHMGIVPQD--TVLfndsifeNIRY--GnpnaddDQVWQAIKhAHlydfvQDLPKKEQ--------TVVG----ER 490
Cdd:COG0444 82 kirgREIQMIFQDpmTSL-------NPVMtvG------DQIAEPLR-IH-----GGLSKAEAreraiellERVGlpdpER 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 491 GLK-----LSGGEKQRVAIARTILKRPPILIFDEATSSLDsGSEQA-ILAALQEIAKGH-TSLV-IAHRLSTIVD-ADKI 561
Cdd:COG0444 143 RLDrypheLSGGMRQRVMIARALALEPKLLIADEPTTALD-VTIQAqILNLLKDLQRELgLAILfITHDLGVVAEiADRV 221
|
250
....*....|....*...
gi 2261045687 562 IVMHQGEIVETGNHQQLL 579
Cdd:COG0444 222 AVMYAGRIVEEGPVEELF 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
357-569 |
1.97e-35 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 132.53 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQS---LRKHM 433
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFND-SIFENIRY-----GNPNadddQVWQAiKHAHLYDFVqDLPKKEQTVVGErglkLSGGEKQRVAIART 507
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFalevtGVPP----REIRK-RVPAALELV-GLSHKHRALPAE----LSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADK--IIVMHQGEI 569
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
358-564 |
1.40e-33 |
|
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: 127.26 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 358 SFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVtqqslRKHMGIVP 437
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 438 QDTVL---FNDSIFENI---RYG------NPNADDdqvWQAIKHAHlyDFVqDLPKKEQTVVGErglkLSGGEKQRVAIA 505
Cdd:cd03235 75 QRRSIdrdFPISVRDVVlmgLYGhkglfrRLSKAD---KAKVDEAL--ERV-GLSELADRQIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVM 564
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLL 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
355-580 |
1.75e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 137.22 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDPSRP-ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFNDSIFENIrygNP--NADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKR 511
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKK 1463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 512 PPILIF-DEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLL 580
Cdd:PTZ00243 1464 GSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
357-568 |
2.53e-33 |
|
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: 125.38 E-value: 2.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYdPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQS--LRKHMG 434
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLF-NDSIFENIRYGnpnadddqvwqaikhahlydfvqdlpkkeqtvvgerglkLSGGEKQRVAIARTILKRPP 513
Cdd:cd03229 80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGE 568
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
357-570 |
3.62e-33 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 126.91 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ---QSLRKHM 433
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFND-SIFENI---RYGNPNAdddqvWQAI----------KHAHLYDFVQDLPKKEQtvvgeRGLKLSGGEK 499
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVlsgRLGRRST-----WRSLfglfpkeekqRALAALERVGLLDKAYQ-----RADQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 500 QRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA--KGHTSLVIAHRLSTIVD-ADKIIVMHQGEIV 570
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
250-567 |
4.16e-33 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 133.78 E-value: 4.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 250 WETARRKNRLTLFGLNSGQALIIASamtsmLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIE 329
Cdd:COG4178 259 RRLIRRQRNLTFFTTGYGQLAVIFP-----ILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSLAEWRATVD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 330 KMFEL---LERVPKVTDKKQAKELNiGDGTISFKDVRFeYDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFR 405
Cdd:COG4178 334 RLAGFeeaLEAADALPEAASRIETS-EDGALALEDLTL-RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 406 FYDVTSGSIEIDSvniktvtqqslRKHMGIVPQDTVLFNDSIFENIRYGNP--NADDDQVWQAIKHAHLYDFVQDLpkke 483
Cdd:COG4178 412 LWPYGSGRIARPA-----------GARVLFLPQRPYLPLGTLREALLYPATaeAFSDAELREALEAVGLGHLAERL---- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 484 qTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIV 563
Cdd:COG4178 477 -DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLE 555
|
....
gi 2261045687 564 MHQG 567
Cdd:COG4178 556 LTGD 559
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
356-574 |
4.72e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 128.24 E-value: 4.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNI--KTVTQQSL 429
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIKHAHL-----YDFVQDLPKKEqtvvgerglkLSGGEKQ 500
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMNivgldYEDYKDKSPFE----------LSGGQKR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 501 RVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
357-573 |
1.26e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 128.68 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQslRKHMGIV 436
Cdd:COG3842 6 LELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLF-NDSIFENIRYG-----NPNAD-DDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTIL 509
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGlrmrgVPKAEiRARVAELLELVGLEGLADRYPHQ-----------LSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAI---LAALQEiAKGHTSLVIAHRLS---TIvdADKIIVMHQGEIVETG 573
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMreeLRRLQR-ELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
357-579 |
1.76e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.87 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRpilKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIkTVTQQSLRKhMGIV 436
Cdd:COG3840 2 LRLDDLTYRYGDFP---LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERP-VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFND-SIFENIRYG-----NPNADD-DQVWQAIKHAHLYDFVQDLPkkEQtvvgerglkLSGGEKQRVAIARTIL 509
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLP--GQ---------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
357-572 |
2.25e-32 |
|
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: 124.12 E-value: 2.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEY---DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIktvtqQSLRKHM 433
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFN-DSIFENIRYG-----NPNAD-DDQVWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIAR 506
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgVPKAEaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 507 TILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLS-TIVDADKIIVMHQ--GEIVET 572
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
357-573 |
4.64e-32 |
|
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: 124.04 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSG-SIEI-----DSVNIktvtqQSLR 430
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDV-----WELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 KHMGIV---------PQDTVL------FNDSIFeniRYGNPNADD-DQVWQAIKHAHLYDFvqdlpkKEQTVvgergLKL 494
Cdd:COG1119 78 KRIGLVspalqlrfpRDETVLdvvlsgFFDSIG---LYREPTDEQrERARELLELLGLAHL------ADRPF-----GTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 495 SGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLV-IAHRLSTIVDA-DKIIVMHQGEIVE 571
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
..
gi 2261045687 572 TG 573
Cdd:COG1119 224 AG 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
355-573 |
3.21e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvniKTVTQQSLRK-HM 433
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTDLPPKDrNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLF-NDSIFENIRYG--NPNADDDQVWQAIKHA----HLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIAR 506
Cdd:COG3839 78 AMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAaellGLEDLLDRKPKQ-----------LSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 507 TILKRPPILIFDEATSSLDsgseqailAAL-----QEIAK-----GHTSLVIAHrlstivD-------ADKIIVMHQGEI 569
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLD--------AKLrvemrAEIKRlhrrlGTTTIYVTH------DqveamtlADRIAVMNDGRI 212
|
....
gi 2261045687 570 VETG 573
Cdd:COG3839 213 QQVG 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
373-579 |
4.48e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 127.11 E-value: 4.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDvTSGSIEIDSVNIKTVTQ---QSLRKHMGIVPQD---------T 440
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRralRPLRRRMQVVFQDpfgslsprmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 441 VLfnDSIFENIRYGNPNADDDQVWQAIkhahlydfvqdlpkkeQTVVGERGLK----------LSGGEKQRVAIARTILK 510
Cdd:COG4172 381 VG--QIIAEGLRVHGPGLSAAERRARV----------------AEALEEVGLDpaarhrypheFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 511 RPPILIFDEATSSLDSgSEQA-ILAALQEIAKGH--TSLVIAHRLStIVDA--DKIIVMHQGEIVETGNHQQLL 579
Cdd:COG4172 443 EPKLLVLDEPTSALDV-SVQAqILDLLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQVF 514
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
297-587 |
4.52e-31 |
|
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: 129.68 E-value: 4.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 297 FVLINAFMMqLFMPLNFLGFVYREIKGSLANIEKMFELLERVPKVTDKKQAKELNIGDG-TISFKDVRFEY---DPsrPI 372
Cdd:TIGR00957 577 FVSLALFNI-LRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGnSITVHNATFTWardLP--PT 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIeidsvniktvtqqSLRKHMGIVPQDTVLFNDSIFENIR 452
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENIL 720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 453 YGNPnADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAI 532
Cdd:TIGR00957 721 FGKA-LNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 533 LAAL---QEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLLLANGRYAK 587
Cdd:TIGR00957 800 FEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE 857
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
357-572 |
8.81e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 120.96 E-value: 8.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDP---SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvniKTVTQQSLRkhM 433
Cdd:COG1116 8 LELRGVSKRFPTgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG---KPVTGPGPD--R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFN-DSIFENIRYG------NPNADDDQVWQAIKHAHLYDFVQDLPKkeQtvvgerglkLSGGEKQRVAIAR 506
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH--Q---------LSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 507 TILKRPPILIFDEATSSLDsgseqAILAA-----LQEI--AKGHTSLVIAH------RLstivdADKIIVM--HQGEIVE 571
Cdd:COG1116 152 ALANDPEVLLMDEPFGALD-----ALTRErlqdeLLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLsaRPGRIVE 221
|
.
gi 2261045687 572 T 572
Cdd:COG1116 222 E 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
375-573 |
9.25e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 122.53 E-value: 9.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 375 GINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---RKHMGIVPQD---------TVl 442
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDpyaslnprmTV- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 443 fNDSIFENIRY---GNPNADDDQVWQAIK-------HAHLYdfvqdlPKkeqtvvgerglKLSGGEKQRVAIARTILKRP 512
Cdd:COG4608 115 -GDIIAEPLRIhglASKAERRERVAELLElvglrpeHADRY------PH-----------EFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 513 PILIFDEATSSLDSgSEQA----ILAALQEiAKGHTSLVIAHRLStIVD--ADKIIVMHQGEIVETG 573
Cdd:COG4608 177 KLIVCDEPVSALDV-SIQAqvlnLLEDLQD-ELGLTYLFISHDLS-VVRhiSDRVAVMYLGKIVEIA 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
357-578 |
1.27e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.63 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPI-LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTV-LFNDSIFE-NIRYGNPN----ADDDQ--VWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIART 507
Cdd:PRK13648 88 VFQNPDnQFVGSIVKyDVAFGLENhavpYDEMHrrVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
185-578 |
1.67e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 127.78 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 185 LGSIVLY--IGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRY----DEELALWETARRKNR 258
Cdd:PLN03232 445 FGSLILFllIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIqgirNEELSWFRKAQLLSA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 259 LTLFGLNSGQALIIASAMTSMLLLAANGVVAKEmtlgdFVLINAFMMqLFMPLNFLGFVYREIKG---SLANIEKMFELL 335
Cdd:PLN03232 525 FNSFILNSIPVVVTLVSFGVFVLLGGDLTPARA-----FTSLSLFAV-LRSPLNMLPNLLSQVVNanvSLQRIEELLLSE 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 336 ERVpkvtdKKQAKELNIGDGTISFKDVRFEYDP--SRPILKGINFTINSGEKLAVVGESGSGKSTLVK-LLFRFYDVTSG 412
Cdd:PLN03232 599 ERI-----LAQNPPLQPGAPAISIKNGYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETS 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 413 SIEIdsvniktvtqqslRKHMGIVPQDTVLFNDSIFENIRYGNpNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGL 492
Cdd:PLN03232 674 SVVI-------------RGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGV 739
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 493 KLSGGEKQRVAIARTILKRPPILIFDEATSSLDSG-SEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVE 571
Cdd:PLN03232 740 NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKE 819
|
....*..
gi 2261045687 572 TGNHQQL 578
Cdd:PLN03232 820 EGTFAEL 826
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
355-579 |
3.39e-30 |
|
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: 119.57 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDvTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:cd03289 1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFNDSIFENIR-YGNPNadDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRP 512
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 513 PILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
369-579 |
4.82e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 4.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVL-FNDSI 447
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FENIRYGnpnadddqvwqAIKHAHLYDFVQDLPKKEQTVVGERGLK------LSGGEKQRVAIARTIL------KRPPIL 515
Cdd:PRK13548 94 EEVVAMG-----------RAPHGLSRAEDDALVAAALAQVDLAHLAgrdypqLSGGEQQRVQLARVLAqlwepdGPPRWL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLS-TIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK13548 163 LLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
357-561 |
9.94e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 116.42 E-value: 9.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQsLRKHMGIV 436
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFND-SIFENIRY----GNPNADDDQVWQAIKHAHLYDFvQDLPkkeqtvVGerglKLSGGEKQRVAIARTILKR 511
Cdd:COG4133 81 GHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGL-ADLP------VR----QLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 512 PPILIFDEATSSLDSGSEQAILAALQE-IAKGHTSLVIAHRLSTIVDADKI 561
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
357-579 |
1.76e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.73 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSrPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTVTQQSLRKHMG 434
Cdd:PRK09493 2 IEFKNVSKHFGPT-QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLFND-SIFENIRYGnPNadddQVWQAIKhAHLYDFVQDLPKKeqtvVG--ERG----LKLSGGEKQRVAIART 507
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFG-PL----RVRGASK-EEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
244-583 |
3.97e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 123.69 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 244 DEELALWETARRKNRLTLFGLNSGQALIIASAMTSMLLLAANGVVAKEMTlgDFVLINAFMMQLFMPLNFLGFVYREiKG 323
Cdd:PLN03130 510 DDELSWFRKAQLLSAFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFT--SLSLFAVLRFPLFMLPNLITQAVNA-NV 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 324 SLANIEKMFELLERV--PKVTdkkqakeLNIGDGTISFKDVRFEYDPS--RPILKGINFTINSGEKLAVVGESGSGKSTL 399
Cdd:PLN03130 587 SLKRLEELLLAEERVllPNPP-------LEPGLPAISIKNGYFSWDSKaeRPTLSNINLDVPVGSLVAIVGSTGEGKTSL 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 400 VKLLFRfydvtsgsiEIDSVNIKTVTqqsLRKHMGIVPQDTVLFNDSIFENIRYGNPnADDDQVWQAIKHAHLYDFVQDL 479
Cdd:PLN03130 660 ISAMLG---------ELPPRSDASVV---IRGTVAYVPQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLL 726
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 480 PKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSG-SEQAILAALQEIAKGHTSLVIAHRLSTIVDA 558
Cdd:PLN03130 727 PGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV 806
|
330 340
....*....|....*....|....*
gi 2261045687 559 DKIIVMHQGEIVETGNHQQlLLANG 583
Cdd:PLN03130 807 DRIILVHEGMIKEEGTYEE-LSNNG 830
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
357-579 |
4.15e-29 |
|
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: 115.86 E-value: 4.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIV 436
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLF-NDSIFENI-------RYGNPNAdDDQVWQAIKHAHL--YDFVQDLPKkeqtvvgerglKLSGGEKQRVAIAR 506
Cdd:cd03295 81 IQQIGLFpHMTVEENIalvpkllKWPKEKI-RERADELLALVGLdpAEFADRYPH-----------ELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 507 TILKRPPILIFDEATSSLDS---GSEQAILAALQEiAKGHTSLVIAHRL-STIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPitrDQLQEEFKRLQQ-ELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
376-579 |
5.37e-29 |
|
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: 116.20 E-value: 5.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL----RKHMGIVPQDTVLF-NDSIFEN 450
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 451 IRYG------NPNADDDQVWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSL 524
Cdd:cd03294 123 VAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 525 D---SGSEQAILAALQEiAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:cd03294 192 DpliRREMQDELLRLQA-ELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
369-579 |
1.91e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 114.06 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVL-FNDSI 447
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FENIR-----YGNPNADDDQVwqaIKHA-HLYDfVQDLpkkeqtvvGERG-LKLSGGEKQRVAIAR-------TILKRPP 513
Cdd:COG4559 93 EEVVAlgrapHGSSAAQDRQI---VREAlALVG-LAHL--------AGRSyQTLSGGEQQRVQLARvlaqlwePVDGGPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLS-TIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLArRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
373-579 |
2.25e-28 |
|
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: 113.20 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQslRKHMGIVPQDTVLF-NDSIFENI 451
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 452 RYG-----NPNADDD----QVWQAIKHAHLydfvqdLPKKEQTvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATS 522
Cdd:cd03299 93 AYGlkkrkVDKKEIErkvlEIAEMLGIDHL------LNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 523 SLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTI-VDADKIIVMHQGEIVETGNHQQLL 579
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
357-578 |
2.40e-28 |
|
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: 113.10 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQslRKHMGIV 436
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFND-SIFENIRYG------NPNADDDQVWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIARTIL 509
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLS-TIVDADKIIVMHQGEIVETGNHQQL 578
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
371-572 |
3.48e-28 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 110.60 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 371 PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTVtQQSLRKHMGIVPQdtvlfndsif 448
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkEVSFASP-RDARRAGIAMVYQ---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 enirygnpnadddqvwqaikhahlydfvqdlpkkeqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGS 528
Cdd:cd03216 83 ---------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2261045687 529 EQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVET 572
Cdd:cd03216 118 VERLFKVIRRLrAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-579 |
5.53e-28 |
|
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: 120.02 E-value: 5.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 8 QDNTPVEFSWrsvKSLIPYLMEHKSRVVLALICLV--LAKVA--IVGLPFILKEIVDSLEQVNDGLTSIIAVPVTLVLLY 83
Cdd:TIGR01271 844 RENVFETTTW---NTYLRYITTNRNLVFVLIFCLVifLAEVAasLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIIT 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 84 GLLRFFNV-ILGEIRDTLFGRVTERamrrvGLKLFDHLHNLDLDFH--------------LNR-QTGGLSRDMERGTSGI 147
Cdd:TIGR01271 921 PTSAYYIFyIYVGTADSVLALGFFR-----GLPLVHTLLTVSKRLHeqmlhsvlqapmavLNTmKAGRILNRFTKDMAII 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 148 SFLMRFMVFNIVPTLLEIL---FVVAIFfHQYGLnfaLITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSL 224
Cdd:TIGR01271 996 DDMLPLTLFDFIQLTLIVLgaiFVVSVL-QPYIF---IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSL 1071
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 225 LNYETVKYFNNEQYESQRYDEELALwETAR---RKNRLTLFGLNSGQALIIASAMTSMLLLAANGVvaKEMTLGdfvLIN 301
Cdd:TIGR01271 1072 KGLWTIRAFGRQSYFETLFHKALNL-HTANwflYLSTLRWFQMRIDIIFVFFFIAVTFIAIGTNQD--GEGEVG---IIL 1145
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 302 AFMMQLFMPLNFLGFVYREIKGSLANIEKMFELLERVPK-----------------VTDKKQAKELNIGDGTISFKDVRF 364
Cdd:TIGR01271 1146 TLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEeprpsggggkyqlstvlVIENPHAQKCWPSGGQMDVQGLTA 1225
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 365 EY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDvTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLF 443
Cdd:TIGR01271 1226 KYtEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIF 1304
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 NDSIFENIrygNPNA--DDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEAT 521
Cdd:TIGR01271 1305 SGTFRKNL---DPYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPS 1381
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 522 SSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
357-573 |
5.81e-28 |
|
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: 111.52 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYdPSRPILKGINFTINSGeKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTvTQQSLRKHMGIV 436
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQD-TVLFNDSIFENIRY-----GNPNAD-DDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTIL 509
Cdd:cd03264 78 PQEfGVYPNFTVREFLDYiawlkGIPSKEvKARVDEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
373-574 |
1.17e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTvTQQSLRKHMGIVPQDTVLFND-SIFE 449
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgePVRFRS-PRDAQAAGIAIIHQELNLVPNlSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIRYGNPNADddqvWQAIKHAHLYDFVQDLPKK------EQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEATSS 523
Cdd:COG1129 99 NIFLGREPRR----GGLIDWRAMRRRARELLARlgldidPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 524 L-DSGSEQ--AILAALQeiAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:COG1129 171 LtEREVERlfRIIRRLK--AQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGP 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
372-579 |
1.25e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.77 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNI---KTVTQQ-----SLRKHMGIVPQDTVLF 443
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkglirQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 -NDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVvgerGLKLSGGEKQRVAIARTILKRPPILIFDEATS 522
Cdd:PRK11264 98 pHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSY----PRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 523 SLDSGSEQAILAALQEIAKGHTSLVI-AHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIvTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
357-578 |
1.38e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 112.52 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDP--SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMG 434
Cdd:PRK13650 5 IEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIKHAHLYDFVQDLPKKEQTvvgerglKLSGGEKQRVAIARTILK 510
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGleNKGIPHEEMKERVNEALELVGMQDFKEREPA-------RLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 511 RPPILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
357-573 |
2.99e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.50 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQslRKHMGIV 436
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLF-NDSIFENIRYG-----NPNAD-DDQVWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIARTIL 509
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqkTPAAEiTPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAI---LAALQEiAKGHTSLVIAH-RLSTIVDADKIIVMHQGEIVETG 573
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMqneLKALQR-KLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
373-580 |
3.19e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 110.64 E-value: 3.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDV-----TSGSIEIDSVNI---KTVTQQsLRKHMGIVPQDTVLFN 444
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 445 DSIFENIRYG---NPNAD----DDQVWQAIKHAHLYDFVQDlpkkeqtVVGERGLKLSGGEKQRVAIARTILKRPPILIF 517
Cdd:PRK14239 100 MSIYENVVYGlrlKGIKDkqvlDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 518 DEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRL---STIvdADKIIVMHQGEIVETGNHQQLLL 580
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQMFM 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
357-578 |
4.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQ----S 428
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 429 LRKHMGIVPQ--DTVLFNDSIFENIRYGNPN---ADDDQVWQAIKHAHLYDFVQDLPKKEQtvvgergLKLSGGEKQRVA 503
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgvSEEDAKQKAREMIELVGLPEELLARSP-------FELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 504 IARTILKRPPILIFDEATSSLDSGSEQAILAALQEI--AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
357-573 |
4.58e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 112.20 E-value: 4.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYD-PSRPI--LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---R 430
Cdd:PRK11153 2 IELKNISKVFPqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 KHMGIVPQDtvlFN----DSIFENIRY-----GNPNADDDQvwqaiKHAHLYDFVqDLPKKEQTVVGErglkLSGGEKQR 501
Cdd:PRK11153 82 RQIGMIFQH---FNllssRTVFDNVALplelaGTPKAEIKA-----RVTELLELV-GLSDKADRYPAQ----LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 502 VAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
360-579 |
7.01e-27 |
|
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: 108.68 E-value: 7.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEYDPSrPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNI-KTVTQQSLRKHMGIVPQ 438
Cdd:cd03224 4 ENLNAGYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERARAGIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 DTVLFND-SIFENIRYGNPNADDDQVWQAIkhAHLYDFVQDLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIF 517
Cdd:cd03224 83 GRRIFPElTVEENLLLGAYARRRAKRKARL--ERVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 518 DEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
372-572 |
1.50e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 107.90 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL----RKHMGIVPQD-------T 440
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSfqllptlT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 441 VLfndsifENI-----RYGNPNAdddqvwQAIKHAHLydfvqdlpkkEQTVVGERgLK-----LSGGEKQRVAIARTILK 510
Cdd:COG4181 107 AL------ENVmlpleLAGRRDA------RARARALL----------ERVGLGHR-LDhypaqLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 511 RPPILIFDEATSSLDSGSEQAILAALQEIAKGH-TSLVIA-HRLSTIVDADKIIVMHQGEIVET 572
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLVED 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
354-573 |
2.81e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.73 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 354 DGTISFKDVRFEY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKL---LFRFYDVTSGSIEIDSVNIKTVTQQSL 429
Cdd:PRK13640 3 DNIVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQ--DTVLFNDSIFENIRYGNPNADDDQ------VWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQR 501
Cdd:PRK13640 83 REKVGIVFQnpDNQFVGATVGDDVAFGLENRAVPRpemikiVRDVLADVGMLDYIDSEPAN-----------LSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 502 VAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA--KGHTSLVIAHRLSTIVDADKIIVMHQGEIVETG 573
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
329-571 |
4.87e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 329 EKMFELLERVPKVTDKKQAK-----ELNIGDGTISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLL 403
Cdd:COG0488 283 IKALEKLEREEPPRRDKTVEirfppPERLGKKVLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 404 frfydvtSGSIEIDSVNIK---TVtqqslrkHMGIVPQDTVLF--NDSIFENIRYGNPNADDdqvwqaikhAHLYDFVQD 478
Cdd:COG0488 362 -------AGELEPDSGTVKlgeTV-------KIGYFDQHQEELdpDKTVLDELRDGAPGGTE---------QEVRGYLGR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 479 L---PKKEQTVVGerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIaKGhTSLVIAH-R--L 552
Cdd:COG0488 419 FlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfL 492
|
250
....*....|....*....
gi 2261045687 553 STIvdADKIIVMHQGEIVE 571
Cdd:COG0488 493 DRV--ATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
356-589 |
7.55e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 107.56 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ----Q 427
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 428 SLRKHMGIVPQ--DTVLFNDSIFENIRYG--NPNADDDQVwqaikHAHLYDFVQDLpKKEQTVVGERGLKLSGGEKQRVA 503
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEV-----KNYAHRLLMDL-GFSRDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 504 IARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA--KGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQlLL 580
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKE-LF 234
|
....*....
gi 2261045687 581 ANGRYAKMW 589
Cdd:PRK13646 235 KDKKKLADW 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
373-573 |
1.61e-25 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 105.21 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIkTVTQQSLRKHMGIVP--QDTVLFND-SIFE 449
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPHEIARLGIGRtfQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIRYG---------NPNADDDQVWQAIKHAH-LYDFVqDLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDE 519
Cdd:cd03219 95 NVMVAaqartgsglLLARARREEREARERAEeLLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 520 ATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03219 170 PAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
357-579 |
1.69e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 106.22 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ-QSLRKHMGI 435
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQ--DTVLFNDSIFENIRYG------NPNADDDQVWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIART 507
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpenlclPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
357-578 |
2.09e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 104.51 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEY-DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTvTQQSLRKHMGI 435
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFND-SIFENIRY-----GNPNADDDQVwqaiKHAHLYDFvqDLPKKEQTVVGErglkLSGGEKQRVAIARTIL 509
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLPKSEIKEE----VELLLRVL--GLTDKANKRART----LSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTI-VDADKIIVMHQGEIVETGNHQQL 578
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
357-574 |
4.67e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.17 E-value: 4.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEY-----DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDsvNIKTVTQQSL-- 429
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--GLDTSDEENLwd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 -RKHMGIVPQ--DTVLFNDSIFENIRYG------NPNADDDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQ 500
Cdd:PRK13633 83 iRNKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPHL-----------LSGGQKQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 501 RVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVDADKIIVMHQGEIVETGN 574
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
357-579 |
5.26e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 5.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPI--LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMG 434
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIKHAHLYDFVQDLPKKEQTvvgerglKLSGGEKQRVAIARTILK 510
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGmeNQGIPREEMIKRVDEALLAVNMLDFKTREPA-------RLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 511 RPPILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
360-573 |
6.36e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 6.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKtVTQQSL---RKHMGIV 436
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIKHAhlydfvqdLPKkeqtvVGERGLK------LSGGEKQRVAIAR 506
Cdd:PRK13639 84 FQnpDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEA--------LKA-----VGMEGFEnkpphhLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 507 TILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTI-VDADKIIVMHQGEIVETG 573
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEG 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
363-573 |
7.11e-25 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.83 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 363 RFEyDPSRPI--LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKhMGIVPQDT 440
Cdd:cd03266 10 RFR-DVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDST 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 441 VLFND-SIFENIRYgnpNADDDQVWQAIKHAHLYDFVQDLPKKEqtVVGERGLKLSGGEKQRVAIARTILKRPPILIFDE 519
Cdd:cd03266 88 GLYDRlTARENLEY---FAGLYGLKGDELTARLEELADRLGMEE--LLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 520 ATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
357-573 |
9.37e-25 |
|
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: 102.19 E-value: 9.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYD--PSRPILkginfTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVtqQSLRKHMG 434
Cdd:cd03298 1 VRLDKIRFSYGeqPMHFDL-----TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLFND-SIFENIRYG-NP----NADDDQ-VWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIART 507
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGlSPglklTAEDRQaIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEI--AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
34-317 |
9.37e-25 |
|
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: 104.44 E-value: 9.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLeqVNDGLTSIIAVPVTLVLLYGLLRffnVILGEIRDTLFGRVTERAMRRVG 113
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV--IGGGLRELLWLLALLILGVALLR---GVFRYLQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 114 LKLFDHLHNLDLDFHLNRQTGGLsrdMERGTS---GISFLMRFMVFNIVPTLLEILFVVAIFFHqygLN--FALITLgSI 188
Cdd:cd18542 76 NDLYDHLQRLSFSFHDKARTGDL---MSRCTSdvdTIRRFLAFGLVELVRAVLLFIGALIIMFS---INwkLTLISL-AI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 VLYIGFTAYATEWRTKYI-REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEE-LALWETARRKNRLTLFGLNS 266
Cdd:cd18542 149 IPFIALFSYVFFKKVRPAfEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKEnEEYRDLNIKLAKLLAKYWPL 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 267 GQaLIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFV 317
Cdd:cd18542 229 MD-FLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRL 278
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
356-571 |
1.34e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.14 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ----Q 427
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 428 SLRKHMGIVPQ--DTVLFNDSIFENIRYGNPN---ADDDQVWQAIKHAHLYDFVQDLPKKEQtvvgergLKLSGGEKQRV 502
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgfSEDEAKEKALKWLKKVGLSEDLISKSP-------FELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 503 AIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVE 571
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKLIK 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-581 |
1.47e-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: 107.46 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 350 LNIGDGTISFKDvrfeYDPSRPILKGINFTINSGEKLAVVGESGSGKS----TLVKLLFRFYDVTSGSIEIDSVNIKTVT 425
Cdd:COG4172 7 LSVEDLSVAFGQ----GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 426 QQSLRK----HMGIVPQD--TVLfndsifenirygNP-NADDDQVWQAIKHaHlydfvQDLPKKE---QTV-----VG-- 488
Cdd:COG4172 83 ERELRRirgnRIAMIFQEpmTSL------------NPlHTIGKQIAEVLRL-H-----RGLSGAAaraRALellerVGip 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 489 --ERGLK-----LSGGEKQRVAIARTILKRPPILIFDEATSSLDSgSEQA-ILAALQEIAK--GHTSLVIAHRLsTIVD- 557
Cdd:COG4172 145 dpERRLDayphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDV-TVQAqILDLLKDLQRelGMALLLITHDL-GVVRr 222
|
250 260
....*....|....*....|....*
gi 2261045687 558 -ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
356-575 |
3.19e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI--------DSVNIKTVtqQ 427
Cdd:COG4161 2 SIQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghqfdfsQKPSEKAI--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 428 SLRKHMGIV-------PQDTVLfnDSIFE---NIRYGNPNADDDQVWQAIKHAHLYDFVQDLPkkeqtvvgergLKLSGG 497
Cdd:COG4161 79 LLRQKVGMVfqqynlwPHLTVM--ENLIEapcKVLGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 498 EKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRlstiVD-----ADKIIVMHQGEIVE 571
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHE----VEfarkvASQVVYMEKGRIIE 221
|
....
gi 2261045687 572 TGNH 575
Cdd:COG4161 222 QGDA 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
373-574 |
3.48e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTvTQQSLRKHMGIVPQDTVLFND-SIFE 449
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVRIRS-PRDAIALGIGMVHQHFMLVPNlTVAE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIRYGNPNA-----DDDQVWQAIKH-AHLYDFVQDLPKKeqtvVGErglkLSGGEKQRVAIARTILKRPPILIFDEATSS 523
Cdd:COG3845 100 NIVLGLEPTkggrlDRKAARARIRElSERYGLDVDPDAK----VED----LSVGEQQRVEILKALYRGARILILDEPTAV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 524 LdsgSEQAI---LAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:COG3845 172 L---TPQEAdelFEILRRLAAeGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVD 224
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
356-576 |
4.91e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDPSRpILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI--DSVNIKTVTQ----QSL 429
Cdd:PRK11124 2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPSdkaiREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIV-------PQDTVLFNdsIFE---NIRYGNPNADDDQVWQAIKHAHLYDFVQDLPkkeqtvvgergLKLSGGEK 499
Cdd:PRK11124 81 RRNVGMVfqqynlwPHLTVQQN--LIEapcRVLGLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 500 QRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRlstiVD-----ADKIIVMHQGEIVETG 573
Cdd:PRK11124 148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHE----VEvarktASRVVYMENGHIVEQG 223
|
...
gi 2261045687 574 NHQ 576
Cdd:PRK11124 224 DAS 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-581 |
5.51e-24 |
|
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: 106.04 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 22 SLIPYLM-EHKSRVVLALICLVLAKVAIVGLpfilkeivdsLEQVNDGLTSIIAVPVTLVLLYGLLRFFNVILGEIRDTL 100
Cdd:COG4615 2 NLLRLLLrESRWLLLLALLLGLLSGLANAGL----------IALINQALNATGAALARLLLLFAGLLVLLLLSRLASQLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 101 FGRVTERAMRRVGLKLFDHLHNLDLDfHLNRQTGG-----LSRDMERgtsgISflmrfMVFNIVPTLLE--ILFVVAIFF 173
Cdd:COG4615 72 LTRLGQHAVARLRLRLSRRILAAPLE-RLERIGAArllaaLTEDVRT----IS-----QAFVRLPELLQsvALVLGCLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 174 HQYgLNF--ALITLGSIVLYIGFTAYATEWRTKYIREANQADsssnsraiDSLLNY-----ETVKYFNNEQYESQR-YDE 245
Cdd:COG4615 142 LAW-LSPplFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAE--------DRLFKHfrallEGFKELKLNRRRRRAfFDE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 246 ELAlwETARRKNRLTLFGLNsgqALIIASAMTSMLLLAANGVV---------AKEMTLGDFVLINAFMMqlfMPL-NFLG 315
Cdd:COG4615 213 DLQ--PTAERYRDLRIRADT---IFALANNWGNLLFFALIGLIlfllpalgwADPAVLSGFVLVLLFLR---GPLsQLVG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 316 FVYREIKG--SLANIEKMFELLERVPKVTDKKQAKELNIGDGTISFKDVRFEYDPSRP----ILKGINFTINSGEKLAVV 389
Cdd:COG4615 285 ALPTLSRAnvALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIV 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 390 GESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSifenirYG-NPNADDDQVWQAIK 468
Cdd:COG4615 365 GGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGlDGEADPARARELLE 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 469 HAHLydfvqdlpkkeQTVVGERG-----LKLSGGEKQRVAIARTILKRPPILIFDE-AtssldsgSEQ----------AI 532
Cdd:COG4615 439 RLEL-----------DHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEwA-------ADQdpefrrvfytEL 500
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 533 LAALQeiAKGHTSLVIAHrlstivD------ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:COG4615 501 LPELK--ARGKTVIAISH------DdryfdlADRVLKMDYGKLVELTGPAALAAS 547
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
357-573 |
9.09e-24 |
|
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: 99.64 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSV----------NIKTVTQ 426
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 427 Q-SLRKHMgivpqdtvlfndSIFENIRYG------NPNADDDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEK 499
Cdd:cd03301 80 NyALYPHM------------TVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 500 QRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAH-RLSTIVDADKIIVMHQGEIVETG 573
Cdd:cd03301 137 QRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
37-328 |
1.12e-23 |
|
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: 101.41 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSLEQVNDG--LTSIIAVPVTLVLLYGLLRFFNVILgeirdtlFGRVTERAMRRVGL 114
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTasLNQIALLLLGLFLLQAVFSFFRIYL-------FARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 115 KLFDHLHNLDLDFHLNRQTGGLSrdmERGTSGISFLMRFMVFNIVPTLLEILF----VVAIFFHQYGLnfALITLGSIVL 190
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELT---SRLSNDVTQIQDTLTTTLAEFLRQILTliggVVLLFFISWKL--TLLMLATVPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 191 YIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEEL-ALWETARRKNRL-TLFGlnSGQ 268
Cdd:cd18576 149 VVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALeRVVKLALKRARIrALFS--SFI 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 269 ALIIASAMTSMLLLAANGVVAKEMTLGDFVlinAFMMqlfmplnFLGFVYREIkGSLANI 328
Cdd:cd18576 227 IFLLFGAIVAVLWYGGRLVLAGELTAGDLV---AFLL-------YTLFIAGSI-GSLADL 275
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
360-579 |
2.34e-23 |
|
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: 98.90 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEYDPSrPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTV-TQQSLRKHMGIVPQ 438
Cdd:COG0410 7 ENLHAGYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 DTVLFND-SIFENIRYGNPNADDDQVWQAIKhAHLYDFVQDL-PKKEQtvvgeRGLKLSGGEKQRVAIARTILKRPPILI 516
Cdd:COG0410 86 GRRIFPSlTVEENLLLGAYARRDRAEVRADL-ERVYELFPRLkERRRQ-----RAGTLSGGEQQMLAIGRALMSRPKLLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 517 FDEAtssldsgSE-------QAILAALQEIAK-GHTSLVI---AHRLSTIvdADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG0410 160 LDEP-------SLglaplivEEIFEIIRRLNReGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELL 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
371-564 |
2.39e-23 |
|
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: 98.66 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 371 PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS----VNIKTVTQQ---SLRKH-MGIVPQ---- 438
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASPReilALRRRtIGYVSQflrv 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 -------DTVLfnDSIFENirygnpNADDDQVWQAIKH--AHLydfvqDLPkkeqtvvgERGLKL-----SGGEKQRVAI 504
Cdd:COG4778 105 iprvsalDVVA--EPLLER------GVDREEARARAREllARL-----NLP--------ERLWDLppatfSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 505 ARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLV-IAHRLSTI--VdADKIIVM 564
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReaV-ADRVVDV 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
377-579 |
2.97e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 98.50 E-value: 2.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 377 NFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNiKTVTQQSLRKhMGIVPQDTVLFND-SIFENIRYG- 454
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRP-VSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 455 NP----NADDDQVWQAI-KHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSE 529
Cdd:PRK10771 97 NPglklNAAQREKLHAIaRQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 530 QAILAALQEIA--KGHTSLVIAHRLStivDADKI----IVMHQGEIVETGNHQQLL 579
Cdd:PRK10771 166 QEMLTLVSQVCqeRQLTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELL 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
373-573 |
3.50e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.81 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIK---TVTQQSLRKHMGIVpqdtvlfndsiFE 449
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIV-----------FQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NiRYG--NPNADDDQVWQ---AIKhahlydfvQDLPKKEQTvvgER--------GLK----------LSGGEKQRVAIAR 506
Cdd:PRK11308 100 N-PYGslNPRKKVGQILEeplLIN--------TSLSAAERR---EKalammakvGLRpehydryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 507 TILKRPPILIFDEATSSLDSgSEQA----ILAALQEiaKGHTSLV-IAHRLStIVD--ADKIIVMHQGEIVETG 573
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDV-SVQAqvlnLMMDLQQ--ELGLSYVfISHDLS-VVEhiADEVMVMYLGRCVEKG 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
356-569 |
6.40e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.30 E-value: 6.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS--VN--------IKTVT 425
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNelepadrdIAMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 426 QQ-SLRKHMgivpqdtvlfndSIFENIRYG--NPNADDDQVWQAIKHA----HLYDFVQDLPKkeqtvvgerglKLSGGE 498
Cdd:PRK11650 83 QNyALYPHM------------SVRENMAYGlkIRGMPKAEIEERVAEAarilELEPLLDRKPR-----------ELSGGQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 499 KQRVAIARTILKRPPILIFDEATSSLDsgseqailAALQ-----EIAKGH-----TSLVIAH-RLSTIVDADKIIVMHQG 567
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLD--------AKLRvqmrlEIQRLHrrlktTSLYVTHdQVEAMTLADRVVVMNGG 211
|
..
gi 2261045687 568 EI 569
Cdd:PRK11650 212 VA 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
356-578 |
6.95e-23 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 97.80 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYdPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvniKTVTQQSLRK-HMG 434
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQErNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLFND-SIFENIRYG--------NPNAD--DDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVA 503
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvkprseRPPEAeiRAKVHELLKLVQLDWLADRYPAQ-----------LSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 504 IARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
333-568 |
7.69e-23 |
|
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: 98.78 E-value: 7.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 333 ELLERVPKVTDKKQAKElniGDGTISFKDVRFEydpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSG 412
Cdd:cd03291 19 ELLEKAKQENNDRKHSS---DDNNLFFSNLCLV---GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 413 SIeidsvniktvtqqslrKHMGIV---PQDTVLFNDSIFENIRYGnPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVVGE 489
Cdd:cd03291 93 KI----------------KHSGRIsfsSQFSWIMPGTIKENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 490 RGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAIL-AALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGE 568
Cdd:cd03291 156 GGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFeSCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
360-572 |
7.79e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.09 E-value: 7.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQD 439
Cdd:PRK10247 11 QNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 TVLFNDSIFENIRYgnPnadddqvWQaIKHAH--LYDFVQDLPKKE--QTVVGERGLKLSGGEKQRVAIARTILKRPPIL 515
Cdd:PRK10247 90 PTLFGDTVYDNLIF--P-------WQ-IRNQQpdPAIFLDDLERFAlpDTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 516 IFDEATSSLDSGSEQAI------LAALQEIAkghtSLVIAHRLSTIVDADKIIVM--HQGEIVET 572
Cdd:PRK10247 160 LLDEITSALDESNKHNVneiihrYVREQNIA----VLWVTHDKDEINHADKVITLqpHAGEMQEA 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
369-527 |
8.89e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 96.78 E-value: 8.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLL-------FRfydvTSGSIEIDSVNIKTVtqQSLRKHMGIVPQDTV 441
Cdd:COG4136 13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtlspaFS----ASGEVLLNGRRLTAL--PAEQRRIGILFQDDL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 442 LF-NDSIFENIRYGNP-----NADDDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTILKRPPIL 515
Cdd:COG4136 87 LFpHLSVGENLAFALPptigrAQRRARVEQALEEAGLAGFADRDPAT-----------LSGGQRARVALLRALLAEPRAL 155
|
170
....*....|..
gi 2261045687 516 IFDEATSSLDSG 527
Cdd:COG4136 156 LLDEPFSKLDAA 167
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
372-581 |
8.97e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.09 E-value: 8.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDvTSGSIEIDSVNIKTVTQQSL---RKHMGIVPQDTvlfNDSIf 448
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSSL- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 enirygNPNADDDQVWQ---AIKHAHLydfvqDLPKKEQTVVG---ERGL----------KLSGGEKQRVAIARTILKRP 512
Cdd:PRK15134 376 ------NPRLNVLQIIEeglRVHQPTL-----SAAQREQQVIAvmeEVGLdpetrhrypaEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 513 PILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLStIVDA--DKIIVMHQGEIVETGNHQQLLLA 581
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
354-579 |
1.27e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.88 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 354 DGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQ--DTVLFNDSIFENIRYGNPNAD------DDQVWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIA 505
Cdd:PRK13647 82 GLVFQdpDDQVFSSTVWDDVAFGPVNMGldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIA-HRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
364-567 |
1.78e-22 |
|
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: 95.86 E-value: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 364 FEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKT----VTQQSLRKHMGIVPQD 439
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfeATRSRNRYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 TVLFNDSIFENIRYGNPNadDDQVWQAIKHA-HLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFD 518
Cdd:cd03290 88 PWLLNATVEENITFGSPF--NKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 519 EATSSLDSG-----SEQAILAALQEIAKghTSLVIAHRLSTIVDADKIIVMHQG 567
Cdd:cd03290 166 DPFSALDIHlsdhlMQEGILKFLQDDKR--TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
376-573 |
2.00e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 95.82 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINsGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSV-------NIKTVTQQslrKHMGIVPQDTVLF-NDSI 447
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkKINLPPQQ---RKIGLVFQQYALFpHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FENIRYG----NPNADDDQVWQAIKHAHLydfvqdlpkkeQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSS 523
Cdd:cd03297 93 RENLAFGlkrkRNREDRISVDELLDLLGL-----------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 524 LDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
356-579 |
2.99e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 98.30 E-value: 2.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYdPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS--VNIKTVTQQslrKHM 433
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdLFTNLPPRE---RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLF-NDSIFENIRYGNPNADDDQvwQAIKH--AHLYDFVQdLPkkeqtvvgerGLK------LSGGEKQRVAI 504
Cdd:COG1118 78 GFVFQHYALFpHMTVAENIAFGLRVRPPSK--AEIRArvEELLELVQ-LE----------GLAdrypsqLSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 505 ARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAH------RLstivdADKIIVMHQGEIVETGNHQ 576
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPD 219
|
...
gi 2261045687 577 QLL 579
Cdd:COG1118 220 EVY 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
368-579 |
3.39e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.89 E-value: 3.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 368 PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLL-FRfydvTSGSIEIDS---VNIKTVTQQSLRKHMGIVPQDTVLF 443
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFR----SPKGVKGSGsvlLNGMPIDAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 ndsifeniryGNPNADDDQVWQA-----------IKHAHLYDFVQD--LPKKEQTVVGERGLK--LSGGEKQRVAIARTI 508
Cdd:TIGR00955 112 ----------PTLTVREHLMFQAhlrmprrvtkkEKRERVDEVLQAlgLRKCANTRIGVPGRVkgLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDA--DKIIVMHQGEIVETGNHQQLL 579
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAV 255
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
357-580 |
4.59e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 4.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIV 436
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQ--DTVLFNDSIFENIRYGNPNADDDQ------VWQAIKHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIARTI 508
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLLL 580
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
365-573 |
4.74e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.03 E-value: 4.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 365 EYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLL---FRFYDVTSGSIEIDSVNIKtvtQQSLRKHMGIVPQ-DT 440
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRK---PDQFQKCVAYVRQdDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 441 VLFNDSIFENIRYG--------NPNADDDQVWQ--AIKHAHLydfvqdlpkkeqTVVGERGLK-LSGGEKQRVAIARTIL 509
Cdd:cd03234 92 LLPGLTVRETLTYTailrlprkSSDAIRKKRVEdvLLRDLAL------------TRIGGNLVKgISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAKGHtSLVIA--HR-LSTIVDA-DKIIVMHQGEIVETG 573
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARRN-RIVILtiHQpRSDLFRLfDRILLLSSGEIVYSG 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-557 |
4.99e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTS-----GSIEIDSVNI--KTVTQQSL 429
Cdd:PRK14258 8 IKVNNLSFYYD-TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQDTVLFNDSIFENIRYG------NPNAD-DDQVWQAIKHAHLYDFVQDLPKKEqtvvgerGLKLSGGEKQRV 502
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEiDDIVESALKDADLWDEIKHKIHKS-------ALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 503 AIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIA----HRLSTIVD 557
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVshnlHQVSRLSD 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
354-574 |
8.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.68 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 354 DGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS--VNIKTVTQQSLRK 431
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 432 HMGIVPQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIKHAHLYDFVQDLPKKEQTVvgerglkLSGGEKQRVAIART 507
Cdd:PRK13636 83 SVGMVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTI-VDADKIIVMHQGEIVETGN 574
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGN 225
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
357-573 |
1.13e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 95.20 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ----QS 428
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 429 LRKHMGIVPQ--DTVLFNDSIFENIRYGNPN---ADDDQVWQAIKHAHLYDFVQDLPKKEQtvvgergLKLSGGEKQRVA 503
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgvSQEEAEALAREKLALVGISESLFEKNP-------FELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 504 IARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
376-578 |
1.50e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.33 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvniKTVTQQSLR-KHMGIVPQDTVLF-NDSIFENIRY 453
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG---EDVTHRSIQqRDICMVFQSYALFpHMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 454 G--NPNADDDQVWQAIKHAhlYDFVqDLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQA 531
Cdd:PRK11432 102 GlkMLGVPKEERKQRVKEA--LELV-DLAGFEDRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2261045687 532 ILAALQEIAK--GHTSLVIAHRLS-TIVDADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK11432 175 MREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
346-581 |
2.69e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 98.00 E-value: 2.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 346 QAKELNIGDG-TISFKDVRFEYDPSR-PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS----- 418
Cdd:PRK10261 3 HSDELDARDVlAVENLNIAFMQEQQKiAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 419 -----VNIKTVTQQSLRK----HMGIVPQDTVLFNDSIF-------ENIRYGNPNADDDQVWQAIKhahLYDFVQdLPkK 482
Cdd:PRK10261 83 rsrqvIELSEQSAAQMRHvrgaDMAMIFQEPMTSLNPVFtvgeqiaESIRLHQGASREEAMVEAKR---MLDQVR-IP-E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 483 EQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAAL----QEIAKGhtSLVIAHRLSTIVD- 557
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvlqKEMSMG--VIFITHDMGVVAEi 235
|
250 260
....*....|....*....|....
gi 2261045687 558 ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:PRK10261 236 ADRVLVMYQGEAVETGSVEQIFHA 259
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
373-569 |
2.95e-21 |
|
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: 91.34 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKT-VTQQSLRKHMGIVPQDtvlfndsifeni 451
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRrSPRDAIRAGIAYVPED------------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 452 RygnpnadddqvwqaikhaHLYDFVQDLPKKEQTVVGERglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQA 531
Cdd:cd03215 84 R------------------KREGLVLDLSVAENIALSSL---LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2261045687 532 ILAALQEIA-KGHTSLVIAHRLSTIVD-ADKIIVMHQGEI 569
Cdd:cd03215 143 IYRLIRELAdAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
370-573 |
4.34e-21 |
|
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: 91.51 E-value: 4.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNikTVTQQSLRKHMG-IVPQDTVLFNDSIF 448
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIGaLIEAPGFYPNLTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENIRYgnpnadddqvwqaikHAHLYdfvqDLPKKE-QTVVGERGLK---------LSGGEKQRVAIARTILKRPPILIFD 518
Cdd:cd03268 91 ENLRL---------------LARLL----GIRKKRiDEVLDVVGLKdsakkkvkgFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 519 EATSSLDSgseQAILAALQEI----AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03268 152 EPTNGLDP---DGIKELRELIlslrDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
370-573 |
4.35e-21 |
|
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: 91.43 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRF--YDVTSGSIEIDSVNIKTVTQQSlRKHMGIvpqdTVLFNDSI 447
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGI----FLAFQYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 fenirygnpnadddqvwqAIKHAHLYDFVQDLpkkeqtvvgerGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSG 527
Cdd:cd03217 88 ------------------EIPGVKNADFLRYV-----------NEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2261045687 528 SEQAILAALQEIAKGHTS-LVIAH--RLSTIVDADKIIVMHQGEIVETG 573
Cdd:cd03217 139 ALRLVAEVINKLREEGKSvLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
372-578 |
4.66e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIeidSVNIKTVTQQSLR-KHMGIVPQDTVLFND-SIFE 449
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI---RFHGTDVSRLHARdRKVGFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIRYG--------NPNADddqvwqAIKH--AHLYDFVQdLPKkeqtvVGER-GLKLSGGEKQRVAIARTILKRPPILIFD 518
Cdd:PRK10851 94 NIAFGltvlprreRPNAA------AIKAkvTQLLEMVQ-LAH-----LADRyPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 519 EATSSLDSGSEQAI---LAALQEIAKgHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK10851 162 EPFGALDAQVRKELrrwLRQLHEELK-FTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
34-329 |
4.99e-21 |
|
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: 93.64 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLeQVNDGLTSIIAVPVTLVLLY---GLLRFFNVILgeirdtlFGRVTERAMR 110
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDI-FVEKDLEALLLVPLAIIGLFllrGLASYLQTYL-------MAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RVGLKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISfLMRFMVFNIVPTLLE-----ILFVVAIFFHQYGLnfALITL 185
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFDRNSSGDL---ISRITNDVN-QVQNALTSALTVLVRdpltvIGLLGVLFYLDWKL--TLIAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 186 GSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELalwetarRKNRLTLFGLN 265
Cdd:cd18552 147 VVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKAN-------ERLRRLSMKIA 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 266 SGQAL-------IIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIE 329
Cdd:cd18552 220 RARALssplmelLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
357-573 |
6.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 93.26 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQS---- 428
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 429 LRKHMGIVPQ--DTVLFNDSIFENIRYGNPN---ADDDQVWQAIKHAHLYDFVQDLPKKEQtvvgergLKLSGGEKQRVA 503
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgiPKEKAEKIAAEKLEMVGLADEFWEKSP-------FELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 504 IARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
355-574 |
7.06e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.15 E-value: 7.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS----VNIKTVTQ 426
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 427 -QSLRKHMGIVPQ--DTVLFNDSIFENIRYG--NPNADDDQVWQAIkhAHLYDFVQdLPKKeqtVVGERGLKLSGGEKQR 501
Cdd:PRK13645 85 vKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYKKV--PELLKLVQ-LPED---YVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 502 VAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
360-570 |
9.92e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEY---DPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL----RKH 432
Cdd:PRK10535 8 KDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 433 MGIVPQDTVLFNDSIFENirygnpNADDDQVWQAI-KHAHLydfvqdlpKKEQTVVGERGL---------KLSGGEKQRV 502
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQ------NVEVPAVYAGLeRKQRL--------LRAQELLQRLGLedrveyqpsQLSGGQQQRV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 503 AIARTILKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVDADKIIVMHQGEIV 570
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-573 |
1.00e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 91.90 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRpILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDV-----TSGSIEIDSVNIKTVTQQSLRK 431
Cdd:PRK14247 4 IEIRDLKVSFGQVE-VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 432 HMGIVPQ-DTVLFNDSIFENIRYG--------NPNADDDQVWQAIKHAHLYDFVQDLpkkeqtvVGERGLKLSGGEKQRV 502
Cdd:PRK14247 83 RVQMVFQiPNPIPNLSIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEVKDR-------LDAPAGKLSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 503 AIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAH------RLStivdaDKIIVMHQGEIVETG 573
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
370-573 |
1.19e-20 |
|
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: 91.05 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvNIKTVtqqsLRKHMGIVPQDTVLfndsifE 449
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL----LGLGGGFNPELTGR------E 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIR-----YGNPNADDDQVWQAIKH-AHLYDFVqDLPKKEqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSS 523
Cdd:cd03220 104 NIYlngrlLGLSRKEIDEKIDEIIEfSELGDFI-DLPVKT----------YSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 524 LDSGSEQAILAALQEIAKGHTSLVIA-HRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
356-581 |
1.63e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:PRK09536 3 MIDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVL-FNDSIFENIRYG-NPN---------ADDDQVWQAIKHAHLYDFVqDLPKKEqtvvgerglkLSGGEKQRVAI 504
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVEMGrTPHrsrfdtwteTDRAAVERAMERTGVAQFA-DRPVTS----------LSGGERQRVLL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 505 ARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVLTA 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
376-579 |
1.64e-20 |
|
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: 93.25 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL----RKHMGIVPQDTVLFND-SIFEN 450
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 451 IRYG-------NPNADDDQVWQAIKHAHLydfVQDLPKKeqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSS 523
Cdd:TIGR02142 96 LRYGmkrarpsERRISFERVIELLGIGHL---LGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 524 LDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
373-576 |
1.88e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.38 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDV-----TSGSIEIDSVNI--KTVTQQSLRKHMGIVPQDTVLFND 445
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 446 SIFENIRYGnPNAD------DDQVWQAIKHAHLYDFVQDLPKkeqtvvgERGLKLSGGEKQRVAIARTILKRPPILIFDE 519
Cdd:PRK14243 106 SIYDNIAYG-ARINgykgdmDELVERSLRQAALWDEVKDKLK-------QSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 520 ATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQ 576
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRY 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
329-567 |
1.99e-20 |
|
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: 96.13 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 329 EKMFELLErvpKVTDKKQAKELNIGDGTISFKDVRFEydpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYD 408
Cdd:TIGR01271 404 EGIGELFE---KIKQNNKARKQPNGDDGLFFSNFSLY---VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELE 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 409 VTSGSIeidsvniktvtqqslrKHMGIV---PQDTVLFNDSIFENIRYGnPNADDDQVWQAIKHAHLYDFVQDLPKKEQT 485
Cdd:TIGR01271 478 PSEGKI----------------KHSGRIsfsPQTSWIMPGTIKDNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKT 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 486 VVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAIL-AALQEIAKGHTSLVIAHRLSTIVDADKIIVM 564
Cdd:TIGR01271 541 VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLL 620
|
...
gi 2261045687 565 HQG 567
Cdd:TIGR01271 621 HEG 623
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
357-573 |
2.21e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.17 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSrPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVtqQSLRKHMGIV 436
Cdd:PRK11000 4 VTLRNVTKAYGDV-VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLF-NDSIFENIRYGN--PNADDDQVWQAIKH-------AHLYDfvqDLPKKeqtvvgerglkLSGGEKQRVAIAR 506
Cdd:PRK11000 81 FQSYALYpHLSVAENMSFGLklAGAKKEEINQRVNQvaevlqlAHLLD---RKPKA-----------LSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 507 TILKRPPILIFDEATSSLDsgseqailAALQ-----EIAKGH-----TSLVIAH-RLSTIVDADKIIVMHQGEIVETG 573
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLD--------AALRvqmriEISRLHkrlgrTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
357-574 |
2.55e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 91.69 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPI----LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ------ 426
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 427 ------------------QSLRKHMGIVPQ--DTVLF-----NDSIFENIRYGNPNAdddqvwQAIKHAHLYDFVQDLPk 481
Cdd:PRK13651 83 vleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFeqtieKDIIFGPVSMGVSKE------EAKKRAAKYIELVGLD- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 482 keQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-AD 559
Cdd:PRK13651 156 --ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVLEwTK 233
|
250
....*....|....*
gi 2261045687 560 KIIVMHQGEIVETGN 574
Cdd:PRK13651 234 RTIFFKDGKIIKDGD 248
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
370-579 |
2.60e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.84 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFND-SIF 448
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENIRYG-NP--------NADDDQ-VWQAIKHAHLYDFVQdlpkkeqtvvgERGLKLSGGEKQRVAIARTILKRPPILIFD 518
Cdd:PRK11231 95 ELVAYGrSPwlslwgrlSAEDNArVNQAMEQTRINHLAD-----------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 519 EATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
357-551 |
3.49e-20 |
|
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: 87.98 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIdsvniktvtqqSLRKHMGIV 436
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFNDSIFENIRYgnPnadddqvWQAIkhahlydfvqdlpkkeqtvvgerglkLSGGEKQRVAIARTILKRPPILI 516
Cdd:cd03223 70 PQRPYLPLGTLREQLIY--P-------WDDV--------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 2261045687 517 FDEATSSLDSGSEQAILAALQEiaKGHTSLVIAHR 551
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
373-578 |
4.37e-20 |
|
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: 88.97 E-value: 4.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQsLRKHMGIVPQDTVLFND-SIFENI 451
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 452 R-----YGNPNADDDQvwqaiKHAHLYDFVQDLPKKEQTVVgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDS 526
Cdd:cd03265 95 YiharlYGVPGAERRE-----RIDELLDFVGLLEAADRLVK-----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 527 GSEQAILAALQEIAKGH--TSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
357-574 |
4.47e-20 |
|
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: 93.71 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRpILKGINFTINSGEKLAVVGESGSGKSTLVKLL--FRFYDVTSGSI-------------------- 414
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 415 -------------EIDSVNIKTVTQQSLRKHMGIVPQDTVLF--NDSIFENIRYGNPNAD---DDQVWQAIKhahLYDFV 476
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGyegKEAVGRAVD---LIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 477 QdLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLST 554
Cdd:TIGR03269 157 Q-LSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEV 231
|
250 260
....*....|....*....|.
gi 2261045687 555 IVD-ADKIIVMHQGEIVETGN 574
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGT 252
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-331 |
4.95e-20 |
|
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: 90.65 E-value: 4.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAkvAIVGL--PFILKEIVDS-LEQVNDGLTSIIAVPVTLVLLygLLRFFNVILGEIRDTLFGRVTERAMR 110
Cdd:cd18563 1 LILGFLLMLLG--TALGLvpPYLTKILIDDvLIQLGPGGNTSLLLLLVLGLA--GAYVLSALLGILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RVGLKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFMVFNIVPTLLEILFVVAIFFHQYGLNF--ALITLgsi 188
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSL---MSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWklALLVL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 vLYIGFTAYATEWRTKYIREA--NQADSSS--NSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGL 264
Cdd:cd18563 151 -IPVPLVVWGSYFFWKKIRRLfhRQWRRWSrlNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 265 NSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKM 331
Cdd:cd18563 230 FPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
357-568 |
6.09e-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: 86.35 E-value: 6.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVniktvtqqslrkhmgiv 436
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 pqdtvlfndsifenirygnpnadddqvwqaIKHAHLydfvqdlpkkEQtvvgerglkLSGGEKQRVAIARTILKRPPILI 516
Cdd:cd03221 63 ------------------------------VKIGYF----------EQ---------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 517 FDEATSSLDSGSEQAILAALQEiaKGHTSLVIAH-R--LSTIvdADKIIVMHQGE 568
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
376-579 |
6.75e-20 |
|
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: 91.32 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKL---LFRfydVTSGSIEIDSvnikTVTQQSLRK--------HMGIVPQDTVLFN 444
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGG----EVLQDSARGiflpphrrRIGYVFQEARLFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 445 D-SIFENIRYGnpnadddqVWQAIKHAHLYDFVQdlpkkeqtVVGERGL---------KLSGGEKQRVAIARTILKRPPI 514
Cdd:COG4148 91 HlSVRGNLLYG--------RKRAPRAERRISFDE--------VVELLGIghlldrrpaTLSGGERQRVAIGRALLSSPRL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 515 LIFDEATSSLDSGSEQAILAALQEIAKgHTSLVI---AH------RLstivdADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG4148 155 LLMDEPLAALDLARKAEILPYLERLRD-ELDIPIlyvSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
357-575 |
9.06e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.39 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQS---LRKHM 433
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTVLFND-SIFENIRY----GNPNADD--DQVWQAIKHAHLYDFVQDLPkkeqtvvgergLKLSGGEKQRVAIAR 506
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAIpliiAGASGDDirRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 507 TILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVDAD-KIIVMHQGEIveTGNH 575
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHL--HGGV 219
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
372-579 |
1.18e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.87 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ-------------QSLRKHMGIVPQ 438
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 DTVLFND-SIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKEQtvvGERGLKLSGGEKQRVAIARTILKRPPILIF 517
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQ---GKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 518 DEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
372-573 |
2.07e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.52 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVK-----LLFRFYDVTSGSIEI----------DSVNIKTVTQ-QSLRKHMGI 435
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIgdkknnheliTNPYSKKIKNfKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQ--DTVLFNDSIFENIRYGnPNADDDQVWQAIKHA--HL------YDFVQDLPkkeqtvvgergLKLSGGEKQRVAIA 505
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAkfYLnkmgldDSYLERSP-----------FGLSGGQKRRVAIA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK13631 189 GILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
371-573 |
2.34e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 91.27 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 371 PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQqSLRKHMGI--VPQDTVLF-NDSI 447
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGIylVPQEPLLFpNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FENIRYGNPNADDDQvwqaikhahlydfvqdlpKKEQTVVGERG--LKLSG-------GEKQRVAIARTILKRPPILIFD 518
Cdd:PRK15439 104 KENILFGLPKRQASM------------------QKMKQLLAALGcqLDLDSsagslevADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 519 EATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSG 222
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
368-572 |
2.43e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.21 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 368 PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNI---KTVTQQSLRKHMGIVPQDTV-LF 443
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQDSIsAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 N------DSIFENIRYgnpNADDDQVWQAIKHAHLYDFVqDLPkkeQTVVGERGLKLSGGEKQRVAIARTILKRPPILIF 517
Cdd:PRK10419 103 NprktvrEIIREPLRH---LLSLDKAERLARASEMLRAV-DLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 518 DEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLStIVD--ADKIIVMHQGEIVET 572
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLR-LVErfCQRVMVMDNGQIVET 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
374-578 |
2.76e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 89.38 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 374 KGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI---DSVNIKTVTQQSLRKHMGIVPQD---------TV 441
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDplaslnprmTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 442 lfNDSIFENIRYGNPNADDDQVWQAIKHAHLYdfVQDLPKkeqtVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEAT 521
Cdd:PRK15079 118 --GEIIAEPLRTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 522 SSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK15079 190 SALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
370-570 |
3.36e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.85 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTVtQQSLRKHMGIVPQD----TVLF 443
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgkPVRIRSP-RDAIRAGIAYVPEDrkgeGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 NDSIFENI---------RYG--NPNADDDQVWQAIKhahlydfvqDL----PKKEQTVVgerglKLSGGEKQRVAIARTI 508
Cdd:COG1129 344 DLSIRENItlasldrlsRGGllDRRRERALAEEYIK---------RLriktPSPEQPVG-----NLSGGNQQKVVLAKWL 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIV 570
Cdd:COG1129 410 ATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAeGKAVIVISSELPELLGlSDRILVMREGRIV 473
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
37-330 |
4.23e-19 |
|
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: 88.00 E-value: 4.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSLEQVNDG--LTSIIAVPVTLVLLYGLLRFFnvilgeiRDTLFGRVTERAMRRVGL 114
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLdvLNELALILLAIYLLQSVFTFV-------RYYLFNIAGERIVARLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 115 KLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFMVFNIVPTLLEILFVVA----IFFHQYGLnfALITLGSIVL 190
Cdd:cd18557 74 DLFSSLLRQEIAFFDKHKTGEL---TSRLSSDTSVLQSAVTDNLSQLLRNILQVIGgliiLFILSWKL--TLVLLLVIPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 191 YIGFTAY---ATEWRTKYIREAnQADSSSNsrAIDSLLNYETVKYFNNEQYESQRYDEELA-LWETARRKNRLTLFgLNS 266
Cdd:cd18557 149 LLIASKIygrYIRKLSKEVQDA-LAKAGQV--AEESLSNIRTVRSFSAEEKEIRRYSEALDrSYRLARKKALANAL-FQG 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 267 GQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEK 330
Cdd:cd18557 225 ITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASER 288
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
369-574 |
7.63e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 86.23 E-value: 7.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRF--YDVTSGSIEIDSVNIKTVTQQsLRKHMGivpqdtvlfnds 446
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLG------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 447 IFENIRY-----GNPNAD-------DDQVWQAIKHAHLYDFVQDLPKKEQTV----------VGErglKLSGGEKQRVAI 504
Cdd:CHL00131 86 IFLAFQYpieipGVSNADflrlaynSKRKFQGLPELDPLEFLEIINEKLKLVgmdpsflsrnVNE---GFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 505 ARTILKRPPILIFDEATSSLDsgseqaiLAALQEIAKGHTSL--------VIAH--RLSTIVDADKIIVMHQGEIVETGN 574
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLD-------IDALKIIAEGINKLmtsensiiLITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
376-578 |
7.66e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.74 E-value: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTqqSLRKHMGIVPQDTVLF-NDSIFENIRYG 454
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 455 -----NPNAD-DDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGS 528
Cdd:PRK11607 116 lkqdkLPKAEiASRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 529 EQAILAALQEIAK--GHTSLVIAH-RLSTIVDADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK11607 185 RDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-579 |
8.71e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 8.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 364 FEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSV------NIKTVTQQSLRKHMGIVP 437
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 438 QDTVLF-NDSIFENIRY--GNPNADDDQVWQAIKHAHLYDFvqDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPI 514
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYplKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 515 LIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
341-579 |
1.14e-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: 89.48 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 341 VTDKKQAKELNIGDGTISFKDV-RFEYDPSRPILK---GINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIE- 415
Cdd:TIGR03269 264 VSEVEKECEVEVGEPIIKVRNVsKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNv 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 416 ------IDSVNIKTVTQQSLRKHMGIVPQDTVLF-NDSIFENIR--YGNPNADDDQVWQAIKHAHLYDFVQdlpKKEQTV 486
Cdd:TIGR03269 344 rvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNLTeaIGLELPDELARMKAVITLKMVGFDE---EKAEEI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 487 VGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSE----QAILAALQEIakGHTSLVIAHRLSTIVD-ADKI 561
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMDFVLDvCDRA 498
|
250
....*....|....*...
gi 2261045687 562 IVMHQGEIVETGNHQQLL 579
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEIV 516
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
351-573 |
1.18e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 351 NIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIdsvnIKTVTQQSLR 430
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 KHM-GIVPQDT-------VLFNDSIFENiRYGN------PNADDDQ-VWQAIKHAHLYDFvqdlpKKEQtvVGErglkLS 495
Cdd:PRK15056 77 KNLvAYVPQSEevdwsfpVLVEDVVMMG-RYGHmgwlrrAKKRDRQiVTAALARVDMVEF-----RHRQ--IGE----LS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 496 GGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETG 573
Cdd:PRK15056 145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
321-579 |
1.19e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 321 IKGSLANIEKMF-ELLERVPKVTDKKQAKELNIGDGTISFKdvrfeydpsrpiLKGINFTINSGEKLAVVGESGSGKSTL 399
Cdd:PRK10070 3 IKLEIKNLYKIFgEHPQRAFKYIEQGLSKEQILEKTGLSLG------------VKDASLAIEEGEIFVIMGLSGSGKSTM 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 400 VKLLFRFYDVTSGSIEIDSVNIKTVTQQSLR-----------KHMGIVPQDTVLfNDSIFENIRYGNPNAD-DDQVWQAI 467
Cdd:PRK10070 71 VRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTVL-DNTAFGMELAGINAEErREKALDAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 468 KHAHLYDFVQDLPKkeqtvvgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGH--TS 545
Cdd:PRK10070 150 RQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHqrTI 218
|
250 260 270
....*....|....*....|....*....|....*
gi 2261045687 546 LVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK10070 219 VFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
369-569 |
2.40e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.14 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVT-QQSL----------RKHMGIVP 437
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLangivyisedRKRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 438 QDTVLFNDSI-----FENiRYGNPNADDDQvwQAIKhahlyDFVQ----DLPKKEQTVvgerGLkLSGGEKQRVAIARTI 508
Cdd:PRK10762 344 GMSVKENMSLtalryFSR-AGGSLKHADEQ--QAVS-----DFIRlfniKTPSMEQAI----GL-LSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTS--LVIAHRLSTIVDADKIIVMHQGEI 569
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSiiLVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
370-544 |
2.48e-18 |
|
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: 83.70 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFE 449
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIRYGNPNADDDQVWQAIKHAHLYDFvQDLPKKEqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSE 529
Cdd:cd03231 93 NLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170
....*....|....*
gi 2261045687 530 qailAALQEIAKGHT 544
Cdd:cd03231 162 ----ARFAEAMAGHC 172
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
356-578 |
3.10e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 88.11 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGI 435
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFnDSIFENiryGNPNADDDQVWQAIKHAHLYDFVqdlpkkeqTVVGER--GLKLSGGEKQRVAIARTILKRPP 513
Cdd:PRK10522 402 VFTDFHLF-DQLLGP---EGKPANPALVEKWLERLKMAHKL--------ELEDGRisNLKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 514 ILIFDEATSSLDSGSE----QAILAALQEiaKGHTSLVIAHRLSTIVDADKIIVMHQGEIVE-TGNHQQL 578
Cdd:PRK10522 470 ILLLDEWAADQDPHFRrefyQVLLPLLQE--MGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDA 537
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
34-317 |
3.40e-18 |
|
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: 85.23 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLeqVNDGLTSIIAVPVTLVLLYGLLRFfnvILGEIRDTLFGRVT---ERAMR 110
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGP--IAHGDRSALWPLVLLLLALGVAEA---VLSFLRRYLAGRLSlgvEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RvglKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFMVF--NIVPTLLEILFVVAIFFHQYGLnFALITLGSI 188
Cdd:cd18543 76 T---DLFAHLQRLDGAFHDRWQSGQL---LSRATSDLSLVQRFLAFgpFLLGNLLTLVVGLVVMLVLSPP-LALVALASL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 VLyIGFTAYAteWRTKYI---REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEEL-ALWETARRKNRLTLFgL 264
Cdd:cd18543 149 PP-LVLVARR--FRRRYFpasRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAArRLRATRLRAARLRAR-F 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 265 NSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFV 317
Cdd:cd18543 225 WPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWL 277
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
35-315 |
3.47e-18 |
|
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: 85.64 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 35 VLALICLVLAKVAIVGLPFILKEIVDS---------LEQVNDGLTS----IIAVPVTLVLLYGLLRffnVILGEIRDTLF 101
Cdd:cd18564 2 ALALLALLLETALRLLEPWPLKVVIDDvlgdkplpgLLGLAPLLGPdplaLLLLAAAALVGIALLR---GLASYAGTYLT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 102 GRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFMV---FNIVPTLLEILFVVAIFFHqygL 178
Cdd:cd18564 79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDL---LSRLTGDVGAIQDLLVsgvLPLLTNLLTLVGMLGVMFW---L 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 179 N--FALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEE-LALWETARR 255
Cdd:cd18564 153 DwqLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAREnRKSLRAGLR 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 256 KNRLTlFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLG 315
Cdd:cd18564 233 AARLQ-ALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLA 291
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
359-525 |
4.51e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 4.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 359 FKDVRFEYdPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIdsvniktvtQQSLRkhMGIVPQ 438
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 DTVLFND-SIFENIRYGNP-----------------NADDD-----QVWQAIKHAHLYDFVQDLpkkeQTVVGERGLK-- 493
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGDAelraleaeleeleaklaEPDEDlerlaELQEEFEALGGWEAEARA----EEILSGLGFPee 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2261045687 494 --------LSGGEKQRVAIARTILKRPPILIFDEATSSLD 525
Cdd:COG0488 145 dldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
373-581 |
5.07e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 84.46 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID------------SVNIKTVTQQ---SL--RKHMGI 435
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfgdysyrSQRIRMIFQDpstSLnpRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVqdlpkkeqtvvgerglkLSGGEKQRVAIARTILKRPPIL 515
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHM-----------------LAPGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 516 IFDEATSSLD-SGSEQAI--LAALQEiAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:PRK15112 172 IADEALASLDmSMRSQLInlMLELQE-KQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLAS 240
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
372-553 |
5.15e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSI--EIDSVN-IKTVTQQSLRKH-MGIVPQDTVLFND-S 446
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifNGQPMSkLSSAAKAELRNQkLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 447 IFENIRY----GNPNADddqvwQAIKHAHLYDFVQDLPKKEQtvvgERGLKLSGGEKQRVAIARTILKRPPILIFDEATS 522
Cdd:PRK11629 104 ALENVAMplliGKKKPA-----EINSRALEMLAAVGLEHRAN----HRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|...
gi 2261045687 523 SLDSGSEQAILAALQEI--AKGHTSLVIAHRLS 553
Cdd:PRK11629 175 NLDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
336-570 |
6.89e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 336 ERVPKVTDKKQAKelnIGDGTISFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIE 415
Cdd:COG3845 240 REVLLRVEKAPAE---PGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 416 IDSVNIKTVTQQSLRKH-MGIVPQD-----TVLfNDSIFENI---RYGNPNAdddQVWQAIKHAHLYDFVQDL------- 479
Cdd:COG3845 317 LDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP-DMSVAENLilgRYRRPPF---SRGGFLDRKAIRAFAEELieefdvr 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 480 PKKEQTVVGerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVD- 557
Cdd:COG3845 393 TPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAl 468
|
250
....*....|...
gi 2261045687 558 ADKIIVMHQGEIV 570
Cdd:COG3845 469 SDRIAVMYEGRIV 481
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
369-569 |
9.53e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.19 E-value: 9.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVtqqslRKHMGIVPQDTVLFN-DSI 447
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSG 527
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLDEPLGALDAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2261045687 528 S----EQAILAALQEiaKGHTSLVIAHRLSTIVD-ADKIIVMHQGEI 569
Cdd:PRK11247 168 TriemQDLIESLWQQ--HGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
372-579 |
1.59e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 83.80 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYD----VTSGSIEIDSVNIKTVTQQSLRKHMGivpQDTVLfndsI 447
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRKIIG---REIAM----I 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FEN-IRYGNPNAD-DDQVWQAIKH----AHLYDFVQDlpKKEQTV-----VGERGLK---------LSGGEKQRVAIART 507
Cdd:COG4170 95 FQEpSSCLDPSAKiGDQLIEAIPSwtfkGKWWQRFKW--RKKRAIellhrVGIKDHKdimnsypheLTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 508 ILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTS-LVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG4170 173 IANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSiLLISHDLESISQwADTITVLYCGQTVESGPTEQIL 247
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
368-564 |
2.49e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 80.36 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 368 PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI-DSVNIKTVTQQS-LRKHMGIVPQDTV---L 442
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaGGARVAYVPQRSeVPDSLPLTVRDLVamgR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 443 FNdsifENIRYGNPNADDDQ-VWQAIKHAHLYDFvqdlpkkEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEAT 521
Cdd:NF040873 83 WA----RRGLWRRLTRDDRAaVDDALERVGLADL-------AGRQLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2261045687 522 SSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVDADKIIVM 564
Cdd:NF040873 148 TGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
368-570 |
3.87e-17 |
|
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: 80.00 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 368 PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLL---FRFYDVTSGSIEIDSVNIKTVTQQslrkhmgivPQDTVLFN 444
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEK---------YPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 445 dsifenirygnpNADDdqvwqaIKHAHL-----YDFVQDLpKKEQTVvgeRGLklSGGEKQRVAIARTILKRPPILIFDE 519
Cdd:cd03233 89 ------------SEED------VHFPTLtvretLDFALRC-KGNEFV---RGI--SGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 520 ATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLS-TIVDA-DKIIVMHQGEIV 570
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADvlKTTTFVSLYQASdEIYDLfDKVLVLYEGRQI 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
373-571 |
4.41e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 80.59 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvniKTVTQQSlrkhmgivPQDTVLFND------- 445
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEPG--------PDRMVVFQNysllpwl 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 446 SIFENIRYgnpnadddqvwqAIKHAhlydfVQDLPKKEQTVVGERGL--------------KLSGGEKQRVAIARTILKR 511
Cdd:TIGR01184 70 TVRENIAL------------AVDRV-----LPDLSKSERRAIVEEHIalvglteaadkrpgQLSGGMKQRVAIARALSIR 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 512 PPILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRL-STIVDADKIIVM------HQGEIVE 571
Cdd:TIGR01184 133 PKVLLLDEPFGALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLtngpaaNIGQILE 201
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
372-573 |
4.56e-17 |
|
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: 80.02 E-value: 4.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQslrkHMGIVPQDTVLFND-SIFEN 450
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLPEERGLYPKmKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 451 IRY-----G-NPNADDDQVWQAIKHAHLYDfvqdlpKKEQTVVgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSL 524
Cdd:cd03269 91 LVYlaqlkGlKKEEARRRIDEWLERLELSE------YANKRVE-----ELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 525 DSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03269 160 DPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
370-546 |
4.91e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.92 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIkTVTQQSLRKHMgIVPQDTVLFNDSIFE 449
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDPDVAEACHY-LGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIR-----YGNPNADDDQVWQAIKHAHlydfVQDLPKKEqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSL 524
Cdd:PRK13539 93 NLEfwaafLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180 190
....*....|....*....|....*....|
gi 2261045687 525 DSGSEQAILAALQE--------IAKGHTSL 546
Cdd:PRK13539 159 DAAAVALFAELIRAhlaqggivIAATHIPL 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
366-581 |
5.35e-17 |
|
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: 84.11 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 366 YDPSRPILKGIN---FTINSGEKLAVVGESGSGKSTLVKLLFRFYD-VTSGSIEIDS--VNIKTvTQQSL---------- 429
Cdd:TIGR02633 266 WDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRN-PAQAIragiamvped 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMGIVPQDTVLFNDSI-----FENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPkkeqtvVGerglKLSGGEKQRVAI 504
Cdd:TIGR02633 345 RKRHGIVPILGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP------IG----RLSGGNQQKAVL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 505 ARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVD-ADKIIVMHQGEI----VETGNHQQL 578
Cdd:TIGR02633 415 AKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKLkgdfVNHALTQEQ 494
|
...
gi 2261045687 579 LLA 581
Cdd:TIGR02633 495 VLA 497
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
373-579 |
5.66e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLvklLFRFYDVTS--GSIEIDSVNIKTVTQQSLRKHMGIVPQDTV-LFNDSIFE 449
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTL---LARMAGLLPgqGEILLNGRPLSDWSAAELARHRAYLSQQQSpPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIR-YGNPNADDDQVWQAIkhAHLYDFVQDLPKKEQTVVgerglKLSGGEKQRVAIARTILKRPP-------ILIFDEAT 521
Cdd:COG4138 89 YLAlHQPAGASSEAVEQLL--AQLAEALGLEDKLSRPLT-----QLSGGEWQRVRLAAVLLQVWPtinpegqLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 522 SSLDSGSEQAILAALQEIA-KGHTSLVIAHRLS-TIVDADKIIVMHQGEIVETGNHQQLL 579
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
361-594 |
5.70e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.22 E-value: 5.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 361 DVRFEYDPsRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDsvniktvtqqslrKHMGIVPQDT 440
Cdd:PTZ00243 665 DDFFELEP-KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 441 VLFNDSIFENIRYGNPNaDDDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:PTZ00243 731 WIMNATVRGNILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 521 TSSLDS--GS---EQAILAALqeiaKGHTSLVIAHRLSTIVDADKIIVMHQGEIVETGNHQQlLLANGRYAKMWAMQQD 594
Cdd:PTZ00243 810 LSALDAhvGErvvEECFLGAL----AGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKE 883
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-573 |
6.10e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.66 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 366 YDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVT-----SGSIEIDSVNIKT--VTQQSLRKHMGIVPQ 438
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEVRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 DTVLF-NDSIFENIRYG--------NPNADDDQVWQAIKHAHLYDFVQDLPKKEQTvvgerglKLSGGEKQRVAIARTIL 509
Cdd:PRK14267 93 YPNPFpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
367-573 |
1.11e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 367 DPSRPILKGINFTINSGEKLAVVGESGSGKS----TLVKLLFRFYDVTSGSIEIDSvniKTVTQQSLR-KHMGIVPQDT- 440
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCALRgRKIATIMQNPr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 441 VLFN------DSIFENIRYGNPNADDDQVWQAIKHAHLYDfvqdlpkkEQTVVGERGLKLSGGEKQRVAIARTILKRPPI 514
Cdd:PRK10418 90 SAFNplhtmhTHARETCLALGKPADDATLTAALEAVGLEN--------AARVLKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 515 LIFDEATSSLDSGSEQAILAALQEIAKGHTS--LVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
369-578 |
1.43e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 80.19 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL---RKHMGIVPQDTVLFND 445
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 446 -SIFENIRYgnPNADDDQVWQAIKHAHLydfvqdLPKKEqtVVGERGL------KLSGGEKQRVAIARTILKRPPILIFD 518
Cdd:PRK11831 99 mNVFDNVAY--PLREHTQLPAPLLHSTV------MMKLE--AVGLRGAaklmpsELSGGMARRAALARAIALEPDLIMFD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 519 EATSSLDSGSEQAILAALQEI--AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK11831 169 EPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
358-574 |
1.88e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 78.97 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 358 SFKDVRFEYDPSRP----ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID-------SVNiktvtq 426
Cdd:COG1134 23 SLKELLLRRRRTRReefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNgrvsallELG------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 427 qslrkhMGIVPQDTVLfndsifENIR-----YGNPNADDDQVWQAIKH-AHLYDFVqDLPKKeqtvvgerglKLSGGEKQ 500
Cdd:COG1134 97 ------AGFHPELTGR------ENIYlngrlLGLSRKEIDEKFDEIVEfAELGDFI-DQPVK----------TYSSGMRA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 501 RVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIA-HRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:COG1134 154 RLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
35-317 |
2.21e-16 |
|
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: 79.76 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 35 VLALICLVLAKVAIVGLPFILKEIVDSLEQVN---DGLTSIIAVPVTLVLLYGLLRFFNvilgeiRDTLFG--RVTERAM 109
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTltaSQLLRYALLILLLALLIGIFRFLW------RYLIFGasRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 110 RRvglKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFM---VFNIVPTLLEILFVVAIFFHqygLNFALiTLG 186
Cdd:cd18541 76 RN---DLFAHLLTLSPSFYQKNRTGDL---MARATNDLNAVRMALgpgILYLVDALFLGVLVLVMMFT---ISPKL-TLI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 187 SIVLYIgFTAYATEWRTKYI----REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELalwETARRKNrLTLF 262
Cdd:cd18541 146 ALLPLP-LLALLVYRLGKKIhkrfRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLN---EEYVEKN-LRLA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 263 GLNS--GQALIIASAMTSMLLLAANG--VVAKEMTLGDFVLINAFMMQLFMPLNFLGFV 317
Cdd:cd18541 221 RVDAlfFPLIGLLIGLSFLIVLWYGGrlVIRGTITLGDLVAFNSYLGMLIWPMMALGWV 279
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-579 |
2.73e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.26 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 351 NIGDGTISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTvTQQSLR 430
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 KHMGIVPQ-DTVLFNDSIFENI----RYGNPNADddQVWQAIkhAHLYDFVQdLPKKEQTVVGErglkLSGGEKQRVAIA 505
Cdd:PRK13536 114 ARIGVVPQfDNLDLEFTVRENLlvfgRYFGMSTR--EIEAVI--PSLLEFAR-LESKADARVSD----LSGGMKRRLTLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAALQE-IAKGHTSLVIAH------RLstivdADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHfmeeaeRL-----CDRLCVLEAGRKIAEGRPHAL 259
|
.
gi 2261045687 579 L 579
Cdd:PRK13536 260 I 260
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
370-571 |
3.72e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 3.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDsvniktvtqqslrkhmgiVPQDTVLFNDSIFE 449
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIrygNPNADDDQVWQAIKHAHLYDFVQDL-PKKEqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGS 528
Cdd:COG2401 105 AI---GRKGDFKDAVELLNAVGLSDAVLWLrRFKE----------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2261045687 529 EQAILAALQEIAK--GHTSLVIAHRlSTIVDA---DKIIVMHQGEIVE 571
Cdd:COG2401 172 AKRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
350-573 |
4.10e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.79 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 350 LNIGDGTISFKDvrfEYDPSRPILKgINFTINSGEKLAVVGESGSGKSTLVKLLFRFYD----VTSGSIEIDSVNIKTVT 425
Cdd:PRK11022 4 LNVDKLSVHFGD---ESAPFRAVDR-ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 426 QQSLRKHMG----IVPQD---------TVLFNdsIFENIRygnpnadddqVWQAIKHAHLYDFVQDLpkkeQTVVG---- 488
Cdd:PRK11022 80 EKERRNLVGaevaMIFQDpmtslnpcyTVGFQ--IMEAIK----------VHQGGNKKTRRQRAIDL----LNQVGipdp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 489 ERGL-----KLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLV-IAHRLSTIVD-ADK 560
Cdd:PRK11022 144 ASRLdvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVlITHDLALVAEaAHK 223
|
250
....*....|...
gi 2261045687 561 IIVMHQGEIVETG 573
Cdd:PRK11022 224 IIVMYAGQVVETG 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
356-572 |
5.11e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 78.37 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 356 TISFKDVRFEYDP---SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVnikTVTQQSLRKh 432
Cdd:COG4525 3 MLTVRHVSVRYPGggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 433 mGIVPQDTVLFN-DSIFENIRYGnpnadddqvwqaIKhahlydfVQDLPKKEQTVVGERGLK--------------LSGG 497
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFG------------LR-------LRGVPKAERRARAEELLAlvgladfarrriwqLSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 498 EKQRVAIARTILKRPPILIFDEATSSLDSGS-EQA---ILAALQEIAKGhtSLVIAHRL-STIVDADKIIVM--HQGEIV 570
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTrEQMqelLLDVWQRTGKG--VFLITHSVeEALFLATRLVVMspGPGRIV 216
|
..
gi 2261045687 571 ET 572
Cdd:COG4525 217 ER 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
376-573 |
5.40e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ---QSLRKHMGIVPQD---------TVlf 443
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDpyasldprqTV-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 NDSIFENIR-YGNPNADDdqvwQAIKHAHLYDFVQDLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEATS 522
Cdd:PRK10261 421 GDSIMEPLRvHGLLPGKA----AAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 523 SLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
370-567 |
5.72e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLfrfydvtSGSIEIDS------VNIKTVTQQSLRKhMGIVPQDTVLF 443
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNftgtilANNRKPTKQILKR-TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 -NDSIFENIRYGN----PNADDDQVWQAIKHAHLYDFvqDLPKKEQTVVGERGLK-LSGGEKQRVAIARTILKRPPILIF 517
Cdd:PLN03211 153 pHLTVRETLVFCSllrlPKSLTKQEKILVAESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 518 DEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDA--DKIIVMHQG 567
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQmfDSVLVLSEG 283
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
350-581 |
9.82e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 350 LNIGDGTISFKdvrfEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRF-------YdvTSGSIEIDSVNIK 422
Cdd:PRK15134 6 LAIENLSVAFR----QQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvY--PSGDIRFHGESLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 423 TVTQQSLRKHMG-----IVPQDTVLFND------------SIFENIRYGNPNADD----DQVwqAIKHA--HLYDFVQdl 479
Cdd:PRK15134 80 HASEQTLRGVRGnkiamIFQEPMVSLNPlhtlekqlyevlSLHRGMRREAARGEIlnclDRV--GIRQAakRLTDYPH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 480 pkkeqtvvgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLStIVD 557
Cdd:PRK15134 156 -------------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS-IVR 221
|
250 260
....*....|....*....|....*.
gi 2261045687 558 --ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:PRK15134 222 klADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
376-574 |
9.95e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.76 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI-DSVNIKTVTQQSL---RKHMGIVPQDTVLF-NDSIFEN 450
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLnGRVLFDAEKGICLppeKRRIGYVFQDARLFpHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 451 IRYGNPNADD---DQVWQAIKHAHLYDfvqDLPkkeqtvvgergLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSG 527
Cdd:PRK11144 97 LRYGMAKSMVaqfDKIVALLGIEPLLD---RYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2261045687 528 SEQAILAALQEIAKGHTS--LVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:PRK11144 163 RKRELLPYLERLAREINIpiLYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
373-573 |
1.15e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQ-SLRKHMGIVPQDTVLFND-SIFEN 450
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQELSVIDElTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 451 IRYGN---------PNADddqvWQAIK-HAHLYDFVQDLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:PRK09700 101 LYIGRhltkkvcgvNIID----WREMRvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 521 TSSLDSGSEQAILAALQEIAKGHTSLV-IAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK09700 173 TSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
34-314 |
1.26e-15 |
|
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: 77.81 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDGLTSIIavpVTLVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVG 113
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGL---LLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 114 LKLFDHLHNLDLDFHLNRQTGGL-SR---DMERgtsgisflMRFMVFNIVPTLL-EILFVVAIFFHQYGLNF--ALITLG 186
Cdd:cd18544 78 RDLFSHIQRLPLSFFDRTPVGRLvTRvtnDTEA--------LNELFTSGLVTLIgDLLLLIGILIAMFLLNWrlALISLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 187 SIVLYIGFTAYAtewrTKYIREANQADSSSNSRaIDSLLN-----YETVKYFNNEQYESQRYDEELALWETARRKNRLTL 261
Cdd:cd18544 150 VLPLLLLATYLF----RKKSRKAYREVREKLSR-LNAFLQesisgMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLF 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 262 FGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFL 314
Cdd:cd18544 225 ALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDL 277
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
318-553 |
1.28e-15 |
|
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: 80.18 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 318 YREI---KGSLANIEKMFELLERV-------PKVTDKKQAKE------LNIGDGTISFKDVRFEYD------PSRPIL-K 374
Cdd:TIGR00954 390 GRDMtrlAGFTARVDTLLQVLDDVksgnfkrPRVEEIESGREggrnsnLVPGRGIVEYQDNGIKFEniplvtPNGDVLiE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 375 GINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS-VNIKTVTQqslRKHMGI-VPQDTVLFNDSIFENIR 452
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAkGKLFYVPQ---RPYMTLgTLRDQIIYPDSSEDMKR 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 453 YGNPNADDDQVWQAIKHAHL------YDFVQDLpkKEQtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDS 526
Cdd:TIGR00954 547 RGLSDKDLEQILDNVQLTHIlereggWSAVQDW--MDV---------LSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
250 260
....*....|....*....|....*..
gi 2261045687 527 GSEQAILAALQEiaKGHTSLVIAHRLS 553
Cdd:TIGR00954 616 DVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
354-579 |
1.42e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.14 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 354 DGTISFKDVRFEYdPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHM 433
Cdd:PRK10575 9 DTTFALRNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 434 GIVPQDTvlfndsifenirygnPNADDDQVWQAIK------HAHLYDF-VQDLPKKEQ--TVVGERGL------KLSGGE 498
Cdd:PRK10575 88 AYLPQQL---------------PAAEGMTVRELVAigrypwHGALGRFgAADREKVEEaiSLVGLKPLahrlvdSLSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 499 KQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIA--HRLSTIVD-ADKIIVMHQGEIVETGNH 575
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINMAARyCDYLVALRGGEMIAQGTP 232
|
....
gi 2261045687 576 QQLL 579
Cdd:PRK10575 233 AELM 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
373-578 |
1.86e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFY--DVTSGS-IEI--DSVNIKTVTQQSLRK---HMGIVPQDTVLFN 444
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELlgRTVQREGRLARDIRKsraNTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 445 D-SIFENI---------------RYGNPnADDDQVWQAIKHAHLYDFVQdlpkkeqtvvgERGLKLSGGEKQRVAIARTI 508
Cdd:PRK09984 100 RlSVLENVligalgstpfwrtcfSWFTR-EQKQRALQALTRVGMVHFAH-----------QRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQL 578
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
31-314 |
2.10e-15 |
|
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: 77.10 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 31 KSRVVLALIC-LVLAKVAIVGlPFILKEIVDSLeqVNDGLTSIIAvpvTLVLLYGLLRFFNVILGEIRDTLFGRVTERAM 109
Cdd:cd18570 1 KKLLILILLLsLLITLLGIAG-SFFFQILIDDI--IPSGDINLLN---IISIGLILLYLFQSLLSYIRSYLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 110 RRVGLKLFDHLHNLDLDFHLNRQTGG-LSR--DMERGTSGISFLMRFMVFNIVptlleILFVVAIFFHQYGLNFALITLG 186
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEiISRfnDANKIREAISSTTISLFLDLL-----MVIISGIILFFYNWKLFLITLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 187 SIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEEL-ALWETARRKNRLTLFgLN 265
Cdd:cd18570 150 IIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFsKLLKKSFKLGKLSNL-QS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2261045687 266 SGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFL 314
Cdd:cd18570 229 SIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENL 277
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
369-579 |
3.25e-15 |
|
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: 75.27 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVT-QQSLRKHMGIVPQDTVLFND-S 446
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 447 IFENIRYGNPNADDDqvwQAIKHAHLYDFVQDLpkKEQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLD- 525
Cdd:cd03218 92 VEENILAVLEIRGLS---KKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 526 -SGSE-QAILAALQEiaKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLL 579
Cdd:cd03218 167 iAVQDiQKIIKILKD--RGIGVLITDHNVRETLSiTDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
360-536 |
5.66e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 77.62 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFrfydvtsGSIEIDSVNIKtvtqQSLRKHMGIVPQD 439
Cdd:PRK15064 323 ENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVK----WSENANIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 TV--LFND-SIFENIRYGNPNADDDQVWQAIKHAHLydFVQDLPKKEQTVvgerglkLSGGEKQRVAIARTILKRPPILI 516
Cdd:PRK15064 391 HAydFENDlTLFDWMSQWRQEGDDEQAVRGTLGRLL--FSQDDIKKSVKV-------LSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180
....*....|....*....|
gi 2261045687 517 FDEATSSLDSGSEQAILAAL 536
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMAL 481
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
357-582 |
5.94e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDPSRpILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKT-VTQQSLRKHMGI 435
Cdd:PRK11614 6 LSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFND-SIFENIRYGNPNADDDQVWQAIKHahLYDFVQDLPKKEQtvvgERGLKLSGGEKQRVAIARTILKRPPI 514
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKW--VYELFPRLHERRI----QRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 515 LIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIV--ETGnhqQLLLAN 582
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVEQNANQALKlADRGYVLENGHVVleDTG---DALLAN 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
373-572 |
8.58e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 8.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTS--GSIEIDSvniKTVTQQSLR--KHMGI---------VPQD 439
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEG---EELQASNIRdtERAGIaiihqelalVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 TVLfndsifENIRYGN---PNA--DDDQVWQaiKHAHLYDFVQdLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPI 514
Cdd:PRK13549 98 SVL------ENIFLGNeitPGGimDYDAMYL--RAQKLLAQLK-LDINPATPVGN----LGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 515 LIFDEATSSLdSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVD-ADKIIVMHQGEIVET 572
Cdd:PRK13549 165 LILDEPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGRHIGT 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
372-548 |
1.20e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 73.66 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQ---SLR-KHMGIVPQDTVLFND-S 446
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPTlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 447 IFENI------RYGNPNADDDQVWQAIKHAHLYDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:PRK10584 105 ALENVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180
....*....|....*....|....*...
gi 2261045687 521 TSSLDSGSEQAILAALQEIAKGHTSLVI 548
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLI 201
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
38-311 |
1.38e-14 |
|
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: 74.46 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 38 LICLVLAKVAIVgLPFILKEIVDSLeQVNDGLTSIIAVPVTLVLLYgllrFFNVILGEIRDTLFGRVTERAMRRVGLKLF 117
Cdd:cd18588 9 LASLFLQLFALV-TPLFFQVIIDKV-LVHRSLSTLDVLAIGLLVVA----LFEAVLSGLRTYLFSHTTNRIDAELGARLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 118 DHLHNLDLDFHLNRQTGGL---SRDMERgtsgisfLMRFMVFNIVPTLLEILFVVaIFF---HQYGLNFALITLGSIVLY 191
Cdd:cd18588 83 RHLLRLPLSYFESRQVGDTvarVRELES-------IRQFLTGSALTLVLDLVFSV-VFLavmFYYSPTLTLIVLASLPLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 192 IGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRknRLTLFGLNSGQALI 271
Cdd:cd18588 155 ALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASF--KTANLSNLASQIVQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2261045687 272 IASAMTSMLLLA--ANGVVAKEMTLGDFVLINAFMMQLFMPL 311
Cdd:cd18588 233 LIQKLTTLAILWfgAYLVMDGELTIGQLIAFNMLAGQVSQPV 274
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
33-330 |
1.56e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 74.52 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 33 RVVLALICLVLAKVAIVGL--PFILKEIVDSLEQVNDGLTsiiavpvTLVLLYGLL--RFFNVILGEIRDTLFGRVTera 108
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLalPLFTQIILDRVLVHKNISL-------LNLILIGLLivGIFQILLSAVRQYLLDYFA--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 109 mRRVGLKL----FDHLHNLDLDFHLNRQTGG-LSRDMERGTsgisfLMRFMVFNIVPTLLEILFVV---AIFFHqYGLNF 180
Cdd:cd18568 71 -NRIDLSLlsdfYKHLLSLPLSFFASRKVGDiITRFQENQK-----IRRFLTRSALTTILDLLMVFiylGLMFY-YNLQL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 181 ALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLT 260
Cdd:cd18568 144 TLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 261 LFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEK 330
Cdd:cd18568 224 SIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVER 293
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
368-526 |
1.62e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.58 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 368 PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSlrkhmGIVPQDTVLFN-DS 446
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 447 IFENIRYGNPNADDDQVWQAIKHAHLYDFVqDLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDS 526
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKV-GLEGAEKRYIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
357-579 |
1.89e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSlRKHMGIV 436
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFND-SIFENIR-----YGNPNAdddQVWQAIkhAHLYDFVQdLPKKEQTVVGErglkLSGGEKQRVAIARTILK 510
Cdd:PRK13537 86 PQFDNLDPDfTVRENLLvfgryFGLSAA---AARALV--PPLLEFAK-LENKADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 511 RPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAH------RLstivdADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPHALI 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
357-525 |
2.45e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEidsvniktvTQQSLRkhMGIV 436
Cdd:PRK09544 5 VSLENVSVSFG-QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQ----DTVL-FNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFvqdlPKKeqtvvgerglKLSGGEKQRVAIARTILKR 511
Cdd:PRK09544 73 PQklylDTTLpLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDA----PMQ----------KLSGGETQRVLLARALLNR 138
|
170
....*....|....
gi 2261045687 512 PPILIFDEATSSLD 525
Cdd:PRK09544 139 PQLLVLDEPTQGVD 152
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
375-579 |
2.48e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 375 GINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS-----VNIKTVTQQSLRKHM----GIV---PQDTVL 442
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLrtewGFVhqhPRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 443 FNDSIFENI----------RYGNPNADDDQVWQAIKHAHlyDFVQDLPKKeqtvvgerglkLSGGEKQRVAIARTILKRP 512
Cdd:PRK11701 104 MQVSAGGNIgerlmavgarHYGDIRATAGDWLERVEIDA--ARIDDLPTT-----------FSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 513 PILIFDEATSSLDSgSEQAILAALQEiakghtSLVIAHRLSTIV---D-------ADKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK11701 171 RLVFMDEPTGGLDV-SVQARLLDLLR------GLVRELGLAVVIvthDlavarllAHRLLVMKQGRVVESGLTDQVL 240
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-326 |
3.26e-14 |
|
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: 73.75 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLeqVND--------GLTSIIAVPVTLVLLYGLLRFF----NVILGEIRDTLF 101
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAV--FNGeasflplvPASLGPADPRGQLWLLGGLTVAafllESLFQYLSGVLW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 102 GRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGG----LSRD---MERgtsgisFLMRFmVFNIVPTLLEILFVVAIFFh 174
Cdd:cd18565 79 RRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDlmsvLNNDvnqLER------FLDDG-ANSIIRVVVTVLGIGAILF- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 175 qyGLN--FALITLGSIVLYIGFTA-YATEWRTKYiREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWE 251
Cdd:cd18565 151 --YLNwqLALVALLPVPLIIAGTYwFQRRIEPRY-RAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 252 TARRKNRLTLFGLNSGQALIIASAMTSMLLL----AANGVVA--KEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSL 325
Cdd:cd18565 228 DANWRAIRLRAAFFPVIRLVAGAGFVATFVVggywVLDGPPLftGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAM 307
|
.
gi 2261045687 326 A 326
Cdd:cd18565 308 A 308
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
37-318 |
3.59e-14 |
|
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: 73.35 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSLEQVNDGLTSIIAVpvtlvLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKL 116
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAV-----LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 117 FDHLHNLDLDFHLNRQTGGL-SR---DMERGTSGISFLMRFMVFNIVptlleILFVVAIFFHQYGLNFALITLGSI-VLY 191
Cdd:cd18572 76 FRSLLRQDIAFFDATKTGELtSRltsDCQKVSDPLSTNLNVFLRNLV-----QLVGGLAFMFSLSWRLTLLAFITVpVIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 192 IGFTAYATeWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWET-ARRKNRLTLFGLNSGQAL 270
Cdd:cd18572 151 LITKVYGR-YYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKlSVRQALAYAGYVAVNTLL 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 271 IIASAMtSMLLLAANGVVAKEMTLGDFVlinAFM---MQLFMPLNFLGFVY 318
Cdd:cd18572 230 QNGTQV-LVLFYGGHLVLSGRMSAGQLV---TFMlyqQQLGEAFQSLGDVF 276
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
372-581 |
5.00e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 372 ILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKHMGIVPQDTVLFNDSIFENI 451
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 452 ----RYGNP-------NADDDQVWQAIKHAHLYDFVQdlpkkeQTVVgerglKLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:PRK10253 102 vargRYPHQplftrwrKEDEEAVTKAMQATGITHLAD------QSVD-----TLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 521 TSSLDSGSEQAILAALQEI--AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAPKEIVTA 234
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
360-578 |
5.41e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.22 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 360 KDVRFEY---DPSRPILKGINFTINSGEKLAVVGESGSGKS----TLVKLLFRfYDVTSGSIEIDSVNIKTVTQQSLRK- 431
Cdd:PRK09473 16 KDLRVTFstpDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKELNKl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 432 ---HMGIVPQD--TVL-----FNDSIFENI----RYGNPNADDDQVwqaikhaHLYDFVQdLP--KKEQTVVGErglKLS 495
Cdd:PRK09473 95 raeQISMIFQDpmTSLnpymrVGEQLMEVLmlhkGMSKAEAFEESV-------RMLDAVK-MPeaRKRMKMYPH---EFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 496 GGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKG-HTSLV-IAHRLSTIVD-ADKIIVMHQGEIVET 572
Cdd:PRK09473 164 GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIImITHDLGVVAGiCDKVLVMYAGRTMEY 243
|
....*.
gi 2261045687 573 GNHQQL 578
Cdd:PRK09473 244 GNARDV 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
368-569 |
6.73e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 368 PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYD-VTSGSIEIDS--VNIKTvTQQSL----------RKHMG 434
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRN-PQQAIaqgiamvpedRKRDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVLFNDSI-----FENIRYGNPNADDDQVWQAIKHAHLYDFVQDLPkkeqtvVGerglKLSGGEKQRVAIARTIL 509
Cdd:PRK13549 352 IVPVMGVGKNITLaaldrFTGGSRIDDAAELKTILESIQRLKVKTASPELA------IA----RLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 510 KRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEI 569
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-579 |
8.50e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 72.05 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 365 EYDPSRPILKGINFTINSGEKL---------------AVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSV--------NI 421
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGFAGKTvldqvsmgfparavtSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrsifNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 422 KTVTQqsLRKHMGIVPQDTVLFNDSIFENIRYGN------PNADDDQVWQA-IKHAHLYDFVQDLpkkeqtvVGERGLKL 494
Cdd:PRK14271 94 RDVLE--FRRRVGMLFQRPNPFPMSIMDNVLAGVrahklvPRKEFRGVAQArLTEVGLWDAVKDR-------LSDSPFRL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 495 SGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEG 244
|
....*.
gi 2261045687 574 NHQQLL 579
Cdd:PRK14271 245 PTEQLF 250
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
31-327 |
1.11e-13 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 71.90 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 31 KSRVVLALICLVLAKVAIVGLPFILKEIVDSLEQ-VNDGLTSIIAVPVTLVLLYGLLRFFNVILGEIRDTLfgRVteRAM 109
Cdd:cd18556 1 KLLFFSILFISLLSSILISISPVILAKITDLLTSsSSDSYNYIVVLAALYVITISATKLLGFLSLYLQSSL--RV--ELI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 110 RRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIVPTLLEILF-VVAIFFHQYGLNFALITLGSI 188
Cdd:cd18556 77 ISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLLQLIIaIVVILSSGDYFVAALFLLYAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 VLYIG---FTAYATEWRTKYIreanqaDSSSNSRAI--DSLLNYETVKYFNNEQYESQRYDEELALWETARR---KNRLT 260
Cdd:cd18556 157 LFVINntiFTKKIVSLRNDLM------DAGRKSYSLltDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQKrywKLTFK 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 261 LFGLNSGQALIIASAMTSMLLlaaNGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLAN 327
Cdd:cd18556 231 MLILNSLLNVILFGLSFFYSL---YGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSVHS 294
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
376-569 |
1.14e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTV-TQQSLRKhmGIV--PQD------------- 439
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALsTAQRLAR--GLVylPEDrqssglyldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 ----TVLFNDSIFEnIRYGNPNADDDQVWQA--IKHAHLydfvqdlpkkEQTVVGerglkLSGGEKQRVAIARTILKRPP 513
Cdd:PRK15439 360 wnvcALTHNRRGFW-IKPARENAVLERYRRAlnIKFNHA----------EQAART-----LSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEIAKGHTS-LVIAHRLSTIVD-ADKIIVMHQGEI 569
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAvLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
373-572 |
1.14e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTS--GSIEIDSvniKTVTQQSLR--KHMGIV--PQDTVLFND- 445
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EVCRFKDIRdsEALGIViiHQELALIPYl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 446 SIFENIRYGNPNA-----DddqvW-QAIKHAhlydfvQDLPKK------EQTVVGERGLklsgGEKQRVAIARTILKRPP 513
Cdd:NF040905 94 SIAENIFLGNERAkrgviD----WnETNRRA------RELLAKvgldesPDTLVTDIGV----GKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVET 572
Cdd:NF040905 160 LLILDEPTAALNEEDSAALLDLLLELkAQGITSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
373-572 |
1.20e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFY--DVTSGSIEIDSVNIKTVT-QQSLRKHMGIVPQDTVLFND-SIF 448
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENIRYGNP-------NADDDQVWQAikHAHLYDF-VQDLPKKEQtvVGERGlklsGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:TIGR02633 97 ENIFLGNEitlpggrMAYNAMYLRA--KNLLRELqLDADNVTRP--VGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 521 TSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTI-VDADKIIVMHQGEIVET 572
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVkAVCDTICVIRDGQHVAT 222
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
34-305 |
1.58e-13 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 71.47 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIvglPFILKEIVD--SLEQVNDGLTSIIAVPVTLVLlygllrfFNVILGEIRDTLFGRVTERAMRR 111
Cdd:cd18782 7 VLALSFVVQLLGLAN---PLLFQVIIDkvLVQQDLATLYVIGVVMLVAAL-------LEAVLTALRTYLFTDTANRIDLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 112 VGLKLFDHLHNLDLDFHLNRQTGGLSRDmergTSGISFLMRFMVFNIVPTLLEILFVV--AIFFHQYGLNFALITLGSIV 189
Cdd:cd18782 77 LGGTIIDHLLRLPLGFFDKRPVGELSTR----ISELDTIRGFLTGTALTTLLDVLFSViyIAVLFSYSPLLTLVVLATVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 190 LYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELAlwETARRKNRLTLFGLNSGQA 269
Cdd:cd18782 153 LQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYA--RSLGEGFKLTVLGTTSGSL 230
|
250 260 270
....*....|....*....|....*....|....*...
gi 2261045687 270 LIIASAMTSMLLL--AANGVVAKEMTLGDFVlinAFMM 305
Cdd:cd18782 231 SQFLNKLSSLLVLwvGAYLVLRGELTLGQLI---AFRI 265
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
369-573 |
1.87e-13 |
|
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: 70.05 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvNIKTVTQQSLRKHMGIV------------ 436
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVfgqktqlwwdlp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVLFNDSIFenirygnpNADDDQVWQAIkhAHLYDFVQDLPKKEQTVvgeRglKLSGGEKQRVAIARTILKRPPILI 516
Cdd:cd03267 112 VIDSFYLLAAIY--------DLPPARFKKRL--DELSELLDLEELLDTPV---R--QLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 517 FDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
36-331 |
2.35e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 71.00 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 36 LALICLV--LAKVAIVGLPFILKEIVDSL--EQVNDGLTSIIAVPVTLVLLYGLlrfFNVILGEIRDTLFGRVTERAMRR 111
Cdd:cd18555 4 LISILLLslLLQLLTLLIPILTQYVIDNVivPGNLNLLNVLGIGILILFLLYGL---FSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 112 VglklFDHLHNLDLDFHLNRQTGGLsrdMERGTSgISFLMRFMVFNIVPTLLEILFVVAIFFH--QYGLNFALITLGSIV 189
Cdd:cd18555 81 F----FEHLLKLPYSFFENRSSGDL---LFRANS-NVYIRQILSNQVISLIIDLLLLVIYLIYmlYYSPLLTLIVLLLGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 190 LYIGFTAYATewrtKYIREANQADSSSNSRA----IDSLLNYETVKYFNNEQYE----SQRYDEELalwETARRKNRLTL 261
Cdd:cd18555 153 LIVLLLLLTR----KKIKKLNQEEIVAQTKVqsylTETLYGIETIKSLGSEKNIykkwENLFKKQL---KAFKKKERLSN 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 262 FgLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLANIEKM 331
Cdd:cd18555 226 I-LNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
379-563 |
3.05e-13 |
|
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: 69.74 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 379 TINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQslrkhmgIVPQDTVLFNDSIFENIR-YGNPN 457
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQY-------IKADYEGTVRDLLSSITKdFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 458 ADDDQVWQAIKHAHLYDfvQDLPKkeqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDsgSEQAILAA-- 535
Cdd:cd03237 94 YFKTEIAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD--VEQRLMASkv 157
|
170 180 190
....*....|....*....|....*....|..
gi 2261045687 536 LQEIAKGH--TSLVIAHR--LSTIVdADKIIV 563
Cdd:cd03237 158 IRRFAENNekTAFVVEHDiiMIDYL-ADRLIV 188
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
357-575 |
3.70e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 69.43 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLF--RFYDVTSGSIEIDS---------------- 418
Cdd:PRK09580 2 LSIKDLHVSVE-DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGkdllelspedragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 419 -------VNIKTVTQQ--------SLRKHMGIVPQDTVLFNDSIFENIRygnpnadddqvwqaikhahLYDFVQDLPKKE 483
Cdd:PRK09580 81 fmafqypVEIPGVSNQfflqtalnAVRSYRGQEPLDRFDFQDLMEEKIA-------------------LLKMPEDLLTRS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 484 QTVvgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVD---ADK 560
Cdd:PRK09580 142 VNV------GFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDY 215
|
250
....*....|....*
gi 2261045687 561 IIVMHQGEIVETGNH 575
Cdd:PRK09580 216 VHVLYQGRIVKSGDF 230
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-338 |
5.25e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 69.82 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDS-LEQVNDGLTSIIAVP-VTLVLLYGLLRFFNVILgeirdtlFGRVTERAMRR 111
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDaLPQGDLGLLVLLALGmVAVAVASALLGVVQTYL-------SARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 112 VGLKLFDHLHNLDLDFHLNRQTGGL-SRdMERGTSGISFLMRFMVFNIVPTLLEILFVVAIFFhqyGLNF--ALITLGSI 188
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIqSR-LNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAML---ALDWrlALLSLVLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 VLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSL------LnyetVKYFNNEQYESQRYDEELAlwETARRKNRLTLF 262
Cdd:cd18550 150 PLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvsgalL----VKLFGREDDEAARFARRSR--ELRDLGVRQALA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 263 GLNSGQALIIASAMTSML--LLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFVYREIKGSLAniekmfeLLERV 338
Cdd:cd18550 224 GRWFFAALGLFTAIGPALvyWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLA-------LFERI 294
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
370-525 |
6.19e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 6.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRK------HMGIvpqDTVLf 443
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllylghQPGI---KTEL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 444 ndSIFENIRY---GNPNADDDQVWQAIKHAHLYDFvQDLPKKEqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:PRK13538 90 --TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEP 156
|
....*
gi 2261045687 521 TSSLD 525
Cdd:PRK13538 157 FTAID 161
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
358-528 |
6.55e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 71.50 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 358 SFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLfrfydvtSGsieIDS-VNIKTVTQQSLRkhMGIV 436
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VDKdFNGEARPQPGIK--VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 PQDTVL-FNDSIFENI-------------------RYGNPNADDDQVW--QA-----IKHAHLYDFVQDL---------P 480
Cdd:TIGR03719 74 PQEPQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDADFDKLAaeQAelqeiIDAADAWDLDSQLeiamdalrcP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2261045687 481 KKEQTVVgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGS 528
Cdd:TIGR03719 154 PWDADVT-----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
363-573 |
6.80e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 363 RFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLL----FRFYDVTSGSIEIDSVniktvTQQSLRKHM-GIV- 436
Cdd:TIGR00956 67 KFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGI-----TPEEIKKHYrGDVv 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 437 ---------PQDTVlfNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQ---DLPKKEQTVVGE---RGLklSGGEKQR 501
Cdd:TIGR00956 142 ynaetdvhfPHLTV--GETLDFAARCKTPQNRPDGVSREEYAKHIADVYMatyGLSHTRNTKVGNdfvRGV--SGGERKR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 502 VAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK--GHTSLVIAHRLSTivDA----DKIIVMHQGEIVETG 573
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANilDTTPLVAIYQCSQ--DAyelfDKVIVLYEGYQIYFG 293
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
35-310 |
1.17e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 69.04 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 35 VLALICLVLAKVAIVGLPFILKEIVDSLEQVNDGLTSIIAV-----PVTLVLLY-GLLRFfnvILGEIRDTLFGRVTERA 108
Cdd:cd18577 2 IIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFlddvnKYALYFVYlGIGSF---VLSYIQTACWTITGERQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 109 MRRVGLKLFDHLHNLDLDFHLNRQTGGL----SRDMERGTSGISFLMRFMVFNIVpTLLeILFVVAiFFHQYGLnfALIT 184
Cdd:cd18577 79 ARRIRKRYLKALLRQDIAWFDKNGAGELtsrlTSDTNLIQDGIGEKLGLLIQSLS-TFI-AGFIIA-FIYSWKL--TLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 185 LGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELalwETARRknrltlFGL 264
Cdd:cd18577 154 LATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKAL---EKARK------AGI 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 265 NSGQALIIASAMTSMLLLAANG---------VVAKEMTLGD------FVLINAFMMQLFMP 310
Cdd:cd18577 225 KKGLVSGLGLGLLFFIIFAMYAlafwygsrlVRDGEISPGDvltvffAVLIGAFSLGQIAP 285
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
37-305 |
1.43e-12 |
|
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: 68.28 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVD------SLEQVNDGLTSIIAVpvtlVLLYGL---LRFFNVI-LGEirdtlfgRVTe 106
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDqgfaagNTALLNRAFLLLLAV----ALVLALasaLRFYLVSwLGE-------RVV- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 107 RAMRRvglKLFDHLHNLDLDFHLNRQTGG-LSR---DMER-----GTSgISFLMRfmvfNIvptlleILFVVAI---FFH 174
Cdd:cd18575 69 ADLRK---AVFAHLLRLSPSFFETTRTGEvLSRlttDTTLiqtvvGSS-LSIALR----NL------LLLIGGLvmlFIT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 175 QYGLnfALITLGSIVLYIGFTAYATEWRTKYIREA--NQADSSSnsRAIDSLLNYETVKYFNNEQYESQRYDEEL-ALWE 251
Cdd:cd18575 135 SPKL--TLLVLLVIPLVVLPIILFGRRVRRLSRASqdRLADLSA--FAEETLSAIKTVQAFTREDAERQRFATAVeAAFA 210
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 252 TARRKNR----LTLFGLnsgqaLIIASAMTSMLLLAANGVVAKEMTLGDFVlinAFMM 305
Cdd:cd18575 211 AALRRIRaralLTALVI-----FLVFGAIVFVLWLGAHDVLAGRMSAGELS---QFVF 260
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
357-567 |
1.86e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 66.11 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYD---PSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYD--VTSGSIEIDSVNIKtvtqQSLRK 431
Cdd:cd03232 4 LTWKNLNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD----KNFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 432 HMGIVPQDTVLF-NDSIFENIRYgnpnadddqvwqaikHAHLydfvqdlpkkeqtvvgeRGLKLSggEKQRVAIARTILK 510
Cdd:cd03232 80 STGYVEQQDVHSpNLTVREALRF---------------SALL-----------------RGLSVE--QRKRLTIGVELAA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 511 RPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDA--DKIIVMHQG 567
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLAdSGQAILCTIHQPSASIFEkfDRLLLLKRG 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
376-583 |
2.07e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTlvkLLFRFYDVT--SGSIEIDSVNIKTVTQQSLRKHMG-IVPQDTVLFNDSIFENI- 451
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLLpgSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQYLt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 452 RYGNPNADDDQVWQAIKhaHLYDFVQdLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPP-------ILIFDEATSSL 524
Cdd:PRK03695 92 LHQPDKTRTEAVASALN--EVAEALG-LDDKLGRSVNQ----LSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 525 DSGSEQAILAALQEIA-KGHTSLVIAHRLS-TIVDADKIIVMHQGEIVETGNHQQLLLANG 583
Cdd:PRK03695 165 DVAQQAALDRLLSELCqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
34-318 |
2.13e-12 |
|
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: 67.90 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDS--LEQVNDGLTSIIAVPVTLVLLYGLLRFFNVILGeirdtlfGRVTERAMRR 111
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSgvRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLT-------GRTGERLLYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 112 VGLKLFDHLHNLDLDFHlNRQTGGlsRDMERGTSGISFLMRFM---VFNIVPTLLEILFVVAIFFHqygLNF--ALITLG 186
Cdd:cd18546 74 LRLRVFAHLQRLSLDFH-ERETSG--RIMTRMTSDIDALSELLqtgLVQLVVSLLTLVGIAVVLLV---LDPrlALVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 187 SIVLyigfTAYATEW-----RTKYiREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNrLTL 261
Cdd:cd18546 148 ALPP----LALATRWfrrrsSRAY-RRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRA-QRL 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 262 FGLNSGQALIIASAMTSMLLLA-ANGVVAKEMTLGdfVLInAFMM---QLFMPLNFLGFVY 318
Cdd:cd18546 222 VAIYFPGVELLGNLATAAVLLVgAWRVAAGTLTVG--VLV-AFLLylrRFFAPIQQLSQVF 279
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
373-572 |
2.98e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.17 E-value: 2.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIK-TVTQQSLrkHMGI---------VPQDTVL 442
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAAL--AAGVaiiyqelhlVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 443 fndsifENI-------RYGNPNADDDQVWQAIKHAHL-YDFVQDLPKKEqtvvgerglkLSGGEKQRVAIARTILKRPPI 514
Cdd:PRK11288 98 ------ENLylgqlphKGGIVNRRLLNYEAREQLEHLgVDIDPDTPLKY----------LSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 515 LIFDEATSSLDS-GSEQ--AILAALQeiAKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVET 572
Cdd:PRK11288 162 IAFDEPTSSLSArEIEQlfRVIRELR--AEGRVILYVSHRMEEIFAlCDAITVFKDGRYVAT 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
373-568 |
3.37e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI--DSVNIKTvTQQSLRKHMGIVPQDTVLF-NDSIFE 449
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNG-PKSSQEAGIGIIHQELNLIpQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIRYG----NPnadddqvWQAIKHAHLYDFVQDLPKK------EQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDE 519
Cdd:PRK10762 99 NIFLGrefvNR-------FGRIDWKKMYAEADKLLARlnlrfsSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 520 ATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGE 568
Cdd:PRK10762 168 PTDALTDTETESLFRVIRELkSQGRGIVYISHRLKEIFEiCDDVTVFRDGQ 218
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
34-328 |
7.50e-12 |
|
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: 66.30 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLeQVNDGLTSIIAVPVTLVLLygllrffNVILGEIRDTLFGRVTERAMRRVG 113
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDAL-SAGGSSGGLLALLVALFLL-------QAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 114 LKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRFMVFNIVPTLLEILFVVAIFFHQYGLNF--ALITLGSIVLY 191
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDL---VSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWvlTLVTLAVVPLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 192 IGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEEL-ALWETARRKNRLtlfglnsgQAL 270
Cdd:cd18551 150 FLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAeRLYRAGLKAAKI--------EAL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 271 IIASAMTSMLL-----LAANG--VVAKEMTLGDFVlinAFMM---QLFMPL-NFLGFV--YREIKGSLANI 328
Cdd:cd18551 222 IGPLMGLAVQLallvvLGVGGarVASGALTVGTLV---AFLLylfQLITPLsQLSSFFtqLQKALGALERI 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
366-582 |
1.12e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.12 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 366 YDPS-RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTvTQQSLRKHMGIVPQDTVLFN 444
Cdd:TIGR01257 938 FEPSgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFH 1016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 445 D-SIFENIR-YGNPNADDDQVWQAIKHAHLYDfvQDLPKKEQtvvgERGLKLSGGEKQRVAIARTILKRPPILIFDEATS 522
Cdd:TIGR01257 1017 HlTVAEHILfYAQLKGRSWEEAQLEMEAMLED--TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 523 SLDSGSEQAILAALQEIAKGHTSLVIAHRLSTI-VDADKIIVMHQGEIVETGNhqQLLLAN 582
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT--PLFLKN 1149
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
371-525 |
1.36e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.10 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 371 PILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSvniKTVTQQSLRKHMGIVPQDTVLFND-SIFE 449
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRFMAYLGHLPGLKADlSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NIRYGNpnadddqvwqAIKHAHlydfVQDLPKKEQTVVGERGL------KLSGGEKQRVAIARTILKRPPILIFDEATSS 523
Cdd:PRK13543 102 NLHFLC----------GLHGRR----AKQMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
..
gi 2261045687 524 LD 525
Cdd:PRK13543 168 LD 169
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-332 |
1.58e-11 |
|
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: 65.25 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDGLTSIIAVPVTLVLLYGLLRFFNVILGEIRDTLFGRVTeRAMRRvg 113
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVV-ADLRS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 114 lKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGISFLMRF---MVFNIVPTLLEILFVVAIFFhqyGLN--FALITLgsi 188
Cdd:cd18778 78 -DLYDKLQRLSLRYFDDRQTGDL---MSRVINDVANVERLiadGIPQGITNVLTLVGVAIILF---SINpkLALLTL--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 vLYIGFTAYATEWRTKYI----REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEElalwetARRKNRLTLFGL 264
Cdd:cd18778 148 -IPIPFLALGAWLYSKKVrpryRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEAL------SRRYRKAQLRAM 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 265 N------SGQALIIASAMTSMLLLAANGVVAKEMTLGDFVlinAFMMqlfmplnFLGFVYREIkGSLANIEKMF 332
Cdd:cd18778 221 KlwaifhPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLV---AFLL-------YLGLFYEPI-TSLHGLNEML 283
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
373-573 |
2.34e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 62.73 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKllfrfydvtsgsiEIdsvnIKTVTQQSLRKHMGIVPQDTVLFNDS----IF 448
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EG----LYASGKARLISFLPKFSRNKLIFIDQlqflID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENIRYGNPNadddqvwqaikhahlydfvqdlpKKEQTvvgerglkLSGGEKQRVAIARTILKRPP--ILIFDEATSSLDS 526
Cdd:cd03238 74 VGLGYLTLG-----------------------QKLST--------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQ 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 527 GSEQAILAALQE-IAKGHTSLVIAHRLSTIVDADKIIVM------HQGEIVETG 573
Cdd:cd03238 123 QDINQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
358-528 |
2.51e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.30 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 358 SFKDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLfrfydvtsGSIEIDSvNIKTVTQQSLRkhMGIVP 437
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM--------AGVDKEF-EGEARPAPGIK--VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 438 QD-------TVLFN---------------DSIFENirYGNPNADDD-------QVWQAIKHAHLYDFVQDL--------- 479
Cdd:PRK11819 77 QEpqldpekTVRENveegvaevkaaldrfNEIYAA--YAEPDADFDalaaeqgELQEIIDAADAWDLDSQLeiamdalrc 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2261045687 480 PKKEQTVVgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGS 528
Cdd:PRK11819 155 PPWDAKVT-----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
374-571 |
2.70e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 374 KGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQ-QSLRKHMGIVPQ---DTVLF-NDSIF 448
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENI---------RYG------NPN-----ADDDQVWQAIKHAHLydfvqdlpkkEQTVVgerglKLSGGEKQRVAIARTI 508
Cdd:PRK09700 360 QNMaisrslkdgGYKgamglfHEVdeqrtAENQRELLALKCHSV----------NQNIT-----ELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDA-DKIIVMHQGEIVE 571
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
33-318 |
2.71e-11 |
|
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: 64.80 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 33 RVVLALICLVLAKVAIVGLPFILKEIVDSLEQVND--GLTsiiavpvTLVLLYGLLRFFNVILGEIRDTLFGRVTERAMR 110
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDlsGLL-------IIALLFLALNLVNWVASRLRIYLMAKVGQRILY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RVGLKLFDHLHNLDLDFHLNRQTGG-LSR---DmergTSGISFLMRFMVFNIVPTLLEILFVVAIFFhqyGLNF--ALIT 184
Cdd:cd18545 74 DLRQDLFSHLQKLSFSFFDSRPVGKiLSRvinD----VNSLSDLLSNGLINLIPDLLTLVGIVIIMF---SLNVrlALVT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 185 LGSIVLYIGFTAYateWRTKyIREA----NQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYD----EELALWETARRK 256
Cdd:cd18545 147 LAVLPLLVLVVFL---LRRR-ARKAwqrvRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDelnrENRKANMRAVRL 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 257 NRLTLFGLNsgqaLIIASAMTSMLLLAANGVVAKEMTLGDFVlinAFMM---QLFMPLNFLGFVY 318
Cdd:cd18545 223 NALFWPLVE----LISALGTALVYWYGGKLVLGGAITVGVLV---AFIGyvgRFWQPIRNLSNFY 280
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
361-559 |
2.80e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 361 DVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIK---TVTQQSL---RKHMG 434
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlCTYQKQLcfvGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 435 IVPQDTVlfNDSIFENIRYGNPNADDDQVWQAIKHAHLYDFVQDLpkkeqtvvgerglkLSGGEKQRVAIARTILKRPPI 514
Cdd:PRK13540 85 INPYLTL--RENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2261045687 515 LIFDEATSSLDSGSEQAILAALQE-IAKGHTSLVIAHRLSTIVDAD 559
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
369-519 |
2.99e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLvkllfrFY------DVTSGSIEIDSVNIktvTQQSL--RKHMGI--VPQ 438
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDI---THLPMhkRARLGIgyLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 DTvlfndSIF------ENIRygnpnadddqvwqAIKHahlydfVQDLPKKEQT--------------VVGERGLKLSGGE 498
Cdd:COG1137 86 EA-----SIFrkltveDNIL-------------AVLE------LRKLSKKEREerleelleefgithLRKSKAYSLSGGE 141
|
170 180
....*....|....*....|.
gi 2261045687 499 KQRVAIARTILKRPPILIFDE 519
Cdd:COG1137 142 RRRVEIARALATNPKFILLDE 162
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
357-536 |
4.11e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.04 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 357 ISFKDVRFEYdPSRPIL-KGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIeidsvniktvtQQSLRKHMGI 435
Cdd:PLN03073 509 ISFSDASFGY-PGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 436 VPQDTVLFNDSIFENIRY------GNPNadddqvwQAIKhAHLYDFvqdlpkkeqTVVGERGLK----LSGGEKQRVAIA 505
Cdd:PLN03073 577 FSQHHVDGLDLSSNPLLYmmrcfpGVPE-------QKLR-AHLGSF---------GVTGNLALQpmytLSGGQKSRVAFA 639
|
170 180 190
....*....|....*....|....*....|.
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAAL 536
Cdd:PLN03073 640 KITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
369-574 |
4.22e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.97 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIktvtQQSLRKHMGIVPQDTVLF-NDSI 447
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL----DPEDRRRIGYLPEERGLYpKMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FENIRY-----GNPNADddqvwqaIKHAHLYDFVQ-DLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEAT 521
Cdd:COG4152 89 GEQLVYlarlkGLSKAE-------AKRRADEWLERlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 522 SSLDSGSEQAILAALQE-IAKGHTSLVIAHRLSTiVD--ADKIIVMHQGEIVETGN 574
Cdd:COG4152 158 SGLDPVNVELLKDVIRElAAKGTTVIFSSHQMEL-VEelCDRIVIINKGRKVLSGS 212
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
35-313 |
6.75e-11 |
|
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: 63.62 E-value: 6.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 35 VLALICLVLAKVAIVGLPFILKEIVDSLEQVNDgLTSIIAVPVTLVLLYGLLRFFNVILgeirdTLFGRVT----ERAMR 110
Cdd:cd18549 5 FLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKN-LRLILIIGAILLALYILRTLLNYFV-----TYWGHVMgariETDMR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RvglKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGIsFLMRFMVF----NIVPTLLEIL--FVVAIFFHqygLNFALIT 184
Cdd:cd18549 79 R---DLFEHLQKLSFSFFDNNKTGQL---MSRITNDL-FDISELAHhgpeDLFISIITIIgsFIILLTIN---VPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 185 LGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETARRKNRLTLFGL 264
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 265 NSGQALIIasAMTSMLLLAANG--VVAKEMTLGDFV----LINAFMMQLFMPLNF 313
Cdd:cd18549 229 FSGMNFFT--NLLNLVVLVAGGyfIIKGEITLGDLVafllYVNVFIKPIRRLVNF 281
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
376-581 |
6.81e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.05 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 376 INFTINSGEKLAVVGESGSGKSTLVKLLFRF----YDVTSGSIEIDSVNIKTVTQQSLRKHMG-----IV--PQDTVLFN 444
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsmIFqePQSCLDPS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 445 DSIFENIRYGNPNAD-DDQVWQ--------AIKHAHLYDFvqdlpKKEQTVVGERGLKLSGGEKQRVAIARTILKRPPIL 515
Cdd:PRK15093 106 ERVGRQLMQNIPGWTyKGRWWQrfgwrkrrAIELLHRVGI-----KDHKDAMRSFPYELTEGECQKVMIAIALANQPRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVD-ADKIIVMHQGEIVETGNHQQLLLA 581
Cdd:PRK15093 181 IADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVTT 249
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
373-574 |
6.89e-11 |
|
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: 63.02 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLV---------KLLFRF------YDVTSGSIEIDSVnikTVTQQSLrkhMGIVP 437
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKkeqpgnHDRIEGLEHIDKV---IVIDQSP---IGRTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 438 QD-----TVLFnDSIFE----------------NIRYGNPNADDdqVWQ-AIKHAHlyDFVQDLPK---KEQTVV----- 487
Cdd:cd03271 85 RSnpatyTGVF-DEIRElfcevckgkrynretlEVRYKGKSIAD--VLDmTVEEAL--EFFENIPKiarKLQTLCdvglg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 488 ----GERGLKLSGGEKQRVAIARTILKRPP---ILIFDEATSSLDSGSEQAILAALQE-IAKGHTSLVIAHRLSTIVDAD 559
Cdd:cd03271 160 yiklGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCAD 239
|
250 260
....*....|....*....|.
gi 2261045687 560 KIIVM------HQGEIVETGN 574
Cdd:cd03271 240 WIIDLgpeggdGGGQVVASGT 260
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-573 |
8.07e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 361 DVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSI--EIDSVNIKTVTQQSLRKHMGIVPQ 438
Cdd:PRK13638 6 DLWFRYQ-DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwQGKPLDYSKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 439 D--TVLFNDSIFENIRYG--NPNADDDQVWQAIKHAhlydfvqdlpkkeQTVVGERGLK------LSGGEKQRVAIARTI 508
Cdd:PRK13638 85 DpeQQIFYTDIDSDIAFSlrNLGVPEAEITRRVDEA-------------LTLVDAQHFRhqpiqcLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 509 LKRPPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
370-579 |
8.30e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.60 E-value: 8.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVT-QQSLRKHMGIVPQDTVLFND-SI 447
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 448 FEN------IRYG-NPNADDDQVWQAIKHAHLYDFVQDLpkkeqtvvgerGLKLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:PRK10895 96 YDNlmavlqIRDDlSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 521 TSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDA-DKIIVMHQGEIVETGNHQQLL 579
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVcERAYIVSQGHLIAHGTPTEIL 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
361-577 |
8.90e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 361 DVRFEYDP-SRPILKG-INFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDS--VNIKTvTQQSL------- 429
Cdd:PRK11288 255 EVRLRLDGlKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRS-PRDAIragimlc 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 ---RKHMGIVPQDtvlfndSIFENI-----RYGNPNAD-DDQVWQAIKHAHlydFVQDL----PKKEQTVVgerglKLSG 496
Cdd:PRK11288 334 pedRKAEGIIPVH------SVADNInisarRHHLRAGClINNRWEAENADR---FIRSLniktPSREQLIM-----NLSG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 497 GEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:PRK11288 400 GNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELA 479
|
...
gi 2261045687 575 HQQ 577
Cdd:PRK11288 480 REQ 482
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
79-305 |
1.36e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 62.60 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 79 LVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFhLNRQTGGLSrdMERGTSgISFLMRFMVFNI 158
Cdd:cd18566 44 LVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSF-FEREPSGAH--LERLNS-LEQIREFLTGQA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 159 VPTLLEILFVV----AIFFhqYGLNFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFN 234
Cdd:cd18566 120 LLALLDLPFVLiflgLIWY--LGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMA 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 235 NEQYESQRYDEELALW-ETARRKNRLTLFGLNSGQALIIASaMTSMLLLAANGVVAKEMTLGDFVlinAFMM 305
Cdd:cd18566 198 MEPQMLRRYERLQANAaYAGFKVAKINAVAQTLGQLFSQVS-MVAVVAFGALLVINGDLTVGALI---ACTM 265
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
355-525 |
1.43e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 355 GTISF--KDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFrfydvtsGSIEIDSVNIKTVTQQSLR-- 430
Cdd:PRK11147 316 GKIVFemENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGRIHCGTKLEVAyf 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 -KHMGIV-PQDTVLfndsifENIrygnpnADDDQ-VWQAIKHAHLYDFVQDL---PKKEQTVVGerglKLSGGEKQRVAI 504
Cdd:PRK11147 388 dQHRAELdPEKTVM------DNL------AEGKQeVMVNGRPRHVLGYLQDFlfhPKRAMTPVK----ALSGGERNRLLL 451
|
170 180
....*....|....*....|.
gi 2261045687 505 ARTILKRPPILIFDEATSSLD 525
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLD 472
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
373-574 |
1.68e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLfrfydvTSGSIEIDSVNI-KtvTQQSLRKHMGIV------------PQD 439
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtgilvpTSGEVRVLGYVPfK--RRKEFARRIGVVfgqrsqlwwdlpAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 440 TVLFNDSIfenirYGNPNADddqvwqaikHAHLYDFVQDL----PKKEQTVvgeRglKLSGGEKQRVAIARTILKRPPIL 515
Cdd:COG4586 116 SFRLLKAI-----YRIPDAE---------YKKRLDELVELldlgELLDTPV---R--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 516 IFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGS 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
379-563 |
1.75e-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: 63.65 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 379 TINSGEKLAVVGESGSGKSTLVKLLfrfydvtSGSIEIDSVNIKTVTQQSLRkhmgivPQ----DtvlFNDSIFENIRYG 454
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDEDLKISYK------PQyispD---YDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 455 NPNADDDQVWQA-------IKHahLYDfvqdlpkkeqtvvgeRGLK-LSGGEKQRVAIARTILKRPPILIFDEATSSLDs 526
Cdd:COG1245 426 NTDDFGSSYYKTeiikplgLEK--LLD---------------KNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLD- 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2261045687 527 gSEQAILAA--LQEIAKGH--TSLVIAHRLsTIVD--ADKIIV 563
Cdd:COG1245 488 -VEQRLAVAkaIRRFAENRgkTAMVVDHDI-YLIDyiSDRLMV 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-554 |
2.01e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.42 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 352 IGDGTISFKDVRFEYDpSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEI-DSVNIKTVTQQslr 430
Cdd:TIGR03719 318 LGDKVIEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQS--- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 431 khmgivpQDTVLFNDSIFENIRYGNpnaDDDQVWQAIKHAHLY----DFV-QDLPKKeqtvVGErglkLSGGEKQRVAIA 505
Cdd:TIGR03719 394 -------RDALDPNKTVWEEISGGL---DIIKLGKREIPSRAYvgrfNFKgSDQQKK----VGQ----LSGGERNRVHLA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 506 RTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKghTSLVIAH------RLST 554
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
351-570 |
2.42e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 2.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 351 NIGDGTISFKD--VRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLF-RFYDV-TSGSIEID--SVNIKTV 424
Cdd:NF040905 252 KIGEVVFEVKNwtVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRnISGTVFKDgkEVDVSTV 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 425 TQ---QSL------RKHMGIVpqdtvlFNDSIFENIRYGNPNA-------DDDQvwqAIKHAHlyDFVQDL----PKKEQ 484
Cdd:NF040905 332 SDaidAGLayvtedRKGYGLN------LIDDIKRNITLANLGKvsrrgviDENE---EIKVAE--EYRKKMniktPSVFQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 485 TVVgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKII 562
Cdd:NF040905 401 KVG-----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVISSELPELLGmCDRIY 475
|
....*...
gi 2261045687 563 VMHQGEIV 570
Cdd:NF040905 476 VMNEGRIT 483
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
493-568 |
5.05e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 493 KLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGseQAILAA--LQEIAKGHTSLVIAHRLsTIVD--ADKIIVMHqGE 568
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR--QRLNVArlIRELAEGKYVLVVEHDL-AVLDylADNVHIAY-GE 287
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
375-573 |
5.60e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 5.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 375 GINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLRKhMGIVP--QDTVLFND-SIFENI 451
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRtfQHVRLFREmTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 452 -----RYGNPN-------------ADDDQVWQAikhAHLYDFVQDLPkkeqtVVGERGLKLSGGEKQRVAIARTILKRPP 513
Cdd:PRK11300 102 lvaqhQQLKTGlfsgllktpafrrAESEALDRA---ATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 514 ILIFDEATSSLDSGSEQAILAALQEIAKGH--TSLVIAHRLSTIVD-ADKIIVMHQGEIVETG 573
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
333-577 |
7.15e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 7.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 333 ELLERVPKVTDKkqAKELNIgdgtisfkDVRFEYDPSRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSG 412
Cdd:PRK10982 234 SLTQRFPDKENK--PGEVIL--------EVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAG 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 413 SIEIDSVNIKT-------------VTQQslRKHMGIVPQDTVLFNdSIFENIR--------YGNPNADDDQVWqaikhah 471
Cdd:PRK10982 304 TITLHGKKINNhnaneainhgfalVTEE--RRSTGIYAYLDIGFN-SLISNIRnyknkvglLDNSRMKSDTQW------- 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 472 LYDFVQDLPKKEQTVVGErglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAH 550
Cdd:PRK10982 374 VIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISS 449
|
250 260 270
....*....|....*....|....*....|.
gi 2261045687 551 RLSTIVD-ADKIIVMHQGE---IVETGNHQQ 577
Cdd:PRK10982 450 EMPELLGiTDRILVMSNGLvagIVDTKTTTQ 480
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
473-578 |
7.19e-10 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 61.95 E-value: 7.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 473 YDFVQDLPK---KEQTVV---------GERGLKLSGGEKQRVAIARTILKR---PPILIFDEATSSLDSGSEQAILAALQ 537
Cdd:TIGR00630 797 YEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQ 876
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2261045687 538 E-IAKGHTSLVIAHRLSTIVDADKIIVM------HQGEIVETGNHQQL 578
Cdd:TIGR00630 877 RlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
379-563 |
1.04e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 379 TINSGEKLAVVGESGSGKSTLVKLLfrfydvtSGSIEIDSVNIKTvtqqSLR---KHMGIVPQdtvlFNDSIFENIRYGN 455
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEVDP----ELKisyKPQYIKPD----YDGTVEDLLRSIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 456 PNADDDQVWQAIKH----AHLYDfvqdlpkKEqtvVGErglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDsgSEQA 531
Cdd:PRK13409 426 DDLGSSYYKSEIIKplqlERLLD-------KN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQR 489
|
170 180 190
....*....|....*....|....*....|....*...
gi 2261045687 532 ILAA--LQEIAKGH--TSLVIAHRLSTIvD--ADKIIV 563
Cdd:PRK13409 490 LAVAkaIRRIAEEReaTALVVDHDIYMI-DyiSDRLMV 526
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
382-568 |
8.09e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.26 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 382 SGEKLAVVGESGSGKSTLVKLLfrfydvtSGSI-----EIDS-VNIKTVtqqsLRKHMGivpqdTVLFNdsIFENIRYGN 455
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKIL-------SGELkpnlgDYDEePSWDEV----LKRFRG-----TELQD--YFKKLANGE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 456 pnadddqvwqaIKHAHLYDFVQDLPKKEQTVVG-------ERGL-------------------KLSGGEKQRVAIARTIL 509
Cdd:COG1245 160 -----------IKVAHKPQYVDLIPKVFKGTVRellekvdERGKldelaeklglenildrdisELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2261045687 510 KRPPILIFDEATSSLDSGseQAILAA--LQEIAKGHTS-LVIAHRLsTIVD--ADKIIVMHqGE 568
Cdd:COG1245 229 RDADFYFFDEPSSYLDIY--QRLNVArlIRELAEEGKYvLVVEHDL-AILDylADYVHILY-GE 288
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
37-321 |
1.60e-08 |
|
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: 56.10 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSLEQV--NDGLTSIIAVPVTLVLLYGLLrFFNVILGEIRDTLFGRVTERAMRRVGL 114
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHsgSGGEEALRALNQAVLILLGVV-LIGSIATFLRSWLFTLAGERVVARLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 115 KLFDHLHNLDLDFHLNRQTGGL----SRDME----RGTSGISFLMRFMVFNIVPtlLEILFVVAIFFHqyglnfaLITLG 186
Cdd:cd18780 80 RLFSAIIAQEIAFFDVTRTGELlnrlSSDTQvlqnAVTVNLSMLLRYLVQIIGG--LVFMFTTSWKLT-------LVMLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 187 SI-VLYIGFTAYAtewrtKYIRE------ANQADSSSNsrAIDSLLNYETVKYFNNEQYESQRYDEEL-ALWETARRKNR 258
Cdd:cd18780 151 VVpPLSIGAVIYG-----KYVRKlskkfqDALAAASTV--AEESISNIRTVRSFAKETKEVSRYSEKInESYLLGKKLAR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2261045687 259 LTlfGLNSGQALIIAS-AMTSMLLLAANGVVAKEMTLGdfvLINAFMM---QLFMPLNFLGFVYREI 321
Cdd:cd18780 224 AS--GGFNGFMGAAAQlAIVLVLWYGGRLVIDGELTTG---LLTSFLLytlTVAMSFAFLSSLYGDF 285
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
354-559 |
1.63e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 354 DGTISFKDvrfeydpsRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLF----RFY--DVT-----SGSIEidsvnik 422
Cdd:PRK10938 265 NGVVSYND--------RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYsnDLTlfgrrRGSGE------- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 423 tvTQQSLRKHMGIVP-------------QDTVL--FNDSIfeniryGNPNADDD------QVWQAIkhAHLYDFVQDLPK 481
Cdd:PRK10938 330 --TIWDIKKHIGYVSsslhldyrvstsvRNVILsgFFDSI------GIYQAVSDrqqklaQQWLDI--LGIDKRTADAPF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 482 KEqtvvgerglkLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAAL-QEIAKGHTSLV------------I 548
Cdd:PRK10938 400 HS----------LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVdVLISEGETQLLfvshhaedapacI 469
|
250
....*....|.
gi 2261045687 549 AHRLSTIVDAD 559
Cdd:PRK10938 470 THRLEFVPDGD 480
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
382-565 |
2.06e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.45 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 382 SGEKLAVVGESGSGKSTLVKLLfrfydvtSGSIeidsvniktvtQQSLRKHMGIVPQDTVL--FNDS----IFENIRYGN 455
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKIL-------AGKL-----------KPNLGKFDDPPDWDEILdeFRGSelqnYFTKLLEGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 456 -------------PNADDDQVWQAIKHAHLYDFVQDLPKK-EQTVVGERGL-KLSGGEKQRVAIARTILKRPPILIFDEA 520
Cdd:cd03236 87 vkvivkpqyvdliPKAVKGKVGELLKKKDERGKLDELVDQlELRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2261045687 521 TSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLStIVD--ADKIIVMH 565
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLA-VLDylSDYIHCLY 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
348-567 |
2.32e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 348 KELNIGDGTISFKDVRFEYDPS---RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRfyDVTSGSIEIDS--VNIK 422
Cdd:TIGR00956 751 MEKESGEDIFHWRNLTYEVKIKkekRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDrlVNGR 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 423 TVtQQSLRKHMGIVPQ-DTVLFNDSIFENIRYG----NPNAdddqvwqaIKHAHLYDFVQ---DLPKKEQ---TVVGERG 491
Cdd:TIGR00956 829 PL-DSSFQRSIGYVQQqDLHLPTSTVRESLRFSaylrQPKS--------VSKSEKMEYVEeviKLLEMESyadAVVGVPG 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 492 LKLSGGEKQRVAIARTILKRPPILIF-DEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVDA--DKIIVMHQG 567
Cdd:TIGR00956 900 EGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
373-572 |
4.65e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 373 LKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEID--SVNIKTvTQQSLRKHMGIVPQD-TVLFNDSIFE 449
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkEIDFKS-SKEALENGISMVHQElNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 NI---RY--GNPNADDDQVWQAIKhAHLYDFVQDLPKKEQTVvgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSL 524
Cdd:PRK10982 93 NMwlgRYptKGMFVDQDKMYRDTK-AIFDELDIDIDPRAKVA------TLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 525 dsgSEQ------AILAALQEiaKGHTSLVIAHRLSTIVD-ADKIIVMHQGEIVET 572
Cdd:PRK10982 166 ---TEKevnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWIAT 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
382-568 |
7.78e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 382 SGEKLAVVGESGSGKSTLVKLLFRFYDVTSGS-IEIDSVNIKTVTQQSLRkhmgivpqdtvlfndsifenirygnpnadd 460
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 461 dqvwqaikhahlydfvqdlpkkeQTVVGERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAA----- 535
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2261045687 536 -LQEIAKGHTSLVIAHRLSTIVD-------ADKIIVMHQGE 568
Cdd:smart00382 108 lLLLKSEKNLTVILTTNDEKDLGpallrrrFDRRIVLLLIL 148
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
34-326 |
1.09e-07 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 53.56 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDG-----LTSIIAVPVTLVLLYGLLRFFNVILGeirdTLFGRVTERA 108
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGgggvdFSGLLRILLLLLGLYLLSALFSYLQN----RLMARVSQRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 109 MRRVGLKLFDHLHNLDLDFHLNRQTGG-LSR---DMERgtsgISFLMRFMVFNIVPTLLEILFVVAIFFHqygLNF--AL 182
Cdd:cd18547 77 VYDLRKDLFEKLQRLPLSYFDTHSHGDiMSRvtnDVDN----ISQALSQSLTQLISSILTIVGTLIMMLY---ISPllTL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 183 ITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDE---ELAlwETARRKNR- 258
Cdd:cd18547 150 IVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEineELY--KASFKAQFy 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2261045687 259 ------LTLFGLNSGQALI-IASAmtsmlLLAANGVvakeMTLGDFVlinAFMM---QLFMPLNFLGFVYREIKGSLA 326
Cdd:cd18547 228 sgllmpIMNFINNLGYVLVaVVGG-----LLVINGA----LTVGVIQ---AFLQysrQFSQPINQISQQINSLQSALA 293
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
369-548 |
1.09e-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: 55.40 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 369 SRPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTvTQQSLRKHMGIVPQdtvlfndsiF 448
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQ---------F 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENIrygnpnaddDQVWQAIKHAHLYDFVQDLPKKEQTVVGERGLK--------------LSGGEKQRVAIARTILKRPPI 514
Cdd:TIGR01257 2021 DAI---------DDLLTGREHLYLYARLRGVPAEEIEKVANWSIQslglslyadrlagtYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190
....*....|....*....|....*....|....
gi 2261045687 515 LIFDEATSSLDSGSEQAILAALQEIAKGHTSLVI 548
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL 2125
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
72-305 |
1.09e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 53.67 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 72 IIAVPVTLVLLygllrfFNVILGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERgTSGI-SFL 150
Cdd:cd18783 43 VLTIGVVIALL------FEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQ-IERIrQFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 151 MRFMVFNIVPTLLEILFVVAIFFHQYGLnfALITLGSIVLyIGFTAYATEWRTKY-IREANQADSSSNSRAIDSLLNYET 229
Cdd:cd18783 116 TGQLFGTLLDATSLLVFLPVLFFYSPTL--ALVVLAFSAL-IALIILAFLPPFRRrLQALYRAEGERQAFLVETVHGIRT 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 230 VKYFNNEQYESQRYDEELAlwETARRKNRLTLFGlNSGQALI--IASAMTSM-LLLAANGVVAKEMTLGdfVLInAFMM 305
Cdd:cd18783 193 VKSLALEPRQRREWDERVA--RAIRARFAVGRLS-NWPQTLTgpLEKLMTVGvIWVGAYLVFAGSLTVG--ALI-AFNM 265
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
349-579 |
2.64e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 349 ELNIGDGTISFKDVRFEYDPSrpilkginFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDsvnIKTVTQQS 428
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPS--------LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ---FSHITRLS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 429 LRKHMGIVPQDtvlFNDSifeNIRYGNPNADDDQVWQAikhahlyDFVQDLPKKEQ------------TVVGERGLKLSG 496
Cdd:PRK10938 72 FEQLQKLVSDE---WQRN---NTDMLSPGEDDTGRTTA-------EIIQDEVKDPArceqlaqqfgitALLDRRFKYLST 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 497 GEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLV-IAHRLSTIVD-ADKIIVMHQGEIVETGN 574
Cdd:PRK10938 139 GETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGE 218
|
....*
gi 2261045687 575 HQQLL 579
Cdd:PRK10938 219 REEIL 223
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
33-314 |
3.65e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 52.16 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 33 RVVLALICLVLAKVAivgLPFILKEIVDSLeqVNDGLTSIIAVpvtLVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRV 112
Cdd:cd18779 6 QILLASLLLQLLGLA---LPLLTGVLVDRV--IPRGDRDLLGV---LGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 113 GLKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSgiSFLMRFMVFN-IVPTLLE----ILFVVAIFFHQYGlnFALITLGS 187
Cdd:cd18779 78 TLGFLEHLLRLPYRFFQQRSTGDL---LMRLSS--NATIRELLTSqTLSALLDgtlvLGYLALLFAQSPL--LGLVVLGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 188 IVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNE----QYESQRYDEELAlweTARRKNRLTLfG 263
Cdd:cd18779 151 AALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEdralDRWSNLFVDQLN---ASLRRGRLDA-L 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 264 LNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFL 314
Cdd:cd18779 227 VDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASL 277
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
380-568 |
4.16e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 50.26 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 380 INSGEKLAVVGESGSGKSTLVKLLfrfydvtSGSIEidsvniktvtqqslrkhmgivpqdtvlfndsifenirygnPNAD 459
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKIL-------AGQLI----------------------------------------PNGD 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 460 DDQvWQAIKHAHlydfvqdlpkKEQTVvgerglKLSGGEKQRVAIARTILKRPPILIFDEATSSLDsgSEQAILAA---- 535
Cdd:cd03222 55 NDE-WDGITPVY----------KPQYI------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLD--IEQRLNAArair 115
|
170 180 190
....*....|....*....|....*....|....
gi 2261045687 536 -LQEIAKgHTSLVIAHRLSTIVDADKIIVMHQGE 568
Cdd:cd03222 116 rLSEEGK-KTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
100-341 |
4.64e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 52.07 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 100 LFGRVTERAMRRVGLKLFDHLHNLDLDFHlnrqtgglsrDMERGTSGI--SFL------MRFMVFNIVPTLLEILFVVAI 171
Cdd:cd18578 75 LFGIAGERLTRRLRKLAFRAILRQDIAWF----------DDPENSTGAltSRLstdasdVRGLVGDRLGLILQAIVTLVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 172 -----FFhqYGLNFALITLGSIVLYIGFTAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEE 246
Cdd:cd18578 145 gliiaFV--YGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 247 L-ALWETARRKNRLT--LFGL-NSGQALIIASAMTSMLLLAANGvvakEMTLGD-FVLINAFMMQLFMPLNFLGFVYREI 321
Cdd:cd18578 223 LeEPLKKGLRRALISglGFGLsQSLTFFAYALAFWYGGRLVANG----EYTFEQfFIVFMALIFGAQSAGQAFSFAPDIA 298
|
250 260
....*....|....*....|
gi 2261045687 322 KGSLAnIEKMFELLERVPKV 341
Cdd:cd18578 299 KAKAA-AARIFRLLDRKPEI 317
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
79-312 |
9.03e-07 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 50.68 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 79 LVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDME--RgtsgiSFLMRFMVF 156
Cdd:cd18586 44 LTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDtlR-----NFLTGPSLF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 157 NIVPTLLEILFVVAIF-FHQYglnFALITLGSIVLYIGFtAYATEWRT-KYIREANQADSSSNSRAIDSLLNYETVKYFN 234
Cdd:cd18586 119 AFFDLPWAPLFLAVIFlIHPP---LGWVALVGAPVLVGL-AWLNHRATrKPLGEANEAQAARDALAAETLRNAETIKALG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 235 NEQYESQRYDEELA--LWETARRKNRLTLFGlNSGQALIIASAmTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLN 312
Cdd:cd18586 195 MLGNLRRRWEARHAetLELQIRASDLAGAIS-AIGKTLRMALQ-SLILGVGAYLVIDGELTIGALIAASILSGRALAPID 272
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
494-573 |
2.55e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 48.79 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 494 LSGGEKQRVAIARTILKR--PPILIFDEATSSLDSGSEQAILAALQEI-AKGHTSLVIAHRLSTIVDADKIIVM------ 564
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIgpgagv 217
|
....*....
gi 2261045687 565 HQGEIVETG 573
Cdd:cd03270 218 HGGEIVAQG 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
370-536 |
2.77e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 2.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIdSVNIKtvtqqslrkhMGIVPQDTVLF---NDS 446
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK----------LGYFAQHQLEFlraDES 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 447 IFENIRYGNPNADDDQvwqaikhahLYDFVQDLPKKEQTVVGERGlKLSGGEKQRVAIARTILKRPPILIFDEATSSLDS 526
Cdd:PRK10636 394 PLQHLARLAPQELEQK---------LRDYLGGFGFQGDKVTEETR-RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
170
....*....|
gi 2261045687 527 GSEQAILAAL 536
Cdd:PRK10636 464 DMRQALTEAL 473
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
37-306 |
3.44e-06 |
|
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: 49.08 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSL-----EQVNDGLTSIIAVPVTLVLLY---GLLRFFNVilgeirdTLFGRVTERA 108
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVIsrslkETNGDFIEDLKKPALKLLGLYllqSLLTFAYI-------SLLSVVGERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 109 MRRVGLKLFDHLHNLDLDFHLNRQTGGLsrdMERGTSGI-----SFLM------RFMV---------FNIVPTLleilfv 168
Cdd:cd18574 74 AARLRNDLFSSLLRQDIAFFDTHRTGEL---VNRLTADVqefksSFKQcvsqglRSVTqtvgcvvslYLISPKL------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 169 vaiffhqyglnfALITLGSI-VLYIGFTAYATEWRtKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEEL 247
Cdd:cd18574 145 ------------TLLLLVIVpVVVLVGTLYGSFLR-KLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEV 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 248 alwETARRKNRLTLFGLNSGQALiiasamTSmllLAANGVV------------AKEMTLGDFVlinAFMMQ 306
Cdd:cd18574 212 ---EKAAKLNEKLGLGIGIFQGL------SN---LALNGIVlgvlyyggslvsRGELTAGDLM---SFLVA 267
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
33-305 |
6.80e-06 |
|
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: 48.23 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 33 RVVLALICL-VLAKVAIVGLPFILKEIVDS-LEQVNDGLTSIIAvpvtlvLLYGLLRFFNVILGEIRdtlfGRVTERAMR 110
Cdd:cd18567 2 RALLQILLLsLALELFALASPLYLQLVIDEvIVSGDRDLLTVLA------IGFGLLLLLQALLSALR----SWLVLYLST 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 111 RVGL----KLFDHLHNLDLDFHLNRQTGG-LSRDmergtSGISFLMRFMVFNIVPTLLEILFVVA----IFFhqYGLNFA 181
Cdd:cd18567 72 SLNLqwtsNLFRHLLRLPLSYFEKRHLGDiVSRF-----GSLDEIQQTLTTGFVEALLDGLMAILtlvmMFL--YSPKLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 182 LITLGSIVLYIG--FTAYatewrtKYIREANQ----ADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELA-LWETAR 254
Cdd:cd18567 145 LIVLAAVALYALlrLALY------PPLRRATEeqivASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVdAINADI 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2261045687 255 RKNRLTLFgLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVlinAFMM 305
Cdd:cd18567 219 RLQRLQIL-FSAANGLLFGLENILVIYLGALLVLDGEFTVGMLF---AFLA 265
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
370-564 |
8.91e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKllfrfydvtsgSIEIdsvnIKTVTQQSLRKHMGIVPQDTVlfndsife 449
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD-----------AIGL----ALGGAQSATRRRSGVKAGCIV-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 450 nirygnpnadddqvwqAIKHAHLYDFVqdlpkkeqtvvgergLKLSGGEKQRVAIArTIL-----KRPPILIFDEATSSL 524
Cdd:cd03227 65 ----------------AAVSAELIFTR---------------LQLSGGEKELSALA-LILalaslKPRPLYILDEIDRGL 112
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2261045687 525 DSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDADKIIVM 564
Cdd:cd03227 113 DPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHI 153
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
494-582 |
9.06e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 494 LSGGEKQRVAIARTIL---KRPPILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDADKIIVMHQgei 569
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLELGP--- 886
|
90
....*....|...
gi 2261045687 570 vETGNHQQLLLAN 582
Cdd:PRK00635 887 -EGGNLGGYLLAS 898
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
37-305 |
1.48e-05 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 47.12 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSleqVNDGLTSIIAVPVTLVLLY-GLLRFFnvILGEI----RDTLFGRVTERAMRR 111
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDV---ASKESGDIEIFGLSLKTFAlALLGVF--VVGAAanfgRVYLLRIAGERIVAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 112 VGLKLFDHLHNLDLDFHLNRQTGGL----------------------SRDMERGTSGISflmrfMVFNIVPTLLEILFVV 169
Cdd:cd18573 76 LRKRLFKSILRQDAAFFDKNKTGELvsrlssdtsvvgksltqnlsdgLRSLVSGVGGIG-----MMLYISPKLTLVMLLV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 170 aiffhqyglnFALITLGSIVLYigftayatewrtKYIREAN----QADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDE 245
Cdd:cd18573 151 ----------VPPIAVGAVFYG------------RYVRKLSkqvqDALADATKVAEERLSNIRTVRAFAAERKEVERYAK 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 246 EL-ALWETARR--KNRLTLFGLNSgqaLIIASAMTSMLLLAANGVVAKEMTLGDFVlinAFMM 305
Cdd:cd18573 209 KVdEVFDLAKKeaLASGLFFGSTG---FSGNLSLLSVLYYGGSLVASGELTVGDLT---SFLM 265
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
494-573 |
2.43e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.33 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 494 LSGGEKQRVAIARTILKRPP---ILIFDEATSSL---DsgseqaI---LAALQE-IAKGHTSLVIAHRLSTIVDADKIIV 563
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhD------IrklLEVLHRlVDKGNTVVVIEHNLDVIKTADWIID 900
|
90
....*....|....*.
gi 2261045687 564 M------HQGEIVETG 573
Cdd:COG0178 901 LgpeggdGGGEIVAEG 916
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
494-573 |
3.91e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 494 LSGGEKQRVAIARTILKRP---PILIFDEATSSLDSGSEQAILAALQEIA-KGHTSLVIAHRLSTIVDADKIIVM----- 564
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVdKGNTVVVIEHNLDVIKTADWIIDLgpegg 910
|
90
....*....|
gi 2261045687 565 -HQGEIVETG 573
Cdd:PRK00349 911 dGGGEIVATG 920
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
350-525 |
4.81e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 350 LNIGDGTISFKDVrfeydpsrPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSL 429
Cdd:PRK11147 4 ISIHGAWLSFSDA--------PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 430 RKHMgivpQDTVLfnDSIFENIRygnpnadddQVWQAIK--HAHLYDFVQD-----------------------LPKKEQ 484
Cdd:PRK11147 76 PRNV----EGTVY--DFVAEGIE---------EQAEYLKryHDISHLVETDpseknlnelaklqeqldhhnlwqLENRIN 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2261045687 485 TVVGERGL-------KLSGGEKQRVAIARTILKRPPILIFDEATSSLD 525
Cdd:PRK11147 141 EVLAQLGLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
51-314 |
5.02e-05 |
|
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: 45.49 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 51 LPFILKEIVDSLEQVN-----DGLTSIIAVPVTLVLLYGLLRffnVILGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDL 125
Cdd:cd18554 18 LPLILKYIVDDVIQGSsltldEKVYKLFTIIGIMFFIFLILR---PPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 126 DFHLNRQTGGL-SR---DMERGTSGIsfLMRFMvfNIVPTLLEILFVVAI-FFHQYGLNFALITLgsIVLYIGFTAYATE 200
Cdd:cd18554 95 RYYANNRSGEIiSRvinDVEQTKDFI--TTGLM--NIWLDMITIIIAICImLVLNPKLTFVSLVI--FPFYILAVKYFFG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 201 WRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEELALWETarRKNRLTLFGLNSGQALIIASAMTSML 280
Cdd:cd18554 169 RLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLT--RALKHTRWNAKTFSAVNTITDLAPLL 246
|
250 260 270
....*....|....*....|....*....|....*.
gi 2261045687 281 LLAANG--VVAKEMTLGDFVLINAFMMQLFMPLNFL 314
Cdd:cd18554 247 VIGFAAylVIEGNLTVGTLVAFVGYMERMYSPLRRL 282
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
80-318 |
5.97e-05 |
|
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: 45.38 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 80 VLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFLMRFMVFNIV 159
Cdd:cd18784 39 IIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 160 PTLLEILFVVAIFFhqyGLNFALITLGSIVLYIGF--TAYATEWRTKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQ 237
Cdd:cd18784 119 RSLVKAIGVIVFMF---KLSWQLSLVTLIGLPLIAivSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 238 YESQRYDEELALWETARRKNRLTLFGLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGFV 317
Cdd:cd18784 196 GEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSV 275
|
.
gi 2261045687 318 Y 318
Cdd:cd18784 276 Y 276
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
485-579 |
8.51e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 485 TVVGERGLK-LSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLS----TIVDAD 559
Cdd:PLN03140 327 TIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFD 406
|
90 100
....*....|....*....|
gi 2261045687 560 KIIVMHQGEIVETGNHQQLL 579
Cdd:PLN03140 407 DIILLSEGQIVYQGPRDHIL 426
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
39-309 |
2.32e-04 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 43.39 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 39 ICLVLAKVAIVGL----PFILKEIVDSLeqvndgltSIIAVPVTLVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGL 114
Cdd:cd18562 2 LGLALANVALAGVqfaePVLFGRVVDAL--------SSGGDAFPLLALWAALGLFSILAGVLVALLADRLAHRRRLAVMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 115 KLFDHLHNLDLDFHLNRQTGGLSRDMERGTSGISFL----MRFMVFNIVPtlLEILFVVAIFfhqygLNF--ALITLGSI 188
Cdd:cd18562 74 SYFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGLwlgfFREHLAALVS--LIVLLPVALW-----MNWrlALLLVVLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 189 VLYIGFTAYATEwRTKYI-REANQADSSSNSRAIDSLLNYETVKYFNNEQYESQrydeelALWETARRKNR-----LT-- 260
Cdd:cd18562 147 AVYAALNRLVMR-RTKAGqAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETS------ALRGITRRLLAaqypvLNww 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2261045687 261 --LFGLNSGQALIiasAMTSMLLLAANGVVAKEMTLGDFV--------LI------NAFMMQLFM 309
Cdd:cd18562 220 alASVLTRAASTL---TMVAIFALGAWLVQRGELTVGEIVsfvgfatlLIgrldqlSGFINRLFM 281
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
370-575 |
2.65e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 370 RPILKGINFTINSGEKLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSV-NIKTVTQQSlrKHMGIVPQDTVLFNDSIF 448
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQET--PALPQPALEYVIDGDREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 449 ENIRYGNPNADDDQVWQAIKHAH-LYDFVQDLPKKEQTVVGERGL------------KLSGGEKQRVAIARTILKRPPIL 515
Cdd:PRK10636 92 RQLEAQLHDANERNDGHAIATIHgKLDAIDAWTIRSRAASLLHGLgfsneqlerpvsDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2261045687 516 IFDEATSSLDsgseqaiLAA---LQEIAKGH--TSLVIAHR---LSTIVdaDKIIVMHQGEIVE-TGNH 575
Cdd:PRK10636 172 LLDEPTNHLD-------LDAviwLEKWLKSYqgTLILISHDrdfLDPIV--DKIIHIEQQSLFEyTGNY 231
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
34-317 |
3.38e-04 |
|
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: 42.77 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 34 VVLALICLVLAKVAIVGLPFILKEIVDSLEQVNDgltsiiavpVTLVLLYGLLRFFNVILGeirdTLFG--------RVT 105
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGD---------LSYILRTGLLMLLLALLG----LIAGilagyfaaKAS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 106 ERAMRRVGLKLFDHLHNLDLdfhlnrqtgglsRDMER-GTS---------------GISFLMRFMVFniVPtlleILFVV 169
Cdd:cd18548 68 QGFGRDLRKDLFEKIQSFSF------------AEIDKfGTSslitrltndvtqvqnFVMMLLRMLVR--AP----IMLIG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 170 AIF--FHQyGLNFALITLGSIVLyIGFTAYATEWRTKYIREANQadsssnsRAID--------SLLNYETVKYFNNEQYE 239
Cdd:cd18548 130 AIImaFRI-NPKLALILLVAIPI-LALVVFLIMKKAIPLFKKVQ-------KKLDrlnrvvreNLTGIRVIRAFNREDYE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 240 SQRYDE---ELAlwETARRKNRLTLFgLNSGQALIIASAMTSMLLLAANGVVAKEMTLGDFVLINAFMMQLFMPLNFLGF 316
Cdd:cd18548 201 EERFDKandDLT--DTSLKAGRLMAL-LNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSM 277
|
.
gi 2261045687 317 V 317
Cdd:cd18548 278 V 278
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
470-582 |
6.10e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 470 AHLYDFVQDLPKKEQTVV---------GERGLKLSGGEKQRVAIARTIL---KRPPILIFDEATSSLDSGSEQAILAALQ 537
Cdd:PRK00635 1667 AETFPFLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLR 1746
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2261045687 538 E-IAKGHTSLVIAHRLSTIVDADKIIVM------HQGEIVETGNHQQLLLAN 582
Cdd:PRK00635 1747 TlVSLGHSVIYIDHDPALLKQADYLIEMgpgsgkTGGKILFSGPPKDISASK 1798
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
37-305 |
8.02e-04 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 41.56 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 37 ALICLVLAKVAIVGLPFILKEIVDSLEQvNDGLTSIIAVpvtlVLLYGLLRFFNVILGEIRDTLFGRVTERAMRRVGLKL 116
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGG-EYQHNAFTSA----IGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 117 FDHLHNLDLDFHLNRQTGGLSRDMERGTSGISflmRFMVFNIVPTLLEILFVVAIFFHQYGLNFALITLGSI---VLYIG 193
Cdd:cd18590 76 FSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMS---RSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIempLTAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 194 FTAYATEWRtKYIREANQADSSSNSRAIDSLLNYETVKYFNNEQYESQRYDEelALWETARRKNRLtlfGLNSGQALIIA 273
Cdd:cd18590 153 QKVYNTYHQ-KLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSE--ALERTYNLKDRR---DTVRAVYLLVR 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 2261045687 274 SAMT-----SMLLLAANGVVAKEMTLGDFVlinAFMM 305
Cdd:cd18590 227 RVLQlgvqvLMLYCGRQLIQSGHLTTGSLV---SFIL 260
|
|
| Septin |
pfam00735 |
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ... |
375-467 |
8.70e-04 |
|
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this family bind GTP. As regards the septins, these are polypeptides of 30-65kDa with three characteriztic GTPase motifs (G-1, G-3 and G-4) that are similar to those of the Ras family. The G-4 motif is strictly conserved with a unique septin consensus of AKAD. Most septins are thought to have at least one coiled-coil region, which in some cases is necessary for intermolecular interactions that allow septins to polymerize to form rod-shaped complexes. In turn, these are arranged into tandem arrays to form filaments. They are multifunctional proteins, with roles in cytokinesis, sporulation, germ cell development, exocytosis and apoptosis.
Pssm-ID: 395596 Cd Length: 272 Bit Score: 41.52 E-value: 8.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 375 GINFTinsgekLAVVGESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQqsLRKHMGIVPQDTVLFNDSIFENIRYG 454
Cdd:pfam00735 1 GFDFT------LMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVE--IKAYTVEIEEDGVKLNLTVIDTPGFG 72
|
90
....*....|...
gi 2261045687 455 NpNADDDQVWQAI 467
Cdd:pfam00735 73 D-AIDNSNCWRPI 84
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
390-525 |
2.15e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 390 GESGSGKSTLVKLLFRFYDVTSGSIEIDSVNIKTVTQQSLR---KHMGIVPQDTVlfndsiFENIRYGNPNADD-DQVWQ 465
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTyigHNLGLKLEMTV------FENLKFWSEIYNSaETLYA 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 466 AIKHAHLYDFVQdlpkkeqtvvgERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLD 525
Cdd:PRK13541 107 AIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
488-578 |
2.37e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261045687 488 GERGLKLSGGEKQRVAIARTILKRPPILIFDEATSSLDSGSEQAILAALQEIAK-GHTSLVIAHRLSTIVD-ADKIIVMH 565
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|...
gi 2261045687 566 QGEIVETGNHQQL 578
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| ABC_RecN |
cd03241 |
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to ABC ... |
484-550 |
2.62e-03 |
|
ATP-binding cassette domain of RecN; RecN ATPase involved in DNA repair; similar to 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 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: 213208 [Multi-domain] Cd Length: 276 Bit Score: 39.88 E-value: 2.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2261045687 484 QTVVGERGLKL----SGGEKQRVAIA-RTIL---KRPPILIFDEATSSLdSGSEQAILA-ALQEIAKGHTSLVIAH 550
Cdd:cd03241 157 STNPGEPLKPLakiaSGGELSRLMLAlKAILarkDAVPTLIFDEIDTGI-SGEVAQAVGkKLKELSRSHQVLCITH 231
|
|
| CDC_Septin |
cd01850 |
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ... |
374-404 |
3.29e-03 |
|
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated with diverse processes in dividing and non-dividing cells. They were first discovered in the budding yeast S. cerevisiae as a set of genes (CDC3, CDC10, CDC11 and CDC12) required for normal bud morphology. Septins are also present in metazoan cells, where they are required for cytokinesis in some systems, and implicated in a variety of other processes involving organization of the cell cortex and exocytosis. In humans, 12 septin genes generate dozens of polypeptides, many of which comprise heterooligomeric complexes. Since septin mutants are commonly defective in cytokinesis and formation of the neck formation of the neck filaments/septin rings, septins have been considered to be the primary constituents of the neck filaments. Septins belong to the GTPase superfamily for their conserved GTPase motifs and enzymatic activities.
Pssm-ID: 206649 Cd Length: 275 Bit Score: 39.84 E-value: 3.29e-03
10 20 30
....*....|....*....|....*....|.
gi 2261045687 374 KGINFTInsgeklAVVGESGSGKSTLVKLLF 404
Cdd:cd01850 1 RGFQFNI------MVVGESGLGKSTFINTLF 25
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
494-562 |
4.82e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.60 E-value: 4.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2261045687 494 LSGGEKQRVAIAR--TILK-RP-PILIFDEATSSLDSGSEQAILAALQEIAKGHTSLVIAHRLSTIVDADKII 562
Cdd:cd03278 114 LSGGEKALTALALlfAIFRvRPsPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| |
