|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
292-847 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 533.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 292 LLAPVKKQMIAGGVLQAIITMVELAPFVVLVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSA 371
Cdd:COG1132 15 YLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 372 DVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVY 451
Cdd:COG1132 95 DLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 452 LLTMMAMMYQSGPKIVEASRWADRMSTESTAYLEGQPVIRIFGGAAASS--FKRRLDDYLRFLNDWQRPFIGRKTFMDLV 529
Cdd:COG1132 175 LLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELerFREANEELRRANLRAARLSALFFPLMELL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 530 TRPTTFLwlIATAGTLFVVSGAMQPVTLLPFLVLGTTFGARLLGIAYGLGSIRGGLESARHIAVALDETE--LDVIEAPV 607
Cdd:COG1132 255 GNLGLAL--VLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeiPDPPGAVP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 608 TADAVASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDEL 687
Cdd:COG1132 333 LPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 688 YAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGEKQRLTIARALL 766
Cdd:COG1132 413 RRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERgVNLSGGQRQRIAIARALL 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 767 ADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLW 846
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLY 572
|
.
gi 491227761 847 E 847
Cdd:COG1132 573 R 573
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
292-848 |
2.08e-110 |
|
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: 354.53 E-value: 2.08e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 292 LLAPVKKQMIAGGVLQAIITMVELA-PFVVLVeLTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFS 370
Cdd:COG2274 150 LLRRYRRLLLQVLLASLLINLLALAtPLFTQV-VIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRID 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 371 ADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDdTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILV 450
Cdd:COG2274 229 LRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPL 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 451 YLLTMMAMmyqsGPKIVEASRWADRMSTESTAYLE----GQPVIRIFGgaAASSFKRRLDDYLRFLNDWQrpfIGRKTFM 526
Cdd:COG2274 308 YVLLGLLF----QPRLRRLSREESEASAKRQSLLVetlrGIETIKALG--AESRFRRRWENLLAKYLNAR---FKLRRLS 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 527 DLVTRPTTFLWLIATAGTLF-----VVSGAMQPVTLLPFLVLGTTFGARLLGIAyglgsirGGLESARHIAVALDETElD 601
Cdd:COG2274 379 NLLSTLSGLLQQLATVALLWlgaylVIDGQLTLGQLIAFNILSGRFLAPVAQLI-------GLLQRFQDAKIALERLD-D 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 602 VIEAPVTADAVA----------SVSFEGVTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERG 670
Cdd:COG2274 451 ILDLPPEREEGRsklslprlkgDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 671 AIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDT 749
Cdd:COG2274 531 RILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVgEGGS 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 750 QLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAET 829
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
570
....*....|....*....
gi 491227761 830 GTHTDLLANNGRYRRLWEG 848
Cdd:COG2274 691 GTHEELLARKGLYAELVQQ 709
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
615-846 |
6.37e-104 |
|
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: 320.72 E-value: 6.37e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGF 693
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPIL 772
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIgERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLW 846
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
615-847 |
4.04e-102 |
|
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: 316.09 E-value: 4.04e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVgERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLWE 847
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
292-840 |
1.00e-100 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 324.40 E-value: 1.00e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 292 LLAPVKKQMIAGGVLQAIITMVELAPFVVLVE-LTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFS 370
Cdd:COG4988 11 LARGARRWLALAVLLGLLSGLLIIAQAWLLASlLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 371 ADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILV 450
Cdd:COG4988 91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 451 YLLTMMAMMYQsgpkiveASRWADR----MSTESTAYLE---GQPVIRIFG--GAAASSFKRRLDDYlrflndwqrpfig 521
Cdd:COG4988 171 IPLFMILVGKG-------AAKASRRqwraLARLSGHFLDrlrGLTTLKLFGraKAEAERIAEASEDF------------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 522 RKTFMDlVTR----PTTFLWLIATAGTLFV-VSGAMQ----PVTLLP---FLVLGTTFGA--RLLGIAYGLGsiRGGLES 587
Cdd:COG4988 231 RKRTMK-VLRvaflSSAVLEFFASLSIALVaVYIGFRllggSLTLFAalfVLLLAPEFFLplRDLGSFYHAR--ANGIAA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 588 ARHIAVALDETELDVI--EAPVTADAVASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFH 665
Cdd:COG4988 308 AEKIFALLDAPEPAAPagTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 666 DVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL 745
Cdd:COG4988 388 PPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPL 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 746 -DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHG 824
Cdd:COG4988 468 gEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDG 547
|
570
....*....|....*.
gi 491227761 825 RVAETGTHTDLLANNG 840
Cdd:COG4988 548 RIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
613-855 |
9.29e-98 |
|
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: 317.92 E-value: 9.29e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVG 692
Cdd:COG5265 356 GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIG 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTV-----LdtdtQLSGGEKQRLTIARALLA 767
Cdd:COG5265 436 IVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRvgergL----KLSGGEKQRVAIARTLLK 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 768 DTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLWE 847
Cdd:COG5265 512 NPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWA 591
|
....*...
gi 491227761 848 GHRHEQSS 855
Cdd:COG5265 592 RQQEEEEA 599
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
615-847 |
1.15e-97 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 304.46 E-value: 1.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGY--RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVG 692
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPI 771
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVgERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 772 LILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLWE 847
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
615-840 |
1.13e-94 |
|
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: 296.44 E-value: 1.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLgENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNG 840
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
367-847 |
1.30e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 300.14 E-value: 1.30e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 367 LRFSADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLI 446
Cdd:COG4987 84 LRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 447 PILVYLLTMMAMMYQSG-PKIVEASRWADRMSTESTAYLEGQPVIRIFGGAAAssFKRRLDDYLRFLNDWQR----PFIG 521
Cdd:COG4987 164 GLLLAGLLLPLLAARLGrRAGRRLAAARAALRARLTDLLQGAAELAAYGALDR--ALARLDAAEARLAAAQRrlarLSAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 522 RKTFMDLVTrpTTFLWLIATAGTLFVVSGAMQPVTL--LPFLVLGTtFGArLLGIAYGLGSIRGGLESARHIAvALDETE 599
Cdd:COG4987 242 AQALLQLAA--GLAVVAVLWLAAPLVAAGALSGPLLalLVLAALAL-FEA-LAPLPAAAQHLGRVRAAARRLN-ELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 600 LDVIE--APVTADAVASVSFEGVTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDG 676
Cdd:COG4987 317 PAVTEpaEPAPAPGGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 677 TDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGE 755
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGgRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 756 KQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDL 835
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|..
gi 491227761 836 LANNGRYRRLWE 847
Cdd:COG4987 557 LAQNGRYRQLYQ 568
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
332-845 |
3.96e-91 |
|
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: 299.31 E-value: 3.96e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 332 ADEAQLRHTGFVFLVLLVLGATLGMALTLWLhVVDL--RFSADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLH 409
Cdd:TIGR02204 51 KDSSGLLNRYFAFLLVVALVLALGTAARFYL-VTWLgeRVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 410 YLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMMAMmyqsGPKIVEASRWADRMSTESTAY----LE 485
Cdd:TIGR02204 130 SVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLF----GRRVRKLSRESQDRIADAGSYagetLG 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 486 GQPVIRIFGG--AAASSFKRRLDDYLRFLNdwqrpfiGRKTFMDLVTRPTTFLWLIATAGTLF-----VVSGAMQPVTLL 558
Cdd:TIGR02204 206 AIRTVQAFGHedAERSRFGGAVEKAYEAAR-------QRIRTRALLTAIVIVLVFGAIVGVLWvgahdVIAGKMSAGTLG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 559 PFLVLGTTFGARLLGIAYGLGSIR---GGLEsaRHIAVALDETELDVIEAPVT--ADAVASVSFEGVTFGY--RPGVPVI 631
Cdd:TIGR02204 279 QFVFYAVMVAGSIGTLSEVWGELQraaGAAE--RLIELLQAEPDIKAPAHPKTlpVPLRGEIEFEQVNFAYpaRPDQPAL 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 632 HDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIAL 711
Cdd:TIGR02204 357 DGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 712 ACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQ 790
Cdd:TIGR02204 437 GRPDATDEEVEAAARAAHAHEFISALPEGYDTYLgERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQ 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 791 QALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRL 845
Cdd:TIGR02204 517 QALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
293-845 |
1.21e-90 |
|
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: 297.78 E-value: 1.21e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 293 LAPVKKQMIAGGVLQAIITMVELAPFVVLVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSAD 372
Cdd:TIGR02203 9 VRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 373 VRRRLLDKLSRVPLGWFTQRGSGSV-KKLIQDDTMSLHYLiTHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLI--PIL 449
Cdd:TIGR02203 89 IRVRMFEKLLGLPVSFFDRQPTGTLlSRITFDSEQVASAA-TDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVmlPVL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 450 VYLLTMMAMMYQS-GPKIVEASRWADRMSTEStayLEGQPVIRIFGGAAASSfkRRLDdylrFLNDWQRPFIGRKTFMDL 528
Cdd:TIGR02203 168 SILMRRVSKRLRRiSKEIQNSMGQVTTVAEET---LQGYRVVKLFGGQAYET--RRFD----AVSNRNRRLAMKMTSAGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 529 VTRP-TTFLWLIATAGTLFVVSGAMQPVTLLP--FLVLGTTFGA------RLLGIAyglGSIRGGLESARHIAVALDET- 598
Cdd:TIGR02203 239 ISSPiTQLIASLALAVVLFIALFQAQAGSLTAgdFTAFITAMIAlirplkSLTNVN---APMQRGLAAAESLFTLLDSPp 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 599 ELDVIEAPVtADAVASVSFEGVTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGT 677
Cdd:TIGR02203 316 EKDTGTRAI-ERARGDVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 678 DIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDD-DVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGE 755
Cdd:TIGR02203 395 DLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRaEIERALAAAYAQDFVDKLPLGLDTPIgENGVLLSGGQ 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 756 KQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDL 835
Cdd:TIGR02203 475 RQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNEL 554
|
570
....*....|
gi 491227761 836 LANNGRYRRL 845
Cdd:TIGR02203 555 LARNGLYAQL 564
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
615-825 |
1.28e-76 |
|
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: 246.14 E-value: 1.28e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGF 693
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAGTVRENIalacpeatdddvesaardaqiherilrlpngydtvldtdtqLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGR 825
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
374-845 |
1.28e-75 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 257.97 E-value: 1.28e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 374 RRRL------LDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIP 447
Cdd:PRK13657 86 RRRLavlteyFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSLVLVVL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 448 ILVY-LLTMMAM-MYQSGPKIVE------ASRWADRMSTEStaylegqpVIRIFGGAAASsfKRRLDDYLRFLNDWQRPF 519
Cdd:PRK13657 166 GIVYtLITTLVMrKTKDGQAAVEehyhdlFAHVSDAIGNVS--------VVQSYNRIEAE--TQALRDIADNLLAAQMPV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 520 IGRKTFMDLVTRPTTFLWLIA--TAGTLFVVSGAMQPVTLLPFLVLGTTFGARLLGIAyglGSIRGGLESARHIA--VAL 595
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAilVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVV---AFINQVFMAAPKLEefFEV 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 596 DETELDVIEAPVTADA---VASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAI 672
Cdd:PRK13657 313 EDAVPDVRDPPGAIDLgrvKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 673 RIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQL 751
Cdd:PRK13657 393 LIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVgERGRQL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 752 SGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGT 831
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
|
490
....*....|....
gi 491227761 832 HTDLLANNGRYRRL 845
Cdd:PRK13657 553 FDELVARGGRFAAL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
373-850 |
2.44e-75 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 256.87 E-value: 2.44e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 373 VRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDT-----MSLHYLIT-----HSIpdavaavvgpVAVLVYLFVIEWRMAL 442
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSeqvasSSSGALITvvregASI----------IGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 443 ILLI--PILVYLLTMMAMMYQSGPKIVEASRWADRMSTESTayLEGQPVIRIFGGAAASsfKRRLDdylRFLNDWqrpfi 520
Cdd:PRK11176 170 ILIViaPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQM--LKGHKEVLIFGGQEVE--TKRFD---KVSNRM----- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 521 gRKTFMDLVTRPTTF---LWLIA--------------------TAGTLFVVSGAMqpVTLLPFLVLGTTFGARLlgiayg 577
Cdd:PRK11176 238 -RQQGMKMVSASSISdpiIQLIAslalafvlyaasfpsvmdtlTAGTITVVFSSM--IALMRPLKSLTNVNAQF------ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 578 lgsiRGGLESARHIAVALD-ETELD----VIEaPVTADavasVSFEGVTFGYrPG--VPVIHDVSLTLRHGTVTALVGPS 650
Cdd:PRK11176 309 ----QRGMAACQTLFAILDlEQEKDegkrVIE-RAKGD----IEFRNVTFTY-PGkeVPALRNINFKIPAGKTVALVGRS 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 651 GSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEA-TDDDVESAARDAQ 729
Cdd:PRK11176 379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAY 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 730 IHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHR 808
Cdd:PRK11176 459 AMDFINKMDNGLDTVIgENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 491227761 809 LHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLwegHR 850
Cdd:PRK11176 539 LSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL---HK 577
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
615-845 |
1.81e-74 |
|
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: 243.16 E-value: 1.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVI-HDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGF 693
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPIL 772
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVgEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRL 845
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
368-845 |
1.16e-72 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 252.72 E-value: 1.16e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 368 RFSADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLI- 446
Cdd:TIGR00958 231 RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLIn 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 447 -PILVYLLTMMAMMYQS-GPKIVEASRWADRMSTEStayLEGQPVIRIFG--GAAASSFKRRLDDYLRFlndWQRPFIGR 522
Cdd:TIGR00958 311 lPLVFLAEKVFGKRYQLlSEELQEAVAKANQVAEEA---LSGMRTVRSFAaeEGEASRFKEALEETLQL---NKRKALAY 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 523 KTFmdLVTRP-------TTFLWLiataGTLFVVSGAMQPVTLLPFLVLGTTFGARLLGIAYGLGSIRGGLESARHIAVAL 595
Cdd:TIGR00958 385 AGY--LWTTSvlgmliqVLVLYY----GGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 596 DET---ELDVIEAPVTADAVasVSFEGVTFGY--RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERG 670
Cdd:TIGR00958 459 DRKpniPLTGTLAPLNLEGL--IEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 671 AIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLD-TDT 749
Cdd:TIGR00958 537 QVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGeKGS 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 750 QLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRliDNRTVLVIAHRLHTIADADQIVVLDHGRVAET 829
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
490
....*....|....*.
gi 491227761 830 GTHTDLLANNGRYRRL 845
Cdd:TIGR00958 695 GTHKQLMEDQGCYKHL 710
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
538-845 |
4.71e-71 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 248.32 E-value: 4.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 538 LIATAGTLFVVSGAMQPVTLLPFLVLGTTFGA---RLLGIAYGLGSIRGGLESARHIA-VALDETELDVIEAPVTADAVA 613
Cdd:TIGR03796 393 LILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEpvnNLVGFGGTLQELEGDLNRLDDVLrNPVDPLLEEPEGSAATSEPPR 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 S----VSFEGVTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELY 688
Cdd:TIGR03796 473 RlsgyVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLA 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 689 AKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGEKQRLTIARALLA 767
Cdd:TIGR03796 553 NSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGgANLSGGQRQRLEIARALVR 632
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 768 DTPILILDEATAFADPESEYLVQQALGRlidnR--TVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRL 845
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDDNLRR----RgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
328-821 |
2.89e-69 |
|
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: 238.73 E-value: 2.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 328 LLAGADEAQLRhtgfvFLVLLVLGATLGMALTLWLH-VVDLRFSADV----RRRLLDKLSRVPLGWFTQRGSGSVKKLIQ 402
Cdd:TIGR02857 34 ISAGEPLAELL-----PALGALALVLLLRALLGWLQeRAAARAAAAVksqlRERLLEAVAALGPRWLQGRPSGELATLAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 403 DDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALIL-----LIPILVYLLTMMAmmyqsgpKIVEASRWA--DR 475
Cdd:TIGR02857 109 EGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILlltapLIPIFMILIGWAA-------QAAARKQWAalSR 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 476 MSTESTAYLEGQPVIRIFG--GAAASSFKRRLDDYlrflndwqrpfigRKTFMDlVTR----PTTFLWLIAT-------- 541
Cdd:TIGR02857 182 LSGHFLDRLRGLPTLKLFGraKAQAAAIRRSSEEY-------------RERTMR-VLRiaflSSAVLELFATlsvalvav 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 542 -------AGTLFVVSG----AMQPVTLLPFLVLGTTFGARLLGIAyglgsirggleSARHIAVALDETELDVIE-APVTA 609
Cdd:TIGR02857 248 yigfrllAGDLDLATGlfvlLLAPEFYLPLRQLGAQYHARADGVA-----------AAEALFAVLDAAPRPLAGkAPVTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 610 DAVASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA 689
Cdd:TIGR02857 317 APASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 KVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGEKQRLTIARALLAD 768
Cdd:TIGR02857 397 QIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGgAGLSGGQAQRLALARAFLRD 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 769 TPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVL 821
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
614-831 |
4.48e-65 |
|
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: 216.98 E-value: 4.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVG 692
Cdd:cd03244 2 DIEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAGTVRENIalaCP--EATDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGEKQRLTIARALLADT 769
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL---DPfgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGgENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 770 PILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGT 831
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
605-826 |
6.28e-65 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 216.95 E-value: 6.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 605 APVTADAVasVSFEGVTFGY--RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTL 682
Cdd:cd03248 4 APDHLKGI--VKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 683 TPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDT-VLDTDTQLSGGEKQRLTI 761
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTeVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 762 ARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRV 826
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
384-845 |
1.54e-60 |
|
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: 216.29 E-value: 1.54e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 384 VPLGWFTQRG-SGSVKKLIQ-DDTMS---LHYLITHsipdaVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMMAM 458
Cdd:TIGR01192 102 MPLSWHQQRGtSNALHTLLRaTETLFglwLEFMRQH-----LATFVALFLLIPTAFAMDWRLSIVLMVLGILYILIAKLV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 459 MYQS--GPKIVEA------SRWADRMSTEStaylegqpVIRIFGGAAASSfkRRLDDYLRFLNDWQRPFIGRKTFMDLVT 530
Cdd:TIGR01192 177 MQRTknGQAAVEHhyhnvfKHVSDSISNVS--------VVHSYNRIEAET--SALKQFTNNLLSAQYPVLDWWALASGLN 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 531 R--PTTFLWLIATAGTLFVVSGAMQPVTLLPFLVLGTTFGARL---LGIAYGLGSIRGGLESARHIAVALDETElDVIEA 605
Cdd:TIGR01192 247 RmaSTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLdqmSGFITQIFEARAKLEDFFDLEDSVFQRE-EPADA 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 606 PVTADAVASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPD 685
Cdd:TIGR01192 326 PELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 686 ELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARA 764
Cdd:TIGR01192 406 SLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVgERGNRLSGGERQRLAIARA 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRR 844
Cdd:TIGR01192 486 ILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYK 565
|
.
gi 491227761 845 L 845
Cdd:TIGR01192 566 L 566
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
613-837 |
1.12e-59 |
|
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: 213.07 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYrPG--VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAK 690
Cdd:COG4618 329 GRLSVENLTVVP-PGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQDVQLVAGTVRENIALAcPEATDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGEKQRLTIARALLADT 769
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIARF-GDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGgARLSGGQRQRIGLARALYGDP 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 770 PILILDEATAFADPESEylvqQALGRLIDN-----RTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLA 837
Cdd:COG4618 487 RLVVLDEPNSNLDDEGE----AALAAAIRAlkargATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
614-826 |
6.37e-59 |
|
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: 200.12 E-value: 6.37e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYrPG--VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKV 691
Cdd:cd03245 2 RIEFRNVSFSY-PNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDT-VLDTDTQLSGGEKQRLTIARALLADTP 770
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLqIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 771 ILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRV 826
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
440-847 |
3.33e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 209.30 E-value: 3.33e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 440 MALILLIPILVYLLTMmammyQSGPKIVEASRwadRMSTESTAYLEGQPVIRIFGgaAASSFKRRLDDylrflndWQRPF 519
Cdd:PRK11160 171 LLLLLLLPLLFYRLGK-----KPGQDLTHLRA---QYRVQLTEWLQGQAELTLFG--AEDRYRQQLEQ-------TEQQW 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 520 IGRKTFMDLVTRPTTFLWLIATAGTLFV--------VSGAMQPVTLLPFLVLGT--TFGArLLGIAYGLGSIRGGLESAR 589
Cdd:PRK11160 234 LAAQRRQANLTGLSQALMILANGLTVVLmlwlaaggVGGNAQPGALIALFVFAAlaAFEA-LMPVAGAFQHLGQVIASAR 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 590 HIAvALDETELDVI--EAPVTADAVASVSFEGVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHD 666
Cdd:PRK11160 313 RIN-EITEQKPEVTfpTTSTAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 667 VERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIhERILRLPNGYDTVL- 745
Cdd:PRK11160 392 PQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLg 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 746 DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGR 825
Cdd:PRK11160 471 EGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQ 550
|
410 420
....*....|....*....|..
gi 491227761 826 VAETGTHTDLLANNGRYRRLWE 847
Cdd:PRK11160 551 IIEQGTHQELLAQQGRYYQLKQ 572
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
604-853 |
3.63e-58 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 209.18 E-value: 3.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 604 EAPVTADAVASVSFE-GV------TFGYrPG--VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRI 674
Cdd:PRK10789 296 EAPVVKDGSEPVPEGrGEldvnirQFTY-PQtdHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 675 DGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDT-VLDTDTQLSG 753
Cdd:PRK10789 375 HDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTeVGERGVMLSG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 754 GEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHT 833
Cdd:PRK10789 455 GQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD 534
|
250 260
....*....|....*....|
gi 491227761 834 DLLANNGRYRrlwEGHRHEQ 853
Cdd:PRK10789 535 QLAQQSGWYR---DMYRYQQ 551
|
|
| ViuB |
COG2375 |
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ... |
18-244 |
2.32e-56 |
|
NADPH-dependent ferric siderophore reductase, contains FAD-binding and SIP domains [Inorganic ion transport and metabolism];
Pssm-ID: 441942 [Multi-domain] Cd Length: 260 Bit Score: 194.71 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 18 HVATVVGTAPVAPNCVRITMSAPTLFEDLLHTPAEWLRFWFPDPDGGTSE----------------HQRAYTIVTTDEDA 81
Cdd:COG2375 16 RELTVVRVERLSPHMRRVTLGGEDLAGFASPGPDDHVKLFFPPPGGGEPVlptlddglalpgeerpVMRTYTVRRFDPEA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 82 GEFSIDVVIHEPAGPACQWAVAAQPGMTIPVVAFGsARFEVPADlPSGFLLIGDSASIPAINSIVAALPAEVDIEVYLER 161
Cdd:COG2375 96 GELDIDFVLHGDGGPASRWAARARPGDRVGILGPG-GSFVPPPD-ADWYLLAGDETALPAIARILEALPADARGTAVIEV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 162 HSPDDElIPLTTHPRRRLHWVDR---IDETSLAAAIEGRDW--SNWYGWASSESGSLKHLRKRLRDEFGFPKADVHAAAY 236
Cdd:COG2375 174 PDAADE-QPLPAPAGVEVTWLHRggaPPGSALLDAVRALELpdGDVYAWVAGEASAVRALRRHLRDERGLPRDRVRASGY 252
|
....*...
gi 491227761 237 WTFGRAMG 244
Cdd:COG2375 253 WRRGRAED 260
|
|
| siderophore_interacting |
cd06193 |
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like ... |
22-238 |
7.90e-56 |
|
Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99790 [Multi-domain] Cd Length: 235 Bit Score: 192.09 E-value: 7.90e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 22 VVGTAPVAPNCVRITMSAPTLFEDLLHTPAEWLRFWFPDPDGGTSE----------------HQRAYTIVTTDEDAGEFS 85
Cdd:cd06193 1 VVRVERLTPHMRRITLGGPDLAGFPSDGPDQHVKLLFPDPGQAPPVlpvlgrrrwppeeprpVMRTYTVRRFDPEAGELD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 86 IDVVIHEPAGPACQWAVAAQPGMTIPVVAFGSaRFEVPADlPSGFLLIGDSASIPAINSIVAALPAEVDIEVYLERHSPD 165
Cdd:cd06193 81 IDFVLHGDEGPASRWAASAQPGDTLGIAGPGG-SFLPPPD-ADWYLLAGDETALPAIAAILEELPADARGTALIEVPDAA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 166 DELiPLTTHPRRRLHWVDRIDE-----TSLAAAIEGRDWSNWYGWASSESGSLKHLRKRLRDEFGFPKADVHAAAYWT 238
Cdd:cd06193 159 DEQ-PLPAPAGVEVTWLHRGGAeagelALLAVRALAPPAGDGYVWIAGEAGAVRALRRHLREERGVPRAQVYASGYWR 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
615-838 |
2.06e-54 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 187.92 E-value: 2.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQ--DVQLVAGTVRENIALAC------PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALL 766
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGPenlglpREEIRERVEEALELVGLEHLADRPPH----------ELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 767 ADTPILILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
534-845 |
1.73e-53 |
|
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: 198.42 E-value: 1.73e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 534 TFLWliatAGTLFVVSGAMQPVTLLPFLVLGTTFGARLLGIAyglgSIRGGLESARHIAVALDETEL------DVIEAPV 607
Cdd:TIGR01193 395 VILW----TGAYLVMRGKLTLGQLITFNALLSYFLTPLENII----NLQPKLQAARVANNRLNEVYLvdsefiNKKKRTE 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 608 TADAVASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDEL 687
Cdd:TIGR01193 467 LNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 688 YAKVGFVFQDVQLVAGTVRENIAL-ACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGEKQRLTIARAL 765
Cdd:TIGR01193 547 RQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEgSSISGGQKQRIALARAL 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 766 LADTPILILDEATAFADPESEYLVQQALGRLIDnRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRL 845
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
304-845 |
2.65e-53 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 197.49 E-value: 2.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 304 GVLQAIITMVelAPFVVLVeLTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLDKLSR 383
Cdd:TIGR03797 145 GLLGTLLGML--VPIATGI-LIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 384 VPLGWFTQRGSGSVKKLIqDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMAL----ILLIPILVYLLTMMAMM 459
Cdd:TIGR03797 222 LPVSFFRQYSTGDLASRA-MGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKLALvavaLALVAIAVTLVLGLLQV 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 460 YQSGPKIVEASRwadrMSTESTAYLEGQPVIRIfggAAASSfkrrlddylRFLNDWQRPFIGRKTFMDLVTR----PTTF 535
Cdd:TIGR03797 301 RKERRLLELSGK----ISGLTVQLINGISKLRV---AGAEN---------RAFARWAKLFSRQRKLELSAQRienlLTVF 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 536 L--WLIATAGTLFVVSGAMQPV------TLLPFLVLGTTFGARLLGIAYGLGSIRGGL---ESARHIAVALDETELDVIE 604
Cdd:TIGR03797 365 NavLPVLTSAALFAAAISLLGGaglslgSFLAFNTAFGSFSGAVTQLSNTLISILAVIplwERAKPILEALPEVDEAKTD 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 605 APVTADAVAsvsFEGVTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLT 683
Cdd:TIGR03797 445 PGKLSGAIE---VDRVTFRYRPdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 684 PDELYAKVGFVFQDVQLVAGTVRENIALACPeATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIA 762
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVIsEGGGTLSGGQRQRLLIA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 763 RALLADTPILILDEATAFADPESEYLVQQALGRLidNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRY 842
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLF 678
|
...
gi 491227761 843 RRL 845
Cdd:TIGR03797 679 AQL 681
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
360-809 |
4.11e-53 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 193.73 E-value: 4.11e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 360 LWLHVVDLRFSADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWR 439
Cdd:TIGR02868 75 LVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVP 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 440 MALILLIPILVYLLTMMAMMYQSGpKIVEASRWADR--MSTESTAYLEGQPVIRIFGGAAASSFK-RRLDDYLRFLNDWQ 516
Cdd:TIGR02868 155 AALILAAGLLLAGFVAPLVSLRAA-RAAEQALARLRgeLAAQLTDALDGAAELVASGALPAALAQvEEADRELTRAERRA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 517 RPFIGRKTFMDLVTRPTTFLWLIATAGTLfVVSGAMQPVTL--LPFLVLGTT--FGArLLGIAYGLGSIRGGLEsaRHIA 592
Cdd:TIGR02868 234 AAATALGAALTLLAAGLAVLGALWAGGPA-VADGRLAPVTLavLVLLPLAAFeaFAA-LPAAAQQLTRVRAAAE--RIVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 593 VALDETELDVIEAPVTADAVA---SVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVER 669
Cdd:TIGR02868 310 VLDAAGPVAEGSAPAAGAVGLgkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQ 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 670 GAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTD- 748
Cdd:TIGR02868 390 GEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGg 469
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 749 TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRL 809
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
616-825 |
3.69e-52 |
|
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: 181.13 E-value: 3.69e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 616 SFEGVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQ--DVQLVAGTVRENIALACPEATDDDVESAARDAQIHERIlrlpnGYDTVLDTDT-QLSGGEKQRLTIARALLADTPI 771
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELV-----GLEGLRDRSPfTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 772 LILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGR 825
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
614-847 |
2.94e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 189.93 E-value: 2.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGF 693
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAGTVRENIALAcPEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPIL 772
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLgEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLWE 847
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
634-853 |
1.67e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 187.74 E-value: 1.67e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 634 VSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVeRGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALAC 713
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 714 PEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQA 792
Cdd:PRK11174 448 PDASDEQLQQALENAWVSEFLPLLPQGLDTPIgDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA 527
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 793 LGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLWEgHRHEQ 853
Cdd:PRK11174 528 LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA-HRQEE 587
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
579-838 |
3.17e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 170.85 E-value: 3.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 579 GSIRGGLESARHIAVALDETELDVIEAPVTADAVASVSFEGVTFGY----RPGVPVIHDVSLTLRHGTVTALVGPSGSGK 654
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 655 STLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KVGFVFQD--VQLVAG-TVRENIALAC-------PEATDDDV 721
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDpySSLNPRmTVGDIIAEPLrlhgllsRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 722 ESAARDAQIHERIL-RLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADpeseYLVQQALGRLID-- 798
Cdd:COG1123 385 AELLERVGLPPDLAdRYPH----------ELSGGQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQILNLLRdl 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 491227761 799 ----NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG1123 451 qrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
615-836 |
6.00e-45 |
|
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: 162.52 E-value: 6.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALAC---------PEATDDD-VESAARDAQIHERILRLpngYDTvldtdtqLSGGEKQRLTIAR 763
Cdd:COG1120 81 PQEPPAPFGlTVRELVALGRyphlglfgrPSAEDREaVEEALERTGLEHLADRP---VDE-------LSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRL-HTIADADQIVVLDHGRVAETGTHTDLL 836
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
614-831 |
9.67e-45 |
|
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: 160.27 E-value: 9.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPGVP-VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVG 692
Cdd:cd03369 6 EIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAGTVRENIalacpeatddDVESAARDAQIHErILRLPNGYDtvldtdtQLSGGEKQRLTIARALLADTPIL 772
Cdd:cd03369 86 IIPQDPTLFSGTIRSNL----------DPFDEYSDEEIYG-ALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGT 831
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
615-828 |
1.81e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.21 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG---VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA-- 689
Cdd:COG1136 5 LELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 --KVGFVFQDVQLVAG-TVRENIALAC------PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLT 760
Cdd:COG1136 85 rrHIGFVFQFFNLLPElTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRPS----------QLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 761 IARALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIADADQIVVLDHGRVAE 828
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
616-826 |
6.84e-44 |
|
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: 156.61 E-value: 6.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 616 SFEGVTFGYrPGV--PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGF 693
Cdd:cd03246 2 EVENVSFRY-PGAepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAGTVRENIalacpeatdddvesaardaqiherilrlpngydtvldtdtqLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491227761 774 LDEATAFADPESEYLVQQALGRL-IDNRTVLVIAHRLHTIADADQIVVLDHGRV 826
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
615-830 |
7.65e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 155.42 E-value: 7.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVpVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVER-----GAIRIDGTDIRTL--TPDEL 687
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLdvDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 688 YAKVGFVFQDVQLVAGTVRENIALACP-------EATDDDVESAARDAQIHERILRLPNGydtvldtdTQLSGGEKQRLT 760
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGLRlhgiklkEELDERVEEALRKAALWDEVKDRLHA--------LGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 761 IARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
615-838 |
1.38e-42 |
|
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: 162.77 E-value: 1.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVE---RGAIRIDGTDIRTLTPDELYAK 690
Cdd:COG1123 5 LEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQD--VQLVAGTVRENIALAC------PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIA 762
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALenlglsRAEARARVLELLEAVGLERRLDRYPH----------QLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 763 RALLADTPILILDEATAFADPESEYLVQQALGRLIDNR--TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
615-826 |
1.91e-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: 151.10 E-value: 1.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG---VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA-- 689
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 --KVGFVFQDVQLVAG-TVRENIALAC------PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLT 760
Cdd:cd03255 81 rrHIGFVFQSFNLLPDlTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYPS----------ELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 761 IARALLADTPILILDEATAFADPESEYLVQQALGRL--IDNRTVLVIAHRlHTIAD-ADQIVVLDHGRV 826
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHD-PELAEyADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
615-838 |
2.00e-41 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 151.58 E-value: 2.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVT--FGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA-- 689
Cdd:cd03258 2 IELKNVSkvFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 -KVGFVFQDVQLVAG-TVRENIALACPEAtddDVESAARDAQIHErILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLA 767
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPLEIA---GVPKAEIEERVLE-LLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 768 DTPILILDEATAFADPESeylVQQALGRLID-NR----TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:cd03258 158 NPKVLLCDEATSALDPET---TQSILALLRDiNRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
631-779 |
3.86e-41 |
|
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: 147.79 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAG-TVRENI 709
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 710 ALACPEATDDDVESAARDAQIHERiLRLPNGYDTVLD-TDTQLSGGEKQRLTIARALLADTPILILDEATA 779
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
615-837 |
6.39e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.21 E-value: 6.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLtPDELYAKVGFV 694
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARD-PAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALAcpeATDDDVESAARDAQIHE--RILRLPNGYDTVLDTdtqLSGGEKQRLTIARALLADTPI 771
Cdd:COG1131 79 PQEPALYPDlTVRENLRFF---ARLYGLPRKEARERIDEllELFGLTDAADRKVGT---LSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 772 LILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
615-831 |
7.75e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.04 E-value: 7.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdIRTLTPDELYA---K 690
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEirkK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQ--DVQLVAGTVRENIALAC------PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIA 762
Cdd:TIGR04520 79 VGMVFQnpDNQFVGATVEDDVAFGLenlgvpREEMRKRVDEALKLVGMEDFRDREPH----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 763 RALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIADADQIVVLDHGRVAETGT 831
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
616-826 |
1.66e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 616 SFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVF 695
Cdd:COG4619 2 ELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVAGTVRENIALACPEATDDDVESAARDAQihERiLRLPngyDTVLDTDT-QLSGGEKQRLTIARALLADTPILIL 774
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQLRERKFDRERALELL--ER-LGLP---PDILDKPVeRLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 775 DEATAFADPESEYLVQQALGRLI--DNRTVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
619-830 |
4.49e-40 |
|
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: 147.65 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 619 GVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KVGFV 694
Cdd:cd03257 8 SVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrkEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLV---AGTVRENIALACPEATDDDVESAARDAQI--------HERIL-RLPNgydtvldtdtQLSGGEKQRLTIA 762
Cdd:cd03257 88 FQDPMSSlnpRMTIGEQIAEPLRIHGKLSKKEARKEAVLlllvgvglPEEVLnRYPH----------ELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 763 RALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
620-837 |
1.47e-39 |
|
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: 146.87 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQD- 697
Cdd:COG1124 9 VSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 ------VQLVAGTVRENIALACPEATDDDVESAARDAQIHERIL-RLPNgydtvldtdtQLSGGEKQRLTIARALLADTP 770
Cdd:COG1124 89 yaslhpRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLdRYPH----------QLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 771 ILILDEATAFADPeseyLVQ-QALGRLIDNR-----TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:COG1124 159 LLLLDEPTSALDV----SVQaEILNLLKDLReerglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
615-828 |
1.49e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.97 E-value: 1.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KV 691
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAG-TVRENIALA--CPEATDDDVESAARDA----QIHERILRLPNgydtvldtdtQLSGGEKQRLTIARA 764
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALPlrVTGKSRKEIRRRVREVldlvGLSDKAKALPH----------ELSGGEQQRVAIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLidNR---TVLVIAHRLHTIADADQ-IVVLDHGRVAE 828
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEI--NRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
615-830 |
4.63e-39 |
|
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: 142.84 E-value: 4.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTpDELYAKVGF 693
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAGTVRENIAlacpeatdddvesaardaqiherilrlpngydtvldtdTQLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03247 80 LNQRPYLFDTTLRNNLG--------------------------------------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETG 830
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
616-825 |
6.35e-39 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 141.61 E-value: 6.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 616 SFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVF 695
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QdvqlvagtvrenialacpeatdddvesaardaqiherilrlpngydtvldtdtqLSGGEKQRLTIARALLADTPILILD 775
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491227761 776 EATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIADA-DQIVVLDHGR 825
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
618-830 |
1.23e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 141.80 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQD 697
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQLVagtvreNIA-LAcpeatdddvesaardaqihERILrlpngydtvldtdTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:cd03214 82 LELL------GLAhLA-------------------DRPF-------------NELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 777 ATAFADPESEYLVQQALGRLID--NRTVLVIAHRL-HTIADADQIVVLDHGRVAETG 830
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
615-839 |
4.16e-38 |
|
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: 142.43 E-value: 4.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KV 691
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDvqlvaG------TVRENIALACPEATDDDvesaarDAQIHERIL-------------RLPNgydtvldtdtQLS 752
Cdd:COG1127 85 GMLFQG-----GalfdslTVFENVAFPLREHTDLS------EAEIRELVLeklelvglpgaadKMPS----------ELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 753 GGEKQRLTIARALLADTPILILDEATAFADPESeylvQQALGRLIDNR------TVLVIAHRLHTIAD-ADQIVVLDHGR 825
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPIT----SAVIDELIRELrdelglTSVVVTHDLDSAFAiADRVAVLADGK 219
|
250
....*....|....
gi 491227761 826 VAETGTHTDLLANN 839
Cdd:COG1127 220 IIAEGTPEELLASD 233
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
615-837 |
1.29e-37 |
|
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: 140.71 E-value: 1.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KV 691
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAG-TVRENIAL------ACPEAT-DDDVESAARDAQIHERILRLPngydtvldtdTQLSGGEKQRLTIAR 763
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFplrehtRLSEEEiREIVLEKLEAVGLRGAEDLYP----------AELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTI-ADADQIVVLDHGRVAETGTHTDLLA 837
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
615-838 |
1.86e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 143.68 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGV--TFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARfhdVER---GAIRIDGTDIRTLTPDELY 688
Cdd:COG1135 2 IELENLskTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LERptsGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 689 A---KVGFVFQDVQLVAG-TVRENIALAcpeatdddVESAARD-AQIHERILRLpngydtvLD----TD------TQLSG 753
Cdd:COG1135 79 AarrKIGMIFQHFNLLSSrTVAENVALP--------LEIAGVPkAEIRKRVAEL-------LElvglSDkadaypSQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 754 GEKQRLTIARALLADTPILILDEATAFADPESeylVQQALGRLID-NR----TVLVIAHRLHTIAD-ADQIVVLDHGRVA 827
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPET---TRSILDLLKDiNRelglTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
250
....*....|.
gi 491227761 828 ETGTHTDLLAN 838
Cdd:COG1135 221 EQGPVLDVFAN 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
614-840 |
1.96e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 152.20 E-value: 1.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPGVP-VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVG 692
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAGTVRENIAlacP--EATDDDVESAARDAQIHERILRLPNGYDT-VLDTDTQLSGGEKQRLTIARALLADT 769
Cdd:PLN03130 1317 IIPQAPVLFSGTVRFNLD---PfnEHNDADLWESLERAHLKDVIRRNSLGLDAeVSEAGENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 770 PILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNG 840
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
341-840 |
5.09e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 147.82 E-value: 5.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 341 GFVFLVLLVLG---ATLGMALTLWLHVVDLRFSADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSlhylITHSIP 417
Cdd:PLN03232 950 GFYIVVYALLGfgqVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGD----IDRNVA 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 418 DAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMMA--MMYQSgpkiveASRWADRMS--TESTAY------LEGQ 487
Cdd:PLN03232 1026 NLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAayLYYQS------TSREVRRLDsvTRSPIYaqfgeaLNGL 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 488 PVIRIFGGA--AASSFKRRLDDYLRFL------NDWqrpfigrkTFMDLVTRPTTFLWLIATAGTLFVVSGAMQPV---T 556
Cdd:PLN03232 1100 SSIRAYKAYdrMAKINGKSMDNNIRFTlantssNRW--------LTIRLETLGGVMIWLTATFAVLRNGNAENQAGfasT 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 557 LLPFLVLGTTFGARLLGIAYGLGSIRGGLESARHIAVALD----ETELDVIEAPVTA-DAVASVSFEGVTFGYRPGVP-V 630
Cdd:PLN03232 1172 MGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDlpseATAIIENNRPVSGwPSRGSIKFEDVHLRYRPGLPpV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIA 710
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 711 lACPEATDDDVESAARDAQIHERILRLPNGYDT-VLDTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLV 789
Cdd:PLN03232 1332 -PFSEHNDADLWEALERAHIKDVIDRNPFGLDAeVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLI 1410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 491227761 790 QQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNG 840
Cdd:PLN03232 1411 QRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
615-826 |
9.85e-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: 133.29 E-value: 9.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTlTPDELYAKVGFV 694
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIalacpeatdddvesaardaqiherilrlpngydtvldtdtQLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03230 79 PEEPSLYENlTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 774 LDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
606-840 |
9.91e-36 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 147.01 E-value: 9.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 606 PVTADAVASVSFEGVTFGYRPGVP-VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP 684
Cdd:TIGR00957 1276 PSGWPPRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGL 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 685 DELYAKVGFVFQDVQLVAGTVRENIAlACPEATDDDVESAARDAQIHERILRLPNGYD-TVLDTDTQLSGGEKQRLTIAR 763
Cdd:TIGR00957 1356 HDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDhECAEGGENLSVGQRQLVCLAR 1434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNG 840
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG 1511
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
615-838 |
1.17e-35 |
|
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: 135.51 E-value: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALAcpeATDDDVESAARDAQIHErILRLPNgydtvLDTDT-------QLSGGEKQRLTIARALL 766
Cdd:cd03295 81 IQQIGLFPHmTVEENIALV---PKLLKWPKEKIRERADE-LLALVG-----LDPAEfadryphELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 767 ADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRL-HTIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
617-825 |
2.64e-35 |
|
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: 132.31 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 617 FEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPD--ELYAKVGFV 694
Cdd:cd03229 3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALAcpeatdddvesaardaqiherilrlpngydtvldtdtqLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03229 82 FQDFALFPHlTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDN--RTVLVIAHRLH-TIADADQIVVLDHGR 825
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
556-844 |
3.15e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 145.17 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 556 TLLPFLVLGTTFGArllgiaygLGSIRGGLESA-----RHIAVALDETELDV-----IEAPVTADAVASVSFEGVTFGY- 624
Cdd:PTZ00265 1105 SLFTFLFTGSYAGK--------LMSLKGDSENAklsfeKYYPLIIRKSNIDVrdnggIRIKNKNDIKGKIEIMDVNFRYi 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 -RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVER---------------------------------- 669
Cdd:PTZ00265 1177 sRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvn 1256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 670 --------------------GAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIALACPEATDDDVESAARDAQ 729
Cdd:PTZ00265 1257 efsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAA 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 730 IHERILRLPNGYDT-VLDTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIA 806
Cdd:PTZ00265 1337 IDEFIESLPNKYDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIA 1416
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 491227761 807 HRLHTIADADQIVVLDH-----GRVAETGTHTDLL-ANNGRYRR 844
Cdd:PTZ00265 1417 HRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVYKK 1460
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
618-838 |
4.35e-35 |
|
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: 133.72 E-value: 4.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVT--FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAK-VGFV 694
Cdd:cd03219 4 RGLTkrFG---GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALACPEATDDDVESAA---RDAQIHERILRLPN--GYDTVLDTDT-QLSGGEKQRLTIARALLA 767
Cdd:cd03219 81 FQIPRLFPElTVLENVMVAAQARTGSGLLLARarrEEREARERAEELLErvGLADLADRPAgELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 768 DTPILILDEATA-FADPESEylvqqALGRLI-----DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:cd03219 161 DPKLLLLDEPAAgLNPEETE-----ELAELIrelreRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNN 233
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
615-830 |
5.21e-35 |
|
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: 132.64 E-value: 5.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGFV 694
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALACPEATdddVESAARDAQIHERILRLpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTPIL 772
Cdd:cd03259 78 FQDYALFPHlTVAENIAFGLKLRG---VPKAEIRARVRELLELV--GLEGLLNRYpHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLIDNR---TVLVIAHRLHTIADADQIVVLDHGRVAETG 830
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELgitTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
613-838 |
8.05e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.96 E-value: 8.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRPGV-PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKV 691
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQ--DVQLVAGTVRENIALAC------PEATDDDVESAARDAQIHErilrlpngydtVLDTDTQ-LSGGEKQRLTIA 762
Cdd:PRK13632 86 GIIFQnpDNQFIGATVEDDIAFGLenkkvpPKKMKDIIDDLAKKVGMED-----------YLDKEPQnLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 763 RALLADTPILILDEATAFADPESEYLVQQALGRLIDNR--TVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
615-828 |
1.34e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 132.52 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRtltpdELYAKVGFV 694
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG---TVRENIALAC---------PEATDDD-VESA--------ARDAQIHErilrlpngydtvldtdtqLSG 753
Cdd:COG1121 81 PQRAEVDWDfpiTVRDVVLMGRygrrglfrrPSRADREaVDEAlervgledLADRPIGE------------------LSG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 754 GEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAE 828
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
635-839 |
1.61e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.80 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 635 SLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGFVFQDVQLVAG-TVRENIALAC 713
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLFPHlTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 714 PEA---TDDD---VESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADP---- 783
Cdd:COG3840 97 RPGlklTAEQraqVEQALERVGLAGLLDRLPG----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDPalrq 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 784 ESEYLVQQALGRLidNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLANN 839
Cdd:COG3840 167 EMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
615-838 |
2.87e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 131.27 E-value: 2.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVT--FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIrTLTPDELYA--- 689
Cdd:COG1126 2 IEIENLHksFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 KVGFVFQDVQLVAG-TVRENIALAcPE----ATDDDVESAARDA----QIHERILRLPNgydtvldtdtQLSGGEKQRLT 760
Cdd:COG1126 78 KVGMVFQQFNLFPHlTVLENVTLA-PIkvkkMSKAEAEERAMELlervGLADKADAYPA----------QLSGGQQQRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 761 IARALLADTPILILDEATAFADPE--SEYL-VQQALGRliDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLL 836
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDPElvGEVLdVMRDLAK--EGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFF 224
|
..
gi 491227761 837 AN 838
Cdd:COG1126 225 EN 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
618-831 |
6.42e-34 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 130.93 E-value: 6.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVT--FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELyAKVGFV- 694
Cdd:COG0411 8 RGLTkrFG---GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI-ARLGIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 -FQDVQLVAG-TVRENIALACPEATDDDVESA--------ARDAQIHERILRLPN--GYDTVLDTDT-QLSGGEKQRLTI 761
Cdd:COG0411 84 tFQNPRLFPElTVLENVLVAAHARLGRGLLAAllrlprarREEREARERAEELLErvGLADRADEPAgNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 762 ARALLADTPILILDEATA-FADPESEYLVqQALGRLIDNR--TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGT 831
Cdd:COG0411 164 ARALATEPKLLLLDEPAAgLNPEETEELA-ELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
615-829 |
7.87e-34 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 129.51 E-value: 7.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG---VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDelyakV 691
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVA-GTVRENIALAcPEATDddvesaARDAQIHERILRLpngYDTVLDTDT------QLSGGEKQRLTIARA 764
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG-LELQG------VPKAEARERAEEL---LELVGLSGFenayphQLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLI--DNRTVLVIAHRLH-TIADADQIVVLD--HGRVAET 829
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTHDIDeAVFLADRVVVLSarPGRIVAE 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
615-845 |
8.33e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 8.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYrPGV--PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdiRTLTPD---ELYA 689
Cdd:PRK13635 6 IRVEHISFRY-PDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEEtvwDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 KVGFVFQ--DVQLVAGTVRENIALAcpeatdddVESAA--RDAQIhERI---LRLPNGYDTVLDTDTQLSGGEKQRLTIA 762
Cdd:PRK13635 82 QVGMVFQnpDNQFVGATVQDDVAFG--------LENIGvpREEMV-ERVdqaLRQVGMEDFLNREPHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 763 RALLADTPILILDEATAFADPESEYLVQQALGRLIDNR--TVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNG 840
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
....*
gi 491227761 841 RYRRL 845
Cdd:PRK13635 233 MLQEI 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
618-838 |
1.03e-33 |
|
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: 129.09 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAK-VGFVFQ 696
Cdd:cd03224 4 ENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 DVQLVAG-TVRENIALACPEATDDDVEsaARDAQIHERILRLpngyDTVLDTD-TQLSGGEKQRLTIARALLADTPILIL 774
Cdd:cd03224 83 GRRIFPElTVEENLLLGAYARRRAKRK--ARLERVYELFPRL----KERRKQLaGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 775 DEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
629-837 |
2.27e-33 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 129.26 E-value: 2.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVREN 708
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 709 IALACpEATDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEY 787
Cdd:cd03288 115 LDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVtEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491227761 788 LVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLA 837
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLA 243
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
618-826 |
4.21e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 126.99 E-value: 4.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRtltPDELYAKVGFVFQD 697
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 V--QLVAGTVRENIALACPEAtdddvesaARDAQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKEL--------DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 776 EATAFADPESEYLVQQALGRLI-DNRTVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
615-830 |
4.54e-33 |
|
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: 126.92 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVpVIHDVSLTLRHGtVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTlTPDELYAKVGFV 694
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALAcpeATDDDVESAARDAQIhERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03264 78 PQEFGVYPNfTVREFLDYI---AWLKGIPSKEVKARV-DEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
589-838 |
1.74e-32 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 136.45 E-value: 1.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 589 RHIAVALDETELDVIE-------APVTADAvASVSFEGVTFGYRPGVP-VIHDVSLTLRHGTVTALVGPSGSGKSTLASL 660
Cdd:PTZ00243 1277 RRTGMAADVTGTVVIEpasptsaAPHPVQA-GSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLT 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 661 LARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVRENIAlacP--EATDDDVESAARDAQIHERILRLP 738
Cdd:PTZ00243 1356 FMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD---PflEASSAEVWAALELVGLRERVASES 1432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 739 NGYDT-VLDTDTQLSGGEKQRLTIARALLA-DTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADAD 816
Cdd:PTZ00243 1433 EGIDSrVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYD 1512
|
250 260
....*....|....*....|..
gi 491227761 817 QIVVLDHGRVAETGTHTDLLAN 838
Cdd:PTZ00243 1513 KIIVMDHGAVAEMGSPRELVMN 1534
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
615-829 |
2.48e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 126.36 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG---VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDelyakV 691
Cdd:COG1116 8 LELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDvqlvAG-----TVRENIALACPEAtddDVESAARDAQIhERILRL----------PNgydtvldtdtQLSGGEK 756
Cdd:COG1116 83 GVVFQE----PAllpwlTVLDNVALGLELR---GVPKAERRERA-RELLELvglagfedayPH----------QLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 757 QRLTIARALLADTPILILDEatAFA--DPESEYLVQQALGRLID--NRTVLVIAH------RLhtiadADQIVVLDH--G 824
Cdd:COG1116 145 QRVAIARALANDPEVLLMDE--PFGalDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpG 217
|
....*
gi 491227761 825 RVAET 829
Cdd:COG1116 218 RIVEE 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
615-825 |
3.78e-32 |
|
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: 124.12 E-value: 3.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGV----PVIHDVSLTLRHGTVTALVGPSGSGKSTL-ASLLARFHdVERGAIRIDGTdirtltpdelya 689
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGELE-KLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 kVGFVFQDVQLVAGTVRENIALACP---EATDDDVESAA--RDAQIherilrLPNGYDTVL-DTDTQLSGGEKQRLTIAR 763
Cdd:cd03250 68 -IAYVSQEPWIQNGTIRENILFGKPfdeERYEKVIKACAlePDLEI------LPDGDLTEIgEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 764 ALLADTPILILDEATAFADPE-SEYLVQQAL-GRLIDNRTVLVIAHRLHTIADADQIVVLDHGR 825
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
618-838 |
2.15e-31 |
|
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: 122.78 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAK-VGFVFQ 696
Cdd:COG0410 7 ENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 DVQLVAG-TVRENIALACpEATDDDVESAARDAQIHERILRL------PNGydtvldtdtQLSGGEKQRLTIARALLADT 769
Cdd:COG0410 86 GRRIFPSlTVEENLLLGA-YARRDRAEVRADLERVYELFPRLkerrrqRAG---------TLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 770 PILILDEATAFADPeseyLVQQALGRLID--NR---TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG0410 156 KLLLLDEPSLGLAP----LIVEEIFEIIRrlNRegvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLAD 226
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
630-826 |
2.18e-31 |
|
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: 122.25 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPD--ELYAKVGFVFQDVQLVAG-TVR 706
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIALACPEA---TDDDVESAARDA----QIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATA 779
Cdd:cd03262 95 ENITLAPIKVkgmSKAEAEERALELlekvGLADKADAYPA----------QLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491227761 780 FADPEseyLVQQALGRLID----NRTVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:cd03262 165 ALDPE---LVGEVLDVMKDlaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
612-821 |
2.52e-30 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 129.38 E-value: 2.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 612 VASVSFEGVTFGY--RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRI-DGTDIRTLTPDELY 688
Cdd:PTZ00265 380 IKKIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 689 AKVGFVFQDVQLVAGTVRENI-----ALACPEA----------------------------------------------- 716
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNSIKNNIkyslySLKDLEAlsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 717 -----TDDDVESAARDAQIHERILRLPNGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQ 790
Cdd:PTZ00265 540 nyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|...
gi 491227761 791 QALGRLI--DNRTVLVIAHRLHTIADADQIVVL 821
Cdd:PTZ00265 620 KTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
633-830 |
5.30e-30 |
|
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: 117.98 E-value: 5.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGFVFQDVQLVAG-TVRENIAL 711
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 712 A------CPEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADPES 785
Cdd:cd03298 94 GlspglkLTAEDRQAIEVALARVGLAGLEKRLPG----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491227761 786 EYLVQQALGRLIDNR--TVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03298 164 RAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
628-833 |
6.06e-30 |
|
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: 118.69 E-value: 6.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA----KVGFVFQDVQLVAG 703
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlrarHVGFVFQSFQLLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 -TVRENIALACPEATDDDVESAARDA----QIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:COG4181 105 lTALENVMLPLELAGRRDARARARALlervGLGHRLDHYPA----------QLSGGEQQRVALARAFATEPAILFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 779 AFADPESEYLVQQALGRLidNR---TVLVIA-HRLHTIADADQIVVLDHGRVAETGTHT 833
Cdd:COG4181 175 GNLDAATGEQIIDLLFEL--NRergTTLVLVtHDPALAARCDRVLRLRAGRLVEDTAAT 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
633-838 |
9.85e-30 |
|
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: 118.21 E-value: 9.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGFVFQDVQLVAG-TVRENIAL 711
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHmTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 712 ACPEATDDDVESAARDAQIHERIlrlpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQ 790
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKpETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491227761 791 QALGRLIDNRTVLVIaHRLHTIADA----DQIVVLDHGRVAETGTHTDLLAN 838
Cdd:cd03299 170 EELKKIRKEFGVTVL-HVTHDFEEAwalaDKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
615-829 |
1.35e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.22 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE-LYAKVGF 693
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQdvqlvagtvrenialacpeatdddvesaardaqiherilrlpngydtvldtdtqLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03216 80 VYQ------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 774 LDEATA-FADPESEYLVQQaLGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVAET 829
Cdd:cd03216 106 LDEPTAaLTPAEVERLFKV-IRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
615-838 |
2.34e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.36 E-value: 2.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARF---HDVERGAIRIDGTDIRTLTPDELYAK 690
Cdd:PRK13640 6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQ--DVQLVAGTVRENIALAcpeatdddVESAARDAQIHERILR--LPN-GYDTVLDTDTQ-LSGGEKQRLTIARA 764
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFG--------LENRAVPRPEMIKIVRdvLADvGMLDYIDSEPAnLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLI--DNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
613-827 |
2.47e-29 |
|
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: 115.73 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRPGV-----PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVER--GAIRIDGTDIRtltPD 685
Cdd:cd03213 2 VTLSFRNLTVTVKSSPsksgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLD---KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 686 ELYAKVGFVFQDVQLVAG-TVRENIALAcpeatdddvesaardAQiheriLRlpngydtvldtdtQLSGGEKQRLTIARA 764
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTlTVRETLMFA---------------AK-----LR-------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHT--IADADQIVVLDHGRVA 827
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
617-827 |
3.42e-29 |
|
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: 116.90 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 617 FEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KVGF 693
Cdd:cd03256 3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAG-TVRENI-------------------------ALACPEATDDDvESAARDAQiherilrlpngydtvldt 747
Cdd:cd03256 83 IFQQFNLIERlSVLENVlsgrlgrrstwrslfglfpkeekqrALAALERVGLL-DKAYQRAD------------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 748 dtQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLI--DNRTVLVIAHRLHTIAD-ADQIVVLDHG 824
Cdd:cd03256 144 --QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAREyADRIVGLKDG 221
|
...
gi 491227761 825 RVA 827
Cdd:cd03256 222 RIV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
626-835 |
4.55e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 122.05 E-value: 4.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 626 PGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE-LYAKVGFVFQDVQLVAG- 703
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALacpeatddDVESAAR----DAQIHERILRLPNGYDTVLDTDTQ---LSGGEKQRLTIARALLADTPILILDE 776
Cdd:COG1129 95 SVAENIFL--------GREPRRGglidWRAMRRRARELLARLGLDIDPDTPvgdLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 777 ATA-FADPESEYLVqqalgRLI-----DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDL 835
Cdd:COG1129 167 PTAsLTEREVERLF-----RIIrrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
616-827 |
5.36e-29 |
|
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: 115.32 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 616 SFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRtltpdELYAKVGFVF 695
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 Q----DVQLVAgTVRENIALAC----------PEATDDDVESAA--------RDAQIherilrlpngydtvldtdTQLSG 753
Cdd:cd03235 75 QrrsiDRDFPI-SVRDVVLMGLyghkglfrrlSKADKAKVDEALervglselADRQI------------------GELSG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 754 GEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRVA 827
Cdd:cd03235 136 GQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
620-838 |
6.83e-29 |
|
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: 118.23 E-value: 6.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHD---VERGAIRIDGTDIRTLTPDEL----YAKV 691
Cdd:COG0444 9 VYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELrkirGREI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQD-------VQlvagTVRENIAlacpEA--TDDDVESAARDAQIHE--RILRLPNGYDTVLDTDTQLSGGEKQRLT 760
Cdd:COG0444 89 QMIFQDpmtslnpVM----TVGDQIA----EPlrIHGGLSKAEARERAIEllERVGLPDPERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 761 IARALLADTPILILDEATAFADPeseyLVQ-QALGRLID-----NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHT 833
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDV----TIQaQILNLLKDlqrelGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVE 236
|
....*
gi 491227761 834 DLLAN 838
Cdd:COG0444 237 ELFEN 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
615-829 |
7.84e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 7.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVT--FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP-DELYAKV 691
Cdd:COG3845 6 LELRGITkrFG---GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAG-TVRENIALAcpeatDDDVESAARD-AQIHERILRLPNGYDTVLDTDT---QLSGGEKQRLTIARALL 766
Cdd:COG3845 83 GMVHQHFMLVPNlTVAENIVLG-----LEPTKGGRLDrKAARARIRELSERYGLDVDPDAkveDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 767 ADTPILILDEATAFADP-ESEYLVqQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVAET 829
Cdd:COG3845 158 RGARILILDEPTAVLTPqEADELF-EILRRLAAEgKSIIFITHKLREVMAiADRVTVLRRGKVVGT 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
621-831 |
1.25e-28 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 114.52 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 621 TFGYRPgVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTlTPDELYAKVGFVFQ-DVQ 699
Cdd:cd03263 9 TYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQfDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 700 LVAGTVRENIALACP----EATDDDVESAArdaqiHERILRLPNgydtVLDTD-TQLSGGEKQRLTIARALLADTPILIL 774
Cdd:cd03263 87 FDELTVREHLRFYARlkglPKSEIKEEVEL-----LLRVLGLTD----KANKRaRTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 775 DEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTI-ADADQIVVLDHGRVAETGT 831
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIGS 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
613-831 |
1.56e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 117.89 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVG 692
Cdd:COG3842 4 PALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--RNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLva-gTVRENIA--LacpeaTDDDVESAARDAQIHErIL----------RLPNgydtvldtdtQLSGGEKQRL 759
Cdd:COG3842 81 MVFQDYALfphlTVAENVAfgL-----RMRGVPKAEIRARVAE-LLelvglegladRYPH----------QLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 760 TIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNR--TVLVIAHrlhtiaD-------ADQIVVLDHGRVAETG 830
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH------DqeealalADRIAVMNDGRIEQVG 218
|
.
gi 491227761 831 T 831
Cdd:COG3842 219 T 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
604-830 |
1.63e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 115.13 E-value: 1.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 604 EAPVTADAVASVsfEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGA-----IRIDGTD 678
Cdd:COG1117 3 APASTLEPKIEV--RNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 679 I--RTLTPDELYAKVGFVFQDVQLVAGTVRENIALAC-------PEATDDDVESAARDAQIherilrlpngYDTV---LD 746
Cdd:COG1117 80 IydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiksKSELDEIVEESLRKAAL----------WDEVkdrLK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 747 TD-TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHG 824
Cdd:COG1117 150 KSaLGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARvSDYTAFFYLG 229
|
....*.
gi 491227761 825 RVAETG 830
Cdd:COG1117 230 ELVEFG 235
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
623-838 |
2.51e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 117.21 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 623 GYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARfhdVER---GAIRIDGTDIRTLTPDELYA---KVGFVFQ 696
Cdd:PRK11153 13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINL---LERptsGRVLVDGQDLTALSEKELRKarrQIGMIFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 DVQLVAG-TVRENIALAcpeatdddVESAARD-AQIHERILRLpngYDTVLDTD------TQLSGGEKQRLTIARALLAD 768
Cdd:PRK11153 90 HFNLLSSrTVFDNVALP--------LELAGTPkAEIKARVTEL---LELVGLSDkadrypAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 769 TPILILDEATAFADPESeylVQQALGRLID-NR----TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK11153 159 PKVLLCDEATSALDPAT---TRSILELLKDiNRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
615-830 |
4.83e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.45 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDV--QLVAGTVRENIALAcP---EATDDDVESAARDAqiheriLRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADT 769
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFG-PvnmGLDKDEVERRVEEA------LKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 770 PILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:PRK13647 158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
615-826 |
5.34e-28 |
|
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: 112.50 E-value: 5.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTL----TPdELYAK 690
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgraIP-YLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQDVQLVAG-TVRENIALAC------PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIAR 763
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFALevtgvpPREIRKRVPAALELVGLSHKHRALPA----------ELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQ--IVVLDHGRV 826
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
625-836 |
6.60e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.33 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDEL---------YAKVGFVF 695
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrravlpqHSSLSFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 qdvqlvagTVRENIALacpeATDDDVESAARDAQIHERILRLpngydtvldTD---------TQLSGGEKQRLTIARALL 766
Cdd:PRK13548 92 --------TVEEVVAM----GRAPHGLSRAEDDALVAAALAQ---------VDlahlagrdyPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 767 ------ADTPILILDEATAFADPeseyLVQQALGRLIDNRT------VLVIAHRLH-TIADADQIVVLDHGRVAETGTHT 833
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDL----AHQHHVLRLARQLAherglaVIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
...
gi 491227761 834 DLL 836
Cdd:PRK13548 227 EVL 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
613-831 |
1.05e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.56 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVG 692
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLV-AGTVRENIALAC-----PEAT-DDDVESAARDAQIHERILRLPngydtvldtdTQLSGGEKQRLTIARAL 765
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPLklrkvPKAEiDRRVREAAELLGLEDLLDRKP----------KQLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 766 LADTPILILDEATAFADPEseyL----------VQQALGrlidnRTVLVIAHrlhtiaD-------ADQIVVLDHGRVAE 828
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAK---LrvemraeikrLHRRLG-----TTTIYVTH------DqveamtlADRIAVMNDGRIQQ 214
|
...
gi 491227761 829 TGT 831
Cdd:COG3839 215 VGT 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
615-830 |
4.15e-27 |
|
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: 109.65 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGFV 694
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALAC------PEATDDDVESAARDAQIHERILRLPngydtvldtdTQLSGGEKQRLTIARALLA 767
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGLklrkvpKDEIDERVREVAELLQIEHLLDRKP----------KQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 768 DTPILILDEATAFADPESEYLVQQALGRLIDN--RTVLVIAH-RLHTIADADQIVVLDHGRVAETG 830
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| SIP |
pfam04954 |
Siderophore-interacting protein; |
127-240 |
2.38e-26 |
|
Siderophore-interacting protein;
Pssm-ID: 428217 Cd Length: 119 Bit Score: 104.22 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 127 PSGFLLIGDSASIPAINSIVAALPAEVDIEVYLERHSPDDELiPLTTHPRRRLHWVDR----IDETSLAAAIEGRDW--S 200
Cdd:pfam04954 1 ADWYLLAGDETALPAIARILEELPADARGTAVIEVPDAADRQ-PLPTPAGVEVHWLVRggaaGAGALLADALRALDLpaG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 491227761 201 NWYGWASSESGSLKHLRKRLRDEFGFPKADVHAAAYWTFG 240
Cdd:pfam04954 80 DPYVWVAGEAAAVRALRRHLRRERGLPRERVRASGYWRRG 119
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
628-838 |
3.46e-26 |
|
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: 108.88 E-value: 3.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA----KVGFVFQDVQLVAG 703
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 -TVRENIALACPEATDDDVESAARDAQIHERI------LRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:cd03294 117 rTVLENVAFGLEVQGVPRAEREERAAEALELVglegweHKYPD----------ELSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 777 ATAFADPESEYLVQQALGRLIDN--RTVLVIAHRL-HTIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:cd03294 187 AFSALDPLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
613-823 |
4.81e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.41 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLtPDELYAKVG 692
Cdd:COG4133 1 MMLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDA-REDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAG-TVRENIALAC----PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLA 767
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWAalygLRADREAIDEALEAVGLAGLADLPVR----------QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 768 DTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIA-HRLHTIADADQIVVLDH 823
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGDF 205
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
614-835 |
8.18e-26 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 107.04 E-value: 8.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGF 693
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAG-TVRENIALACPEATDDDVESAAR-DAQIHE--RILRLPNGYDTVldtDTQLSGGEKQRLTIARALLADT 769
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEiRAKVHEllKLVQLDWLADRY---PAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 770 PILILDEATAFADPESEYLVQQALGRLIDN---RTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDL 835
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
618-831 |
1.05e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.09 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQD 697
Cdd:COG4604 5 KNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQLVAG-TVRENIA----------LacpeaTDDD---VESAARDAQIHEriLRlpngyDTVLDtdtQLSGGEKQRLTIAR 763
Cdd:COG4604 84 NHINSRlTVRELVAfgrfpyskgrL-----TAEDreiIDEAIAYLDLED--LA-----DRYLD---ELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 764 ALLADTPILILDEATAFADPesEYLVQ--QALGRLID--NRTVLVIahrLHTI----ADADQIVVLDHGRVAETGT 831
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDM--KHSVQmmKLLRRLADelGKTVVIV---LHDInfasCYADHIVAMKDGRVVAQGT 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
614-838 |
1.18e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 109.08 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRT-LTPDELyaKVG 692
Cdd:COG1118 2 SIEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRER--RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLva-gTVRENIALACPEATDDDVESAARDAQIHERI-L-----RLPNgydtvldtdtQLSGGEKQRLTIARAL 765
Cdd:COG1118 79 FVFQHYALfphmTVAENIAFGLRVRPPSKAEIRARVEELLELVqLegladRYPS----------QLSGGQRQRVALARAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 766 LADTPILILDEatAFA--DPESEYLVQQALGRLID--NRTVLVIAH------RLhtiadADQIVVLDHGRVAETGTHTDL 835
Cdd:COG1118 149 AVEPEVLLLDE--PFGalDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEV 221
|
...
gi 491227761 836 LAN 838
Cdd:COG1118 222 YDR 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
629-831 |
3.06e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.87 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQdvQLVAG---TV 705
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ--HHLTPegiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIALA-CP------EATDDD---VESAARDAQIHERILRLPngydtvldtdTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:PRK11231 94 RELVAYGrSPwlslwgRLSAEDnarVNQAMEQTRINHLADRRL----------TDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 776 EATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGT 831
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGT 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
614-846 |
3.60e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 3.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE--- 686
Cdd:PRK13646 2 TIRFDNVSYTYQKGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 687 -LYAKVGFVFQ--DVQLVAGTVRENIALAcPEATDDDVESAARDAqiHERILRLPNGYDTVLDTDTQLSGGEKQRLTIAR 763
Cdd:PRK13646 82 pVRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQALGRLI--DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLaNNG 840
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF-KDK 237
|
....*.
gi 491227761 841 RYRRLW 846
Cdd:PRK13646 238 KKLADW 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
615-838 |
4.12e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.79 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVT--FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE--LYAK 690
Cdd:PRK09493 2 IEFKNVSkhFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDErlIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQDVQLVAG-TVRENIALAcP----EATDDDVESAARD----AQIHERILRLPNgydtvldtdtQLSGGEKQRLTI 761
Cdd:PRK09493 79 AGMVFQQFYLFPHlTALENVMFG-PlrvrGASKEEAEKQAREllakVGLAERAHHYPS----------ELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 762 ARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAhrLHTIADADQI----VVLDHGRVAETGTHTDLLA 837
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIV--THEIGFAEKVasrlIFIDKGRIAEDGDPQVLIK 225
|
.
gi 491227761 838 N 838
Cdd:PRK09493 226 N 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
614-831 |
1.24e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 104.74 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDI--RTLTPDEL 687
Cdd:PRK13637 2 SIKIENLTHIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 688 YAKVGFVFQ--DVQLVAGTVRENIALAcPE---ATDDDVESAARDAQiheRILRLPngYDTVLDTDT-QLSGGEKQRLTI 761
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFG-PInlgLSEEEIENRVKRAM---NIVGLD--YEDYKDKSPfELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 762 ARALLADTPILILDEATAFADPES--EYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGT 831
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGrdEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
615-835 |
1.24e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.45 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVP-VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGF 693
Cdd:PRK13648 8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQ--DVQLVAGTVRENIAL-----ACP-EATDDDVESAARDAQIHERILRLPNGydtvldtdtqLSGGEKQRLTIARAL 765
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFglenhAVPyDEMHRRVSEALKQVDMLERADYEPNA----------LSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 766 LADTPILILDEATAFADPESeylvQQALGRLI------DNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDL 835
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDA----RQNLLDLVrkvkseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
592-824 |
1.37e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 592 AVALDETE-LDVIEAPVTADAVASVSFEGVTFgYRP-GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVER 669
Cdd:COG4178 339 EEALEAADaLPEAASRIETSEDGALALEDLTL-RTPdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 670 GAIRIdgtdirtltPDElyAKVGFVFQDVQLVAGTVREniALACPEA----TDDDVESAARDAQIHERILRLpngyDTVL 745
Cdd:COG4178 418 GRIAR---------PAG--ARVLFLPQRPYLPLGTLRE--ALLYPATaeafSDAELREALEAVGLGHLAERL----DEEA 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 746 DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHG 824
Cdd:COG4178 481 DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
630-835 |
2.85e-24 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 102.22 E-value: 2.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAK-VGFVFQDVQLVAG-TVRE 707
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFPRlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 708 NIAL---ACPeatdddvesaARDAQIHERILRL-PngydtVLDTDTQ-----LSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:TIGR03410 95 NLLTglaALP----------RRSRKIPDEIYELfP-----VLKEMLGrrggdLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 779 AFADPESEYLVQQALGRLIDNR--TVLVIAHRLH-TIADADQIVVLDHGRVAETGTHTDL 835
Cdd:TIGR03410 160 EGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
635-839 |
3.73e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.97 E-value: 3.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 635 SLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGFVFQDVQLVAG-TVRENIALAC 713
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR--RPVSMLFQENNLFSHlTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 714 -P-----EATDDDVESAARDAQIHERILRLPngydtvldtdTQLSGGEKQRLTIARALLADTPILILDEATAFADP---- 783
Cdd:PRK10771 97 nPglklnAAQREKLHAIARQMGIEDLLARLP----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalrq 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 784 ESEYLVQQalgrLIDNR--TVLVIAHRLhtiADADQI----VVLDHGRVAETGTHTDLLANN 839
Cdd:PRK10771 167 EMLTLVSQ----VCQERqlTLLMVSHSL---EDAARIaprsLVVADGRIAWDGPTDELLSGK 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
615-838 |
9.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.99 E-value: 9.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP-DELYAKVGF 693
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQ--DVQLVAGTVRENIALA----C--PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARAL 765
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpenlClpPIEIRKRVDRALAEIGLEKYRHRSPK----------TLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 766 LADTPILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
620-837 |
1.60e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.35 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGYRPGV--PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdiRTLTPD---ELYAKVGFV 694
Cdd:PRK13650 10 LTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEEnvwDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQ--DVQLVAGTVRENIALACPEATDDDVESAARdaqIHErILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPIL 772
Cdd:PRK13650 87 FQnpDNQFVGATVEDDVAFGLENKGIPHEEMKER---VNE-ALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
615-835 |
3.17e-23 |
|
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: 99.23 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVT--FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVG 692
Cdd:cd03300 1 IELENVSkfYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAG-TVRENIALA-----CPEAT-DDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARAL 765
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrlkkLPKAEiKERVAEALDLVQLEGYANRKPS----------QLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 766 LADTPILILDEATAFADPESEYLVQQALGRLIDNR--TVLVIAH-RLHTIADADQIVVLDHGRVAETGTHTDL 835
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
623-821 |
5.19e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.25 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 623 GYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLV 701
Cdd:PRK10247 14 GYLAGdAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 702 AGTVRENIALAC--------PEATDDDVESaardaqiheriLRLPngyDTVLDTD-TQLSGGEKQRLTIARALLADTPIL 772
Cdd:PRK10247 94 GDTVYDNLIFPWqirnqqpdPAIFLDDLER-----------FALP---DTILTKNiAELSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLIDNRTVLVI--AHRLHTIADADQIVVL 821
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
614-835 |
6.96e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.43 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE--- 686
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 687 -LYAKVGFVFQ--DVQLVAGTVRENIALAcPE---ATDDDVESAARDAqiheriLRLPNGYDTVLDTDT-QLSGGEKQRL 759
Cdd:PRK13649 82 qIRKKVGLVFQfpESQLFEETVLKDVAFG-PQnfgVSQEEAEALAREK------LALVGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 760 TIARALLADTPILILDEATAFADPESEYLVQQALGRL-IDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDL 835
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
633-830 |
1.84e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 96.60 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRhGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGT---DIRT---LTPDElyAKVGFVFQDVQLVAG-TV 705
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQQ--RKIGLVFQQYALFPHlNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIALACPeatdddVESAARDAQIHERILRLPnGYDTVLDTDT-QLSGGEKQRLTIARALLADTPILILDEATAFADPE 784
Cdd:cd03297 93 RENLAFGLK------RKRNREDRISVDELLDLL-GLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491227761 785 SEYLVQQALGRL--IDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03297 166 LRLQLLPELKQIkkNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
615-836 |
1.88e-22 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 97.46 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFgYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFH------DVERGAIRIDGTDIRtltpdELY 688
Cdd:COG1119 4 LELRNVTV-RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygnDVRLFGERRGGEDVW-----ELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 689 AKVGFVFQDVQL---VAGTVRE--------NIALAcPEATDDDVESAardaqiHERILRLpnGYDTVLDTD-TQLSGGEK 756
Cdd:COG1119 78 KRIGLVSPALQLrfpRDETVLDvvlsgffdSIGLY-REPTDEQRERA------RELLELL--GLAHLADRPfGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 757 QRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDN--RTVLVIAHRLHTIADA-DQIVVLDHGRVAETGTHT 833
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
...
gi 491227761 834 DLL 836
Cdd:COG1119 229 EVL 231
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
633-859 |
2.26e-22 |
|
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: 99.79 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDG-----TDIRTLTPDELYAkVGFVFQDVQLVAG-TVR 706
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdSARGIFLPPHRRR-IGYVFQEARLFPHlSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIALACPEAtdddvESAARDAQIHERILRLpnGYDTVLD-TDTQLSGGEKQRLTIARALLADTPILILDEATAFADPES 785
Cdd:COG4148 96 GNLLYGRKRA-----PRAERRISFDEVVELL--GIGHLLDrRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 786 EYLVQQALGRLIDNRT--VLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAnngRYRRLWEGHRHEQSSVLAG 859
Cdd:COG4148 169 KAEILPYLERLRDELDipILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLS---RPDLLPLAGGEEAGSVLEA 242
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
615-840 |
2.41e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.17 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRI------DGTDIRTLTP 684
Cdd:PRK13634 3 ITFQKVEHRYQYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 685 deLYAKVGFVFQ--DVQLVAGTVRENIALAcPE---ATDDDVESAARDAqiheriLRLPNGYDTVLD-TDTQLSGGEKQR 758
Cdd:PRK13634 83 --LRKKVGIVFQfpEHQLFEETVEKDICFG-PMnfgVSEEDAKQKAREM------IELVGLPEELLArSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 759 LTIARALLADTPILILDEATAFADPESEYLVQQALGRL--IDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGT---- 831
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTprei 233
|
250
....*....|.
gi 491227761 832 --HTDLLANNG 840
Cdd:PRK13634 234 faDPDELEAIG 244
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
629-838 |
2.90e-22 |
|
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: 96.46 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElYAKVGF--------VFQDVql 700
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgylpqeasIFRKL-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 701 vagTVRENIALACPEATDDDVESAAR-DAQIHE-RI--LRLPNGYdtvldtdtQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:cd03218 91 ---TVEENILAVLEIRGLSKKEREEKlEELLEEfHIthLRKSKAS--------SLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 777 ATAFADPESEYLVQQALGRLID-NRTVLVIAHRLH-TIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
620-826 |
3.09e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.08 E-value: 3.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGyrPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVF 695
Cdd:COG1101 9 KTFN--PGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQlvAGT-----VRENIALAcpeatdddvE------------SAARDAQIHERILRLPNGYDTVLDTDT-QLSGGEKQ 757
Cdd:COG1101 87 QDPM--MGTapsmtIEENLALA---------YrrgkrrglrrglTKKRRELFRELLATLGLGLENRLDTKVgLLSGGQRQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 758 RLTIARALLADTPILILDEATAFADPESEYLVQQALGRLI--DNRTVLVIAHRL-HTIADADQIVVLDHGRV 826
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVeeNNLTTLMVTHNMeQALDYGNRLIMMHEGRI 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
615-831 |
3.60e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 99.25 E-value: 3.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYakVGFV 694
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH--VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALA-----CPEA-TDDDVESAARDAQIHERILRLPngydtvldtdTQLSGGEKQRLTIARALLA 767
Cdd:PRK09452 92 FQSYALFPHmTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKP----------HQLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 768 DTPILILDEATAFADPESEYLVQQALGRLidNRT-----VLVIAHRLHTIADADQIVVLDHGRVAETGT 831
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELKAL--QRKlgitfVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
620-838 |
4.05e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.52 E-value: 4.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVE-----RGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:PRK14247 11 VSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALA--------CPEATDDDVESAARDAQIHERI---LRLPNGydtvldtdtQLSGGEKQRLTIA 762
Cdd:PRK14247 88 FQIPNPIPNlSIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEVkdrLDAPAG---------KLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 763 RALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
597-838 |
5.60e-22 |
|
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: 100.91 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 597 ETELDVIEAPVTADAVASVSFEGVTFGYRPG--------VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVE 668
Cdd:COG4172 260 EPRGDPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 669 rGAIRIDGTDIRTLTPDE---LYAKVGFVFQDV-------QLVAGTVRENIALACPEATDddvesAARDAQIhERILRlp 738
Cdd:COG4172 340 -GEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPfgslsprMTVGQIIAEGLRVHGPGLSA-----AERRARV-AEALE-- 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 739 ngyDTVLDTDT------QLSGGEKQRLTIARALLADTPILILDEATAFADpeseYLVQ-QALGRLID-----NRTVLVIA 806
Cdd:COG4172 411 ---EVGLDPAArhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDLLRDlqrehGLAYLFIS 483
|
250 260 270
....*....|....*....|....*....|...
gi 491227761 807 HRLHTI-ADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG4172 484 HDLAVVrALAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
614-826 |
6.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 6.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRPGVPV----IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPD---- 685
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 686 ELYAKVGFVFQ--DVQLVAGTVRENIALAcPE---ATDDDVESAARdaqihERILRLPNGYDTVLDTDTQLSGGEKQRLT 760
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFG-PKnfgFSEDEAKEKAL-----KWLKKVGLSEDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 761 IArALLADTP-ILILDEATAFADPESE------YLVQQALGrlidnRTVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:PRK13641 156 IA-GVMAYEPeILCLDEPAAGLDPEGRkemmqlFKDYQKAG-----HTVILVTHNMDDVAEyADDVLVLEHGKL 223
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
627-831 |
6.07e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.90 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARF--HDVERGAIRIDGTDIRTLTPDElYAKVG-FV-FQDVQLVA 702
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDE-RARAGiFLaFQYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 G-TVRENIALACPEATDDDVESAARDAQIHE--RILRLPNGYdtvLDTD--TQLSGGEKQRLTIARALLADTPILILDEA 777
Cdd:COG0396 91 GvSVSNFLRTALNARRGEELSAREFLKLLKEkmKELGLDEDF---LDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDET 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 778 TAFADPESEYLVQQALGRLID-NRTVLVIAH--RLHTIADADQIVVLDHGRVAETGT 831
Cdd:COG0396 168 DSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
631-809 |
9.57e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 9.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVE-----RGAIRIDGTDIRTLTPD--ELYAKVGFVFQDVQLVAG 703
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDtvDLRKEIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALAC-------PEATDDDVESAARDAQIHERIlrlpngYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:PRK14239 101 SIYENVVYGLrlkgikdKQVLDEAVEKSLKGASIWDEV------KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190
....*....|....*....|....*....|...
gi 491227761 777 ATAFADPESEYLVQQALGRLIDNRTVLVIAHRL 809
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
631-830 |
1.10e-21 |
|
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: 94.84 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELyakvgFVFQDVQLVAG-TVRENI 709
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 710 ALACPEATDDDVESAARdaQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLV 789
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERR--AIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491227761 790 QQALGRLI-DNR-TVLVIAHRL-HTIADADQIVVLDHGRVAETG 830
Cdd:TIGR01184 154 QEELMQIWeEHRvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
633-859 |
1.20e-21 |
|
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: 97.49 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRT------LTPDElyAKVGFVFQDVQL-----V 701
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEK--RRIGYVFQEARLfphlsV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 702 AGTVRENIALACPEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATAFA 781
Cdd:TIGR02142 93 RGNLRYGMKRARPSERRISFERVIELLGIGHLLGRLPG----------RLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 782 DPESEYLVQQALGRLID--NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLANNGryrrLWEGHRHEQSSVLA 858
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD----LPWLAREDQGSLIE 238
|
.
gi 491227761 859 G 859
Cdd:TIGR02142 239 G 239
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
630-826 |
1.39e-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: 92.88 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE-LYAKVGFVFQDVQ---LVAG-T 704
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVLDlS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 705 VRENIALACpeatdddvesaardaqiherilrlpngydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADPE 784
Cdd:cd03215 95 VAENIALSS------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491227761 785 SEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:cd03215 139 AKAEIYRLIRELADaGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
613-776 |
2.63e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.54 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGvtfgYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTltPDelyAKVG 692
Cdd:COG4525 9 VSVRYPG----GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PG---ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAG-TVRENIALACPEAtddDVESAARDaQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPI 771
Cdd:COG4525 80 VVFQKDALLPWlNVLDNVAFGLRLR---GVPKAERR-ARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
....*
gi 491227761 772 LILDE 776
Cdd:COG4525 156 LLMDE 160
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
629-831 |
2.86e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.77 E-value: 2.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDirtlTPDE-----LYAKVGFVFQ--DVQLV 701
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD----TSDEenlwdIRNKAGMVFQnpDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 702 AGTVRENIALAcPEATDDDVEsaardaQIHERI---LRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:PRK13633 100 ATIVEEDVAFG-PENLGIPPE------EIRERVdesLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 779 AFADPESEYLVQQALGRL--IDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGT 831
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
630-830 |
2.91e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.49 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLA---RFHDVERGAIRIDGtdiRTLTPDELYAKVGFVFQDVQLVAG-TV 705
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIA----LACPEATDDDVeSAARDAQIHERILRLPNGYDTVLdtdTQLSGGEKQRLTIARALLADTPILILDEATAFA 781
Cdd:cd03234 99 RETLTytaiLRLPRKSSDAI-RKKRVEDVLLRDLALTRIGGNLV---KGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491227761 782 DPESEYLVQQALGRLI-DNRTVLVIAHRLHtiADA----DQIVVLDHGRVAETG 830
Cdd:cd03234 175 DSFTALNLVSTLSQLArRNRIVILTIHQPR--SDLfrlfDRILLLSSGEIVYSG 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
627-854 |
3.58e-21 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 99.98 E-value: 3.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVErGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVR 706
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFR 1309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIAlacPEA--TDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADP 783
Cdd:TIGR01271 1310 KNLD---PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLvDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 784 ESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYR---------RLWEGHRHEQS 854
Cdd:TIGR01271 1387 VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKqamsaadrlKLFPLHRRNSS 1466
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
619-836 |
3.78e-21 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 94.10 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 619 GVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KVGFVF 695
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVAG---TVRENIALacPEATDDDVESAARDAQIHErILRLPNGYDTVLDT-DTQLSGGEKQRLTIARALLADTPI 771
Cdd:TIGR02769 95 QDSPSAVNprmTVRQIIGE--PLRHLTSLDESEQKARIAE-LLDMVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 772 LILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLL 836
Cdd:TIGR02769 172 IVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
627-838 |
3.89e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.66 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP--------DELYAKVGFVFQDV 698
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 699 QLVAG-TVRENIaLACPEAtdddVESAARDAQIHE-RILRLPNGYDTVLDT-DTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:PRK11264 95 NLFPHrTVLENI-IEGPVI----VKGEPKEEATARaRELLAKVGLAGKETSyPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 776 EATAFADPEseyLVQQALGRLI----DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK11264 170 EPTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
628-850 |
3.90e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 93.61 E-value: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKS-TLASLLARF-HDVER--GAIRIDGTDIrtlTPDELYAK-VGFVFQD----- 697
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpAGVRQtaGRVLLDGKPV---APCALRGRkIATIMQNprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 --VQLVAGTVRENIaLACPEATDDDVESAARDAQIHERILRLPNGYdtvldtDTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:PRK10418 93 npLHTMHTHARETC-LALGKPADDATLTAALEAVGLENAARVLKLY------PFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 776 EATAFADPESEYLVQQALGRLIDNRT--VLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLANNGR--YRRLWEGHR 850
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKHavTRSLVSAHL 245
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
623-821 |
4.53e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 623 GYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDI------RTLTPDELYAKVgfvfq 696
Cdd:NF040873 1 GY-GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqRSEVPDSLPLTV----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 dVQLVA-GTVRENIALACPEATDDDVESAARDAQIHERILRLPngydtvLDTdtqLSGGEKQRLTIARALLADTPILILD 775
Cdd:NF040873 75 -RDLVAmGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQ------LGE---LSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491227761 776 EATAFADPESEYLVQQALGRLI-DNRTVLVIAHRLHTIADADQIVVL 821
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
621-830 |
7.19e-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: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 621 TFGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLArfhdverGAIRIDGTDIRTLTPD-----ELYAKVGfVF 695
Cdd:cd03268 9 TYG---KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL-------GLIKPDSGEITFDGKSyqkniEALRRIG-AL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVAG--TVRENIALACPEATDDDvesaardaQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03268 78 IEAPGFYPnlTARENLRLLARLLGIRK--------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
618-830 |
7.87e-21 |
|
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: 92.05 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYRPGVPVIH---DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTlTPDELYAKVGFV 694
Cdd:cd03266 5 DALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG-TVRENIALAcpeATDDDVESAARDAQIHERILRLpnGYDTVLDTDTQ-LSGGEKQRLTIARALLADTPIL 772
Cdd:cd03266 84 SDSTGLYDRlTARENLEYF---AGLYGLKGDELTARLEELADRL--GMEELLDRRVGgFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
628-825 |
8.34e-21 |
|
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: 92.11 E-value: 8.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRID----GTDIRTLTPDELYA----KVGFVFQ--- 696
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREILAlrrrTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 ------DVQLVAGTVRENialacpEATDDDVESAARDA----QIHERILRLPngydtvldtDTQLSGGEKQRLTIARALL 766
Cdd:COG4778 104 viprvsALDVVAEPLLER------GVDREEARARARELlarlNLPERLWDLP---------PATFSGGEQQRVNIARGFI 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 767 ADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLV-IAHRLHTI-ADADQIVVLDHGR 825
Cdd:COG4778 169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReAVADRVVDVTPFS 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
622-837 |
9.37e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.83 E-value: 9.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 622 FGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KVGFVFQDv 698
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrDIQMVFQD- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 699 QLVA----GTVRENIALACPEATDDDveSAARDAQIHErILRLPNGYDTVLDT-DTQLSGGEKQRLTIARALLADTPILI 773
Cdd:PRK10419 98 SISAvnprKTVREIIREPLRHLLSLD--KAERLARASE-MLRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 774 LDEATAFADpeseyLVQQA-----LGRLIDNRTV--LVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PRK10419 175 LDEAVSNLD-----LVLQAgvirlLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
633-838 |
1.16e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.03 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KVGFVFQDVQlvaG------ 703
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPY---Aslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIAlacpEATD--DDVESAARDAQIHErILRLpngydtV-LDTDT------QLSGGEKQRLTIARALLADTPILIL 774
Cdd:COG4608 113 TVGDIIA----EPLRihGLASKAERRERVAE-LLEL------VgLRPEHadryphEFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 775 DEATAFADpeseYLVQ-QALGRLID-----NRTVLVIAHRL----HTiadADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG4608 182 DEPVSALD----VSIQaQVLNLLEDlqdelGLTYLFISHDLsvvrHI---SDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
613-826 |
1.38e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.10 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRPG---VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA 689
Cdd:PRK10535 3 ALLELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 ----KVGFVFQDVQLVAG-TVRENIALACPEAtddDVESAARDAQIHERILRLPNGyDTVLDTDTQLSGGEKQRLTIARA 764
Cdd:PRK10535 83 lrreHFGFIFQRYHLLSHlTAAQNVEVPAVYA---GLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIADADQIVVLDHGRV 826
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
614-838 |
1.63e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 96.29 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTfgyrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLA----SLLARFHDVERGAIRIDGTDIRTLTPDELYA 689
Cdd:COG4172 13 SVAFGQGG----GTVEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 ----KVGFVFQD-------VQLVAGTVRENIALacpeatdddvESAARDAQIHERIL------RLPNGYDTVLDTDTQLS 752
Cdd:COG4172 89 irgnRIAMIFQEpmtslnpLHTIGKQIAEVLRL----------HRGLSGAAARARALellervGIPDPERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 753 GGEKQRLTIARALLADTPILILDEATAFADPeseyLVQ-QALGRLID-----NRTVLVIAHRLHTIAD-ADQIVVLDHGR 825
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDLLKDlqrelGMALLLITHDLGVVRRfADRVAVMRQGE 234
|
250
....*....|...
gi 491227761 826 VAETGTHTDLLAN 838
Cdd:COG4172 235 IVEQGPTAELFAA 247
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
630-831 |
1.66e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVGFVFQDVQLVAG-TVREN 708
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 709 IALACPEATDDDVESAARDAQIHERIL------RLPNGYdtvldtDTQLSGGEKQRLTIARALLADTPILILDEATAFAD 782
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAIKAKVTQLLemvqlaHLADRY------PAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 783 PEseylVQQALGRLIDN-------RTVLVIAHRLHTIADADQIVVLDHGRVAETGT 831
Cdd:PRK10851 169 AQ----VRKELRRWLRQlheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
614-836 |
1.78e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGF 693
Cdd:PRK09536 5 DVSDLSVEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VFQDVQLVAG-TVRENIALA-CPEATDDDVESAARDAQIHERILRlpNGYDTVLDTD-TQLSGGEKQRLTIARALLADTP 770
Cdd:PRK09536 82 VPQDTSLSFEfDVRQVVEMGrTPHRSRFDTWTETDRAAVERAMER--TGVAQFADRPvTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 771 ILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLL 836
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
615-836 |
1.79e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIdGTDIRTLTPDE---- 686
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQkeik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 687 -LYAKVGFVFQ--DVQLVAGTVRENIALAcPEATDDDVESAARDAQIHERILRLPNGYDTvlDTDTQLSGGEKQRLTIAR 763
Cdd:PRK13643 81 pVRKKVGVVFQfpESQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAEKLEMVGLADEFWE--KSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLL 836
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
602-831 |
2.18e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.99 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 602 VIEAPVTADAVASVSFEGVTFGYRPG--VPVIHDVSLTLRHGTVTALVGPSGSGKSTLAS-----LLARFHDVERGAIRI 674
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVFDEKQEneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 675 dGTDIRTLTPD------------ELYAKVGFVFQ--DVQLVAGTVRENIALAcPEATDDDVESAARDAQIHERILRLpnG 740
Cdd:PRK13631 91 -GDKKNNHELItnpyskkiknfkELRRRVSMVFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYLNKMGL--D 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 741 YDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEY-LVQQALGRLIDNRTVLVIAHRL-HTIADADQI 818
Cdd:PRK13631 167 DSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMeHVLEVADEV 246
|
250
....*....|...
gi 491227761 819 VVLDHGRVAETGT 831
Cdd:PRK13631 247 IVMDKGKILKTGT 259
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
627-830 |
3.17e-20 |
|
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: 89.51 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHD--VERGAIRIDGTDIRTLTPDElYAKVG-FV-FQDVQLVA 702
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEE-RARLGiFLaFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 G-TVREnialacpeatdddvesaardaqiherILRlpngydtvlDTDTQLSGGEKQRLTIARALLADTPILILDEATAFA 781
Cdd:cd03217 91 GvKNAD--------------------------FLR---------YVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 782 DPESEYLVQQALGRLID-NRTVLVIAHRLHtIAD---ADQIVVLDHGRVAETG 830
Cdd:cd03217 136 DIDALRLVAEVINKLREeGKSVLIITHYQR-LLDyikPDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
618-839 |
3.21e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYRPGVPV--IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVF 695
Cdd:PRK13642 8 ENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 Q--DVQLVAGTVRENIALACPEATDDDVESAARdaqIHERILRLpNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILI 773
Cdd:PRK13642 88 QnpDNQFVGATVEDDVAFGMENQGIPREEMIKR---VDEALLAV-NMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 774 LDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANN 839
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
633-835 |
3.29e-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: 90.12 E-value: 3.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTlTPDELYAKVGFVFQDVQLVAG-TVRENIAL 711
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 712 acpEATDDDVESAARDaqihERILRLPNGYDTVLDTDTQL---SGGEKQRLTIARALLADTPILILDEATAFADPESEYL 788
Cdd:cd03265 97 ---HARLYGVPGAERR----ERIDELLDFVGLLEAADRLVktySGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491227761 789 VQQALGRLID--NRTVLVIAHRLHTiAD--ADQIVVLDHGRVAETGTHTDL 835
Cdd:cd03265 170 VWEYIEKLKEefGMTILLTTHYMEE-AEqlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
625-776 |
4.61e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 89.46 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVE---RGAIRIDGTDIRTLTPDElyAKVGFVFQDVQLV 701
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQ--RRIGILFQDDLLF 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 702 AG-TVRENIALACPEAtdddVESAARDAQIHERILRLpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:COG4136 89 PHlSVGENLAFALPPT----IGRAQRRARVEQALEEA--GLAGFADRDpATLSGGQRARVALLRALLAEPRALLLDE 159
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
587-842 |
5.22e-20 |
|
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: 96.17 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 587 SARHIAVALDETELD---VIEAPVTADAVASVSFEGVTFGYRPGVP-VIHDVSLTLRHGTVTALVGPSGSGKSTLAS-LL 661
Cdd:TIGR00957 606 SLKRLRIFLSHEELEpdsIERRTIKPGEGNSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLL 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 662 ARFHDVErGAIRIDGTdirtltpdelyakVGFVFQDVQLVAGTVRENIALAC---PEATDDDVESAA--RDAQIherilr 736
Cdd:TIGR00957 686 AEMDKVE-GHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKalnEKYYQQVLEACAllPDLEI------ 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 737 LPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPE-SEYLVQQALGR--LIDNRTVLVIAHRLHTI 812
Cdd:TIGR00957 746 LPSGDRTEIgEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPegVLKNKTRILVTHGISYL 825
|
250 260 270
....*....|....*....|....*....|
gi 491227761 813 ADADQIVVLDHGRVAETGTHTDLLANNGRY 842
Cdd:TIGR00957 826 PQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
630-852 |
5.96e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.29 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVE-----RGAIRIDGTDIRT--LTPDELYAKVGFVFQDVQLVA 702
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 G-TVRENIALACP--------EATDDDVESAARDAQIHERIlrlpngYDTVLDTDTQLSGGEKQRLTIARALLADTPILI 773
Cdd:PRK14267 99 HlTIYDNVAIGVKlnglvkskKELDERVEWALKKAALWDEV------KDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 774 LDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETgthtdllannGRYRRLWEGHRHE 852
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEV----------GPTRKVFENPEHE 242
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
630-838 |
7.37e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGT------DIRTLTPDELYAKVGFVFQDVQLVAG 703
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 -TVRENIALACpeaTDDDVESAARDAQIHERILR----LPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:PRK14246 105 lSIYDNIAYPL---KSHGIKEKREIKKIVEECLRkvglWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 779 AFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
631-848 |
7.65e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.79 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDEL----YAKVGFVFQDVQLVAG-TV 705
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIALACPEA--TDDDVESAARDAQIHERILRLPNGYdtvldtDTQLSGGEKQRLTIARALLADTPILILDEATAFADP 783
Cdd:PRK10070 124 LDNTAFGMELAgiNAEERREKALDALRQVGLENYAHSY------PDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 784 ESEYLVQQALGRL--IDNRTVLVIAHRL-HTIADADQIVVLDHGRVAETGTHTDLLAN--NGRYRRLWEG 848
Cdd:PRK10070 198 LIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpaNDYVRTFFRG 267
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
627-844 |
9.72e-20 |
|
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: 90.30 E-value: 9.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVErGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTVR 706
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIAlacPEA--TDDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADP 783
Cdd:cd03289 95 KNLD---PYGkwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLvDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 784 ESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRR 844
Cdd:cd03289 172 ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
611-835 |
1.46e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 611 AVASVSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIR-TLTPDELYA 689
Cdd:PRK11288 1 SSPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 KVGFVFQDVQLVAG-TVRENIALACPEATDDDVESAARDAQIHERILRLpnGYDtvLDTDTQ---LSGGEKQRLTIARAL 765
Cdd:PRK11288 80 GVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVD--IDPDTPlkyLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 766 LADTPILILDEAT-AFADPESEYLVqqalgRLI-----DNRTVLVIAHRLHTI-ADADQIVVLDHGRVAEtgTHTDL 835
Cdd:PRK11288 156 ARNARVIAFDEPTsSLSAREIEQLF-----RVIrelraEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
630-824 |
1.69e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.33 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVErGAIRIDG------TDI--RTLTPDELYAKVGFVFQDVQLV 701
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnQNIyeRRVNLNRLRRQVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 702 AGTVRENIALAC------PEAT-DDDVESAARDAQIHERIlrlpngYDTVLDTDTQLSGGEKQRLTIARALLADTPILIL 774
Cdd:PRK14258 101 PMSVYDNVAYGVkivgwrPKLEiDDIVESALKDADLWDEI------KHKIHKSALDLSGGQQQRLCIARALAVKPKVLLM 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491227761 775 DEATAFADPES----EYLVQQAlgRLIDNRTVLVIAHRLHTIADADQIVVLDHG 824
Cdd:PRK14258 175 DEPCFGLDPIAsmkvESLIQSL--RLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
625-831 |
2.33e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.19 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLA--RFHDVER-GAIRIDGTDIrtlTPDELYAKVGFVFQDVQLV 701
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrSPKGVKGsGSVLLNGMPI---DAKEMRAISAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 702 AG-TVRENIALACPEATDDDVESAARDAQIHERI--LRLPNGYDTVLDTDTQ---LSGGEKQRLTIARALLADTPILILD 775
Cdd:TIGR00955 112 PTlTVREHLMFQAHLRMPRRVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 776 EATAFADPESEYLVQQALGRLIDN-RTVLVIAHR--LHTIADADQIVVLDHGRVAETGT 831
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQpsSELFELFDKIILMAEGRVAYLGS 250
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
596-832 |
4.00e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.50 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 596 DETELDVIEAPVTADAVASVSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRID 675
Cdd:PRK13536 23 HQGISEAKASIPGSMSTVAIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 676 GTDIrtltPDELY---AKVGFVFQ-DVQLVAGTVRENIALACPEATDDDVESAARDAQIHErILRLPNGYDTVLdtdTQL 751
Cdd:PRK13536 102 GVPV----PARARlarARIGVVPQfDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLE-FARLESKADARV---SDL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 752 SGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLI-DNRTVLVIAHRLHTiAD--ADQIVVLDHGR-VA 827
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEE-AErlCDRLCVLEAGRkIA 252
|
....*
gi 491227761 828 ETGTH 832
Cdd:PRK13536 253 EGRPH 257
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
614-833 |
4.60e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYrpGV-PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGT--DIRTlTPDE---- 686
Cdd:PRK11124 2 SIQLNGINCFY--GAhQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSK-TPSDkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 687 -LYAKVGFVFQDVQLVAG-TVRENIALA-CPEATDDDVESAARDAQIHERiLRLPNGYDTVldtDTQLSGGEKQRLTIAR 763
Cdd:PRK11124 79 eLRRNVGMVFQQYNLWPHlTVQQNLIEApCRVLGLSKDQALARAEKLLER-LRLKPYADRF---PLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQALGRLIDNR-TVLVIAHRLHtIAD--ADQIVVLDHGRVAETGTHT 833
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVE-VARktASRVVYMENGHIVEQGDAS 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
631-852 |
5.20e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAiRIDGTDI--------RTLTPDELYAKVGFVFQDVQLVA 702
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGKVTfhgknlyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 GTVRENIALAcPEAT------DDDVESAARDAQIHERIlrlpngYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:PRK14243 105 KSIYDNIAYG-ARINgykgdmDELVERSLRQAALWDEV------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 777 ATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGthtdllannGRYRRLWEGHRHE 852
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGG---------GRYGYLVEFDRTE 244
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
613-830 |
5.46e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 89.70 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVG 692
Cdd:PRK11000 2 ASVTLRNVTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAG-TVRENIALACPEATDDDVESAARDAQIHErILRLpngyDTVLDTDTQ-LSGGEKQRLTIARALLADTP 770
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKEEINQRVNQVAE-VLQL----AHLLDRKPKaLSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 771 ILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAH-RLHTIADADQIVVLDHGRVAETG 830
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
622-837 |
8.38e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.15 E-value: 8.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 622 FGYRPGVpVIHDVSLTLRHGTVTALVGPSGSGKST-LASLLARFhDVERGairidgtdirtltpdELYAK--VGFVFQDV 698
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTlLQSLLSQF-EISEG---------------RVWAErsIAYVPQQA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 699 QLVAGTVRENIALACPEATdDDVESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEA 777
Cdd:PTZ00243 731 WIMNATVRGNILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIgEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 778 TAFADPE-SEYLVQQA-LGRLIDNRTVLViAHRLHTIADADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PTZ00243 810 LSALDAHvGERVVEECfLGALAGKTRVLA-THQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
614-833 |
9.83e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 86.22 E-value: 9.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDG------TDIRTLTPDEL 687
Cdd:COG4161 2 SIQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 688 YAKVGFVFQDVQLVAG-TVRENIaLACPEATDDDVESAARD-AQIHERILRLPNGYDTVldtDTQLSGGEKQRLTIARAL 765
Cdd:COG4161 81 RQKVGMVFQQYNLWPHlTVMENL-IEAPCKVLGLSKEQAREkAMKLLARLRLTDKADRF---PLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 766 LADTPILILDEATAFADPESEYLVQQALGRLIDNR-TVLVIAHRLHtIAD--ADQIVVLDHGRVAETGTHT 833
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVE-FARkvASQVVYMEKGRIIEQGDAS 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
617-826 |
6.56e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.81 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 617 FEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTdirtltpdelyAKVGFVFQ 696
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 DVQLVAG-TVRENIALACPE-------------ATDDDVESAARDAQIHERILRLpNGYD------TVL--------DTD 748
Cdd:COG0488 69 EPPLDDDlTVLDTVLDGDAElraleaeleeleaKLAEPDEDLERLAELQEEFEAL-GGWEaearaeEILsglgfpeeDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 749 TQ---LSGGEKQRLTIARALLADTPILILDEATAFADPES-----EYLVQQalgrlidNRTVLVIAH-R--LHTIadADQ 817
Cdd:COG0488 148 RPvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY-------PGTVLVVSHdRyfLDRV--ATR 218
|
....*....
gi 491227761 818 IVVLDHGRV 826
Cdd:COG0488 219 ILELDRGKL 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
634-831 |
8.53e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 8.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 634 VSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVErGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAG-TVRENIALA 712
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAmPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 713 CPEATDDDvESAARDAQIHERiLRLPNGYDTVLdtdTQLSGGEKQRLTIARALL----ADTP---ILILDEATAFADpes 785
Cdd:COG4138 94 QPAGASSE-AVEQLLAQLAEA-LGLEDKLSRPL---TQLSGGEWQRVRLAAVLLqvwpTINPegqLLLLDEPMNSLD--- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 786 eyLVQQ-ALGRLIDN-----RTVLVIAHRL-HTIADADQIVVLDHGRVAETGT 831
Cdd:COG4138 166 --VAQQaALDRLLRElcqqgITVVMSSHDLnHTLRHADRVWLLKQGKLVASGE 216
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
622-824 |
1.01e-17 |
|
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: 82.76 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 622 FGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLasLLARFHDVER--GAIRIDGTDIRTLTPDELYAK----VGFVF 695
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSL--LLAILGEMQTleGKVHWSNKNESEPSFEATRSRnrysVAYAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVAGTVRENIALACPeaTDDDVESAARDA-QIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILI 773
Cdd:cd03290 86 QKPWLLNATVEENITFGSP--FNKQRYKAVTDAcSLQPDIDLLPFGDQTEIgERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491227761 774 LDEATAFADPE-SEYLVQQALGRLI--DNRTVLVIAHRLHTIADADQIVVLDHG 824
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
631-858 |
1.26e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.52 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARF---------------HDVERGAiRIDGtDIRtltpdELYAKVGFVF 695
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshiellgRTVQREG-RLAR-DIR-----KSRANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVAG-TVRENI---ALAC------------PEATDDDVESAARDAQIHERILRLpngydtvldtdTQLSGGEKQRL 759
Cdd:PRK09984 93 QQFNLVNRlSVLENVligALGStpfwrtcfswftREQKQRALQALTRVGMVHFAHQRV-----------STLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 760 TIARALLADTPILILDEATAFADPESEYLVQQALGRL--IDNRTVLVIAHRL-HTIADADQIVVLDHGRVAETGTHTDLl 836
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF- 240
|
250 260
....*....|....*....|...
gi 491227761 837 aNNGRYRRLWEG-HRHEQSSVLA 858
Cdd:PRK09984 241 -DNERFDHLYRSiNRVEENAKAA 262
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
327-838 |
2.34e-17 |
|
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: 86.39 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 327 QLLAGADEAQLRH-TGFVFLVLLVLGATLGMALTL-WL--HVVdlrfsADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQ 402
Cdd:COG4615 38 QALNATGAALARLlLLFAGLLVLLLLSRLASQLLLtRLgqHAV-----ARLRLRLSRRILAAPLERLERIGAARLLAALT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 403 DDTMSlhylIT---HSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMMAMMYQSGPKIVEASRWADRMSTE 479
Cdd:COG4615 113 EDVRT----ISqafVRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKH 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 480 STAYLEGQPVIRIfggaaaSSFKRRlddylRFLNDWQRPFIGRktFMDLVTRPTTFLWLIATAG--TLFVVSGAMqpVTL 557
Cdd:COG4615 189 FRALLEGFKELKL------NRRRRR-----AFFDEDLQPTAER--YRDLRIRADTIFALANNWGnlLFFALIGLI--LFL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 558 LPFLVLG-----TTFGARLLGIAYGLGSIRGGLE-------SARHIA---VALDETELDVIEAPVTADAVA--SVSFEGV 620
Cdd:COG4615 254 LPALGWAdpavlSGFVLVLLFLRGPLSQLVGALPtlsranvALRKIEeleLALAAAEPAAADAAAPPAPADfqTLELRGV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 621 TFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQ 696
Cdd:COG4615 334 TYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFS 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 DVQLvagtvrenialacpeaTDD--DVESAARDAQIHERILRLpnGYDTVLD------TDTQLSGGEKQRLTIARALLAD 768
Cdd:COG4615 414 DFHL----------------FDRllGLDGEADPARARELLERL--ELDHKVSvedgrfSTTDLSQGQRKRLALLVALLED 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 769 TPILILDEATAFADPE-SEYLVQQALGRL-IDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG4615 476 RPILVFDEWAADQDPEfRRVFYTELLPELkARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGPAALAAS 547
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
626-829 |
3.29e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 626 PGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdIRTLTPDelyAKVGFVFQDVQLVA-GT 704
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPG---AERGVVFQNEGLLPwRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 705 VRENIALACPEAtddDVESAARDAQIHERILRLP-NGYDTVLdtDTQLSGGEKQRLTIARALLADTPILILDEATAFADP 783
Cdd:PRK11248 87 VQDNVAFGLQLA---GVEKMQRLEIAHQMLKKVGlEGAEKRY--IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491227761 784 ESEYLVQQALGRLIDN--RTVLVIAHRL-HTIADADQIVVL--DHGRVAET 829
Cdd:PRK11248 162 FTREQMQTLLLKLWQEtgKQVLLITHDIeEAVFMATELVLLspGPGRVVER 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
627-776 |
4.66e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 84.12 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPdelYAK-VGFVFQDVQLVAG-T 704
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP---YQRpINMMFQSYALFPHmT 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 705 VRENIALACPEatdDDVESAARDAQIHErILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:PRK11607 108 VEQNIAFGLKQ---DKLPKAEIASRVNE-MLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
620-831 |
5.56e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQ--D 697
Cdd:PRK13652 9 LCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQLVAGTVRENIALAC------PEATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPI 771
Cdd:PRK13652 89 DQIFSPTVEQDIAFGPinlgldEETVAHRVSSALHMLGLEELRDRVPH----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 772 LILDEATAFADPESEYLVQQALGRLIDN--RTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGT 831
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
637-831 |
7.05e-17 |
|
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: 84.84 E-value: 7.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 637 TLRHGTVTALVGPSGSGKSTLASLLArfhdverGAiridgtdirtLTPDElyakvGFVFQDV------QLVA----GTVR 706
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILA-------GV----------LKPDE-----GEVDEDLkisykpQYISpdydGTVE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIALACPeatdDDVESAARDAQIHERiLRLPNGYDTVLDTdtqLSGGEKQRLTIARALLADTPILILDEATAFADPESE 786
Cdd:COG1245 420 EFLRSANT----DDFGSSYYKTEIIKP-LGLEKLLDKNVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 491227761 787 YLVQQALGRLIDNR--TVLVIAHRLHTIaD--ADQIVVLDhGRVAETGT 831
Cdd:COG1245 492 LAVAKAIRRFAENRgkTAMVVDHDIYLI-DyiSDRLMVFE-GEPGVHGH 538
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
610-838 |
7.17e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 81.98 E-value: 7.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 610 DAVASVSFEGVTFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDI-----R 680
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 681 TLTPDELYAKVGFVFQ--DVQLVAGTVRENIALAcPEATDDDVESAARDAQIHERILRLPNGYdtVLDTDTQLSGGEKQR 758
Cdd:PRK13645 82 IKEVKRLRKEIGLVFQfpEYQLFQETIEKDIAFG-PVNLGENKQEAYKKVPELLKLVQLPEDY--VKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 759 LTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDN--RTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDL 835
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
...
gi 491227761 836 LAN 838
Cdd:PRK13645 239 FSN 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
637-822 |
8.98e-17 |
|
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: 80.92 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 637 TLRHGTVTALVGPSGSGKSTLASLLArfhdverGAIRIDGTDIRTLTPDELYaKVGFVFQDVQlvaGTVRENIAlacpEA 716
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLA-------GVLKPDEGDIEIELDTVSY-KPQYIKADYE---GTVRDLLS----SI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 717 TDDdvesAARDAQIHERILRlPNGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGR 795
Cdd:cd03237 86 TKD----FYTHPYFKTEIAK-PLQIEQILDREvPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|.
gi 491227761 796 LIDN--RTVLVIAHRLHtIAD--ADQIVVLD 822
Cdd:cd03237 161 FAENneKTAFVVEHDII-MIDylADRLIVFE 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
627-835 |
1.10e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.95 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYaKVG--FVFQDVQLVAG- 703
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH-QLGiyLVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALACPEATDDDVESAARDAQIherilrlpngyDTVLDTDTQ---LSGGEKQRLTIARALLADTPILILDEATAF 780
Cdd:PRK15439 102 SVKENILFGLPKRQASMQKMKQLLAAL-----------GCQLDLDSSagsLEVADRQIVEILRGLMRDSRILILDEPTAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 781 ADP-ESEYLVQQALGRLIDNRTVLVIAHRLHTI-ADADQIVVLDHGRVAETGTHTDL 835
Cdd:PRK15439 171 LTPaETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
629-838 |
1.41e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.07 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIrtlTPDELY--AKVGF--------VFQDV 698
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI---THLPMHkrARLGIgylpqeasIFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 699 qlvagTVRENIaLACPEATDDDveSAARDAQIHE-----RILRLPN--GYdtvldtdtQLSGGEKQRLTIARALLADTPI 771
Cdd:COG1137 94 -----TVEDNI-LAVLELRKLS--KKEREERLEElleefGITHLRKskAY--------SLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 772 LILDEatAFA--DPES--------EYLVQQALGRLI-D-N-RTVLVIAHRLHtiadadqivVLDHGRVAETGTHTDLLAN 838
Cdd:COG1137 158 ILLDE--PFAgvDPIAvadiqkiiRHLKERGIGVLItDhNvRETLGICDRAY---------IISEGKVLAEGTPEEILNN 226
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
627-830 |
1.44e-16 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 80.00 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVE--RGAIRIDGTDIRTLTPDELyAKVG-FV-FQDVQLVA 702
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtSGTILFKGQDLLELEPDER-ARAGlFLaFQYPEEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 G-TVRENIALACPEATDDDVESAARDAQIHERI------LRLPNGYDTvLDTDTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:TIGR01978 91 GvSNLEFLRSALNARRSARGEEPLDLLDFEKLLkeklalLDMDEEFLN-RSVNEGFSGGEKKRNEILQMALLEPKLAILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 776 EATAFADPESEYLVQQALGRLID-NRTVLVIAH--RLHTIADADQIVVLDHGRVAETG 830
Cdd:TIGR01978 170 EIDSGLDIDALKIVAEGINRLREpDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
615-826 |
1.73e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.53 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE---LYAKV 691
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAG-TVRENIA--LACPEATDDDVE---SAARDaqiheRILRLpngyDTVLDTDTQLSGGEKQRLTIARAL 765
Cdd:PRK10908 82 GMIFQDHHLLMDrTVYDNVAipLIIAGASGDDIRrrvSAALD-----KVGLL----DKAKNFPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 766 LADTPILILDEATAFADPEseylVQQALGRLID--NR---TVLVIAHRLHTIADAD-QIVVLDHGRV 826
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDA----LSEGILRLFEefNRvgvTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
627-859 |
2.09e-16 |
|
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: 80.67 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdirtltpdelyaKVGFVFQDVQLVAGTVR 706
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIALAcpeATDDD--VESAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADP 783
Cdd:cd03291 116 ENIIFG---VSYDEyrYKSVVKACQLEEDITKFPEKDNTVLgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 784 ESEYLV-QQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLlanngryrrlwEGHRHEQSSVLAG 859
Cdd:cd03291 193 FTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL-----------QSLRPDFSSKLMG 258
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
627-835 |
2.29e-16 |
|
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: 84.19 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdirtltpdelyaKVGFVFQDVQLVAGTVR 706
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIALAcpeATDDDVE--SAARDAQIHERILRLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDEATAFADP 783
Cdd:TIGR01271 505 DNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 784 ESEY-LVQQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDL 835
Cdd:TIGR01271 582 VTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
623-830 |
2.95e-16 |
|
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: 78.73 E-value: 2.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 623 GYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTdIRTLtpdeLYAKVGFvfqDVQLva 702
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSL----LGLGGGF---NPEL-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 gTVRENIALACpeatdddVESAARDAQIHERILR------LPNGYDTVLDTdtqLSGGEKQRLTIARALLADTPILILDE 776
Cdd:cd03220 100 -TGRENIYLNG-------RLLGLSRKEIDEKIDEiiefseLGDFIDLPVKT---YSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 777 ATAFADpesEYLVQQALGRLI----DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:cd03220 169 VLAVGD---AAFQEKCQRRLRellkQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
303-847 |
5.53e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 83.10 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 303 GGVLQAIITMVELAPFVVLVELTRQLLAGaDEAQLrhtGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLDKLS 382
Cdd:PLN03232 306 GGIFKIGHDLSQFVGPVILSHLLQSMQEG-DPAWV---GYVYAFLIFFGVTFGVLCESQYFQNVGRVGFRLRSTLVAAIF 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 383 RVPLGwFTQRG-----SGSVKKLIQDDTMSLHYLITH-----SIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYL 452
Cdd:PLN03232 382 HKSLR-LTHEArknfaSGKVTNMITTDANALQQIAEQlhglwSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLI 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 453 LTMMAMMYQSGpkiveaSRWADRMSTESTAYLEGQPVIRIFggAAASSFKRRLDDYLRFLNDWQRPFIGRKTFMDLVTRP 532
Cdd:PLN03232 461 VRKMRKLTKEG------LQWTDKRVGIINEILASMDTVKCY--AWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNS 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 533 TTFLWLIATAGTLFVVSGAMQPVTLLPFLVLGTTFGARLLGIAYGLGSIRGGLESARHIAVALDETELDVIEAPVTADAV 612
Cdd:PLN03232 533 IPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGA 612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGY--RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLAS-LLARFHDVERGAIRIDGTdirtltpdelya 689
Cdd:PLN03232 613 PAISIKNGYFSWdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS------------ 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 kVGFVFQDVQLVAGTVRENIALAcpeatdDDVESA----ARDAQIHERILRLPNGYD--TVLDTDTQLSGGEKQRLTIAR 763
Cdd:PLN03232 681 -VAYVPQVSWIFNATVRENILFG------SDFESErywrAIDVTALQHDLDLLPGRDltEIGERGVNISGGQKQRVSMAR 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 764 ALLADTPILILDEATAFADPESEYLV-QQALGRLIDNRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRY 842
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLF 833
|
....*
gi 491227761 843 RRLWE 847
Cdd:PLN03232 834 KKLME 838
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
615-837 |
6.60e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.65 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIdGTDIrtltpdelyaKVGFV 694
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAG--TVRENIAlacpEATDDDVESAARD---------AQIHERIlrlpngydtvldtdTQLSGGEKQRLTIAR 763
Cdd:COG0488 384 DQHQEELDPdkTVLDELR----DGAPGGTEQEVRGylgrflfsgDDAFKPV--------------GVLSGGEKARLALAK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 764 ALLADTPILILDEATAFADPESEYLVQQAL----GrlidnrTVLVIAH-R--LHTIadADQIVVLDHGRVAE-TGTHTDL 835
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALddfpG------TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDDY 517
|
..
gi 491227761 836 LA 837
Cdd:COG0488 518 LE 519
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
622-838 |
6.95e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 78.97 E-value: 6.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 622 FGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPD--ELYAKVGFVFQ--D 697
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQLVAGTVRENIA-----LACPEatdDDVESAARDAqiheriLRLPN--GYDTvlDTDTQLSGGEKQRLTIARALLADTP 770
Cdd:PRK13639 89 DQLFAPTVEEDVAfgplnLGLSK---EEVEKRVKEA------LKAVGmeGFEN--KPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 771 ILILDEATAFADPESEYLVQQALGRLidNR---TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDL--NKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
300-561 |
7.21e-16 |
|
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: 79.13 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 300 MIAGGVLQAIITMVELAPFVVLVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLD 379
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 380 KLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMMAMm 459
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYF- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 460 yqsGPKIVEASR----WADRMSTESTAYLEGQPVIRIFGG--AAASSFKRRLDDYLR------FLNDWQRPFIGrkTFMD 527
Cdd:cd07346 160 ---RRRIRKASRevreSLAELSAFLQESLSGIRVVKAFAAeeREIERFREANRDLRDanlraaRLSALFSPLIG--LLTA 234
|
250 260 270
....*....|....*....|....*....|....
gi 491227761 528 LVTrpttflWLIATAGTLFVVSGAMQPVTLLPFL 561
Cdd:cd07346 235 LGT------ALVLLYGGYLVLQGSLTIGELVAFL 262
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
637-822 |
8.65e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 637 TLRHGTVTALVGPSGSGKSTLASLLArfhdverGAIridgtdirtlTPDElyakvGFVFQDVQL----------VAGTVR 706
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLA-------GVL----------KPDE-----GEVDPELKIsykpqyikpdYDGTVE 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIalacpEATDDDVESAARDAQIHERiLRLPNGYDTVLDTdtqLSGGEKQRLTIARALLADTPILILDEATAFADPESE 786
Cdd:PRK13409 419 DLL-----RSITDDLGSSYYKSEIIKP-LQLERLLDKNVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491227761 787 YLVQQALGRLIDNR--TVLVIAHRLHTIaD--ADQIVVLD 822
Cdd:PRK13409 490 LAVAKAIRRIAEEReaTALVVDHDIYMI-DyiSDRLMVFE 528
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
624-797 |
1.01e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 624 YRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGfvFQDVQLVAG 703
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIAL--ACPEATDDDVESAARDAQIHeRILRLPNGYdtvldtdtqLSGGEKQRLTIARALLADTPILILDEATAFA 781
Cdd:PRK13539 89 TVAENLEFwaAFLGGEELDIAAALEAVGLA-PLAHLPFGY---------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|....*.
gi 491227761 782 DPESeylvQQALGRLI 797
Cdd:PRK13539 159 DAAA----VALFAELI 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
615-839 |
1.27e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.79 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV 694
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAgtvreniALACPEATdddvesAARDAQIHERILRLPNGYDTVLD----TDTQLSGGEKQRLTIARALLADTP 770
Cdd:PRK10522 403 FTDFHLFD-------QLLGPEGK------PANPALVEKWLERLKMAHKLELEdgriSNLKLSKGQKKRLALLLALAEERD 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 771 ILILDEATAFADPE-SEYLVQQALGRL-IDNRTVLVIAHRLHTIADADQIVVLDHGRVAE-TGTHTDLLANN 839
Cdd:PRK10522 470 ILLLDEWAADQDPHfRREFYQVLLPLLqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
633-859 |
2.06e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.76 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGT---DIRT---LTPDElyAKVGFVFQDVQL-----V 701
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEK--RRIGYVFQDARLfphykV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 702 AGTVRENIALACPEATDDDVESAArdaqIHERILRLPngydtvldtdTQLSGGEKQRLTIARALLADTPILILDEATAFA 781
Cdd:PRK11144 94 RGNLRYGMAKSMVAQFDKIVALLG----IEPLLDRYP----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 782 D-PESE----YLvqQALGRLIdNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLANNGryRRLWEGhRHEQSS 855
Cdd:PRK11144 160 DlPRKRellpYL--ERLAREI-NIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLEEVWASSA--MRPWLP-KEEQSS 233
|
....
gi 491227761 856 VLAG 859
Cdd:PRK11144 234 ILKV 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
622-831 |
2.22e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 622 FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLtPDELYAKVGFV--FQDVQ 699
Cdd:PRK11300 15 FG---GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVrtFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 700 LVAG-TVRENIALA---------------CPEATDDDVESAARDAQIHERI--LRLPNgydtvlDTDTQLSGGEKQRLTI 761
Cdd:PRK11300 91 LFREmTVIENLLVAqhqqlktglfsgllkTPAFRRAESEALDRAATWLERVglLEHAN------RQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 762 ARALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGT 831
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
628-831 |
3.27e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdiRTLTPDELYAkvGFvfqDVQLvagTVRE 707
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSALLELGA--GF---HPEL---TGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 708 NIALAC------PEATDDDVESAARDAQIHERIlrlpngydtvldtDTQL---SGGEKQRLTIARALLADTPILILDEAT 778
Cdd:COG1134 108 NIYLNGrllglsRKEIDEKFDEIVEFAELGDFI-------------DQPVktySSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 779 AFADpesEYLVQQALGRLID----NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGT 831
Cdd:COG1134 175 AVGD---AAFQKKCLARIRElresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
300-571 |
3.34e-15 |
|
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: 76.91 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 300 MIAGGVLQAIITMVELAPFVVLVELTRQLLAGADeAQLRHTGFVFLVLLVLGatLGMALTLWLH-----VVDLRFSADVR 374
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD-PETQALNVYSLALLLLG--LAQFILSFLQsyllnHTGERLSRRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 375 RRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLI--PILVYL 452
Cdd:pfam00664 78 RKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAvlPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 453 LTMMAMMYQSGpKIVEASRWADRMS--TEStayLEGQPVIRIFGG--AAASSFKRRLDDYLRF---LNDWQRPFIGRKTF 525
Cdd:pfam00664 158 SAVFAKILRKL-SRKEQKAVAKASSvaEES---LSGIRTVKAFGReeYELEKYDKALEEALKAgikKAVANGLSFGITQF 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 491227761 526 MdlvtrpTTFLWLIAT-AGTLFVVSGAMQPVTLLPFLVLGTTFGARL 571
Cdd:pfam00664 234 I------GYLSYALALwFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
619-823 |
3.34e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 619 GVTFGYRPgvpVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRidgtdirtlTPDELyaKVGFVFQDV 698
Cdd:PRK09544 11 SVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL--RIGYVPQKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 699 QLVAG---TVRENIALAcPEATDDDVESAARDAQIhERILRLPNgydtvldtdTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:PRK09544 77 YLDTTlplTVNRFLRLR-PGTKKEDILPALKRVQA-GHLIDAPM---------QKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 776 EATAFADPESeylvQQALGRLID------NRTVLVIAHRLHTI-ADADQIVVLDH 823
Cdd:PRK09544 146 EPTQGVDVNG----QVALYDLIDqlrrelDCAVLMVSHDLHLVmAKTDEVLCLNH 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
613-836 |
4.23e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.36 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVG 692
Cdd:PRK10575 10 TTFALRNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAG-TVRENIALA-CPEATDDDVESAARDAQIHERI--LRLPNGYDTVLDTdtqLSGGEKQRLTIARALLAD 768
Cdd:PRK10575 89 YLPQQLPAAEGmTVRELVAIGrYPWHGALGRFGAADREKVEEAIslVGLKPLAHRLVDS---LSGGERQRAWIAMLVAQD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 769 TPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAhRLHTIADA----DQIVVLDHGRVAETGTHTDLL 836
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
634-782 |
4.50e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.20 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 634 VSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPD---ELYAK-VGFVFQDVQLVAG-TVREN 708
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQSFMLIPTlNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 709 IALACPEATDDDVESAARDAQ------IHERILRLPngydtvldtdTQLSGGEKQRLTIARALLADTPILILDEATAFAD 782
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKAlleqlgLGKRLDHLP----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
615-823 |
5.94e-15 |
|
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: 73.34 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIdgtdirtLTPDELYakvgFV 694
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-------PEGEDLL----FL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAGTVREnialacpeatdddvesaardaqiherILRLPngydtvldTDTQLSGGEKQRLTIARALLADTPILIL 774
Cdd:cd03223 70 PQRPYLPLGTLRE--------------------------QLIYP--------WDDVLSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491227761 775 DEATAFADPESE-YLVQQALGRLIdnrTVLVIAHRLHTIADADQIVVLDH 823
Cdd:cd03223 116 DEATSALDEESEdRLYQLLKELGI---TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
615-825 |
6.77e-15 |
|
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: 72.48 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARfhdvergairidgtdirTLTPDElyakvGFV 694
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-----------------ELEPDE-----GIV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQLVAGTVrenialacpeatdddvesaardaqiherilrlpngydtvldtdTQLSGGEKQRLTIARALLADTPILIL 774
Cdd:cd03221 58 TWGSTVKIGYF-------------------------------------------EQLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491227761 775 DEATAFADPESEYLVQQALGRLidNRTVLVIAH-R--LHTIadADQIVVLDHGR 825
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
629-827 |
8.32e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 8.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE-LYAKVGFVFQDVQ---LVAG- 703
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDRKgegLVLDl 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALACPEAT------DDDVESAARDAQIHE-RIlRLPNGYDTVldtdTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:COG1129 346 SIRENITLASLDRLsrggllDRRRERALAEEYIKRlRI-KTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 777 ATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRVA 827
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRELAAEgKAVIVISSELPELLGlSDRILVMREGRIV 473
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
621-849 |
9.66e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 75.21 E-value: 9.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 621 TFGYRPG------VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGtdiRTLT-PDELY--AKV 691
Cdd:PRK15112 13 TFRYRTGwfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHfGDYSYrsQRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQlVAGTVRENIA--LACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADT 769
Cdd:PRK15112 90 RMIFQDPS-TSLNPRQRISqiLDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 770 PILILDEATAFADPESEYLVQQALGRLIDNRT---VLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLAN--NGRYRR 844
Cdd:PRK15112 169 KVIIADEALASLDMSMRSQLINLMLELQEKQGisyIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASplHELTKR 248
|
....*
gi 491227761 845 LWEGH 849
Cdd:PRK15112 249 LIAGH 253
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
615-835 |
1.17e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.52 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPdELYAK--VG 692
Cdd:PRK09700 6 ISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDH-KLAAQlgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAG-TVRENIALA-------CPEATDDDVESAARDAQIHERIlrlpnGYDTVLDTDT-QLSGGEKQRLTIAR 763
Cdd:PRK09700 84 IIYQELSVIDElTVLENLYIGrhltkkvCGVNIIDWREMRVRAAMMLLRV-----GLKVDLDEKVaNLSISHKQMLEIAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 764 ALLADTPILILDEAT-AFADPESEYL---VQQALGrliDNRTVLVIAHRLHTI-ADADQIVVLDHGRVAETGTHTDL 835
Cdd:PRK09700 159 TLMLDAKVIIMDEPTsSLTNKEVDYLfliMNQLRK---EGTAIVYISHKLAEIrRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
606-830 |
1.22e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.82 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 606 PVTADAVASVSFEG--VTFGYRPGV--------PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDvERGAIRID 675
Cdd:PRK15134 267 PLPEPASPLLDVEQlqVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 676 GTDIRTLTPDELYA---KVGFVFQD-----------VQLVAgtvrENIALACPEATdddveSAARDAQIHERILRLPNGY 741
Cdd:PRK15134 346 GQPLHNLNRRQLLPvrhRIQVVFQDpnsslnprlnvLQIIE----EGLRVHQPTLS-----AAQREQQVIAVMEEVGLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 742 DTVLDTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTV--LVIAHRLHTI-ADADQI 818
Cdd:PRK15134 417 ETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVrALCHQV 496
|
250
....*....|..
gi 491227761 819 VVLDHGRVAETG 830
Cdd:PRK15134 497 IVLRQGEVVEQG 508
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
628-826 |
1.26e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 74.29 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLArfhdverGAIRIDGTDIRT--LTP----DELYAKVGFVF-QDVQL 700
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILS-------GLLQPTSGEVRVagLVPwkrrKKFLRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 701 VAG-TVRENIALACPEATDDDVESAARDAQIHErILRLpngyDTVLDTDT-QLSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:cd03267 107 WWDlPVIDSFYLLAAIYDLPPARFKKRLDELSE-LLDL----EELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491227761 779 AFADPESEYLVQQALGRLIDNR--TVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
618-837 |
1.32e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDG--TDIRTLTPDELYAKVGFVF 695
Cdd:PRK13636 9 EELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 Q--DVQLVAGTVRENIA-----LACPEatdddvesaardAQIHERILRL--PNGYDTVLDTDTQ-LSGGEKQRLTIARAL 765
Cdd:PRK13636 89 QdpDNQLFSASVYQDVSfgavnLKLPE------------DEVRKRVDNAlkRTGIEHLKDKPTHcLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 766 LADTPILILDEATAFADP----ESEYLVQQALGRLidNRTVLVIAHRLHTIA-DADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPmgvsEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFA 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
612-848 |
1.59e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 612 VASVSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIrTLTPDELYAK- 690
Cdd:PRK10895 1 MATLTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPLHARARr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 -VGFVFQDVQLVAG-TVRENIaLACPEATDDDVESAARD------AQIHERILRLPNGydtvldtdTQLSGGEKQRLTIA 762
Cdd:PRK10895 79 gIGYLPQEASIFRRlSVYDNL-MAVLQIRDDLSAEQREDranelmEEFHIEHLRDSMG--------QSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 763 RALLADTPILILDEATAFADPES--------EYLVQQALGRLIDNRTVlviahrLHTIADADQIVVLDHGRVAETGTHTD 834
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISvidikriiEHLRDSGLGVLITDHNV------RETLAVCERAYIVSQGHLIAHGTPTE 223
|
250
....*....|....
gi 491227761 835 LLANNgRYRRLWEG 848
Cdd:PRK10895 224 ILQDE-HVKRVYLG 236
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
630-838 |
1.82e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE-------------LYAKVGFVFQ 696
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 697 DVQLVAG-TVRENIALAcPEATDDDVESAARdaqihERILRLPN--GYDTVLDTD--TQLSGGEKQRLTIARALLADTPI 771
Cdd:PRK10619 100 HFNLWSHmTVLENVMEA-PIQVLGLSKQEAR-----ERAVKYLAkvGIDERAQGKypVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 772 LILDEATAFADPE--SEYL-VQQALGRliDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK10619 174 LLFDEPTSALDPElvGEVLrIMQQLAE--EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
631-824 |
2.04e-14 |
|
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: 72.66 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLA-RFHD-VERGAIRIDGTDIrtltPDELYAKVGFVFQ-DVQLVAGTVRE 707
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgRKTAgVITGEILINGRPL----DKNFQRSTGYVEQqDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 708 NIALacpeatdddveSAArdaqiheriLRlpngydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADPESEY 787
Cdd:cd03232 99 ALRF-----------SAL---------LR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491227761 788 LVQQALGRLIDN-RTVLVIAHR--LHTIADADQIVVLDHG 824
Cdd:cd03232 146 NIVRFLKKLADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
633-838 |
2.26e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.00 E-value: 2.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDirTLTPDELYAKVgfVFQDVQLV----AGTV--R 706
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQD--LLKADPEAQKL--LRQKIQIVfqnpYGSLnpR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIA--LACPEATDDDVESAARDAQIHERI----LRlPNGYDTVldtDTQLSGGEKQRLTIARALLADTPILILDEATAF 780
Cdd:PRK11308 109 KKVGqiLEEPLLINTSLSAAERREKALAMMakvgLR-PEHYDRY---PHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 781 ADPEseylVQ-QALGRLID-----NRTVLVIAHRL----HTiadADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK11308 185 LDVS----VQaQVLNLMMDlqqelGLSYVFISHDLsvveHI---ADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
609-838 |
2.54e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.36 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 609 ADAVASVSfegVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDV-----ERGAIRIDGTDIRTLT 683
Cdd:PRK14271 19 APAMAAVN---LTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 684 PD-ELYAKVGFVFQDVQLVAGTVRENIaLACPEATDDDVESAARD-AQIHERILRLPNGY-DTVLDTDTQLSGGEKQRLT 760
Cdd:PRK14271 95 DVlEFRRRVGMLFQRPNPFPMSIMDNV-LAGVRAHKLVPRKEFRGvAQARLTEVGLWDAVkDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 761 IARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
613-776 |
2.59e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.26 E-value: 2.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDElyAKVG 692
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDVQLVAG-TVRENIALA-----CPEAT-DDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARAL 765
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGlkirgMPKAEiEERVAEAARILELEPLLDRKPR----------ELSGGQRQRVAMGRAI 149
|
170
....*....|.
gi 491227761 766 LADTPILILDE 776
Cdd:PRK11650 150 VREPAVFLFDE 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
619-825 |
2.71e-14 |
|
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: 76.51 E-value: 2.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 619 GVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLArfhdverGairIDgTDIR---TLTPDelyAKVGFVF 695
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------G---VD-KDFNgeaRPQPG---IKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQL-VAGTVRENIALACPEAT----------------DDDVES-AARDAQIHERI------------------LRLPN 739
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKdaldrfneisakyaepDADFDKlAAEQAELQEIIdaadawdldsqleiamdaLRCPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 740 GydtvlDTD-TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLidNRTVLVIAHRLHTIADADQ- 817
Cdd:TIGR03719 155 W-----DADvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTHDRYFLDNVAGw 227
|
....*...
gi 491227761 818 IVVLDHGR 825
Cdd:TIGR03719 228 ILELDRGR 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
621-853 |
2.77e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 73.72 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 621 TFGYRPG------VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGT------------DIRtl 682
Cdd:COG4167 13 TFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdykyrckHIR-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 683 tpdelyakvgFVFQDvqlvAGTV---RENIA--LACPEATDDDVESAARDAQIHErILRL-----------PNgydtvld 746
Cdd:COG4167 91 ----------MIFQD----PNTSlnpRLNIGqiLEEPLRLNTDLTAEEREERIFA-TLRLvgllpehanfyPH------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 747 tdtQLSGGEKQRLTIARALLADTPILILDEATAFADPE------------------SEYLVQQALGrlidnrtvlVIAHr 808
Cdd:COG4167 149 ---MLSSGQKQRVALARALILQPKIIIADEALAALDMSvrsqiinlmlelqeklgiSYIYVSQHLG---------IVKH- 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 491227761 809 lhtIadADQIVVLDHGRVAETGTHTDLLAN--NGRYRRLWEGHRHEQ 853
Cdd:COG4167 216 ---I--SDKVLVMHQGEVVEYGKTAEVFANpqHEVTKRLIESHFGEA 257
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
612-837 |
2.97e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 2.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 612 VASVSFEGVTFGYRPGVpVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPdELYAKV 691
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR-HARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAG-TVRENI----------ALACPEATDDDVESAardaqiherilRLPNGYDTVLdtdTQLSGGEKQRLT 760
Cdd:PRK13537 83 GVVPQFDNLDPDfTVRENLlvfgryfglsAAAARALVPPLLEFA-----------KLENKADAKV---GELSGGMKRRLT 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 761 IARALLADTPILILDEATAFADPESEYLVQQALGRLI-DNRTVLVIAH------RLhtiadADQIVVLDHGRVAETGTHT 833
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVIEEGRKIAEGAPH 223
|
....
gi 491227761 834 DLLA 837
Cdd:PRK13537 224 ALIE 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
615-848 |
4.35e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.26 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGyRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KV 691
Cdd:PRK11831 8 VDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAG-TVRENIALACPEATdddvesaardaQIHERILRlpngyDTVLD-------------TDTQLSGGEKQ 757
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPLREHT-----------QLPAPLLH-----STVMMkleavglrgaaklMPSELSGGMAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 758 RLTIARALLADTPILILDEATAFADPeseyLVQQALGRLIDNR------TVLVIAH---RLHTIADADQIVVlDHGRVAE 828
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPFVGQDP----ITMGVLVKLISELnsalgvTCVVVSHdvpEVLSIADHAYIVA-DKKIVAH 225
|
250 260
....*....|....*....|.
gi 491227761 829 tGTHTDLLANNG-RYRRLWEG 848
Cdd:PRK11831 226 -GSAQALQANPDpRVRQFLDG 245
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
629-847 |
4.41e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 76.70 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLAS-LLARFHDVERGAIRIDGTdirtltpdelyakVGFVFQDVQLVAGTVRE 707
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFNATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 708 NIALACPEATDD-----DVESAARDAQIherilrLPNGYDTVL-DTDTQLSGGEKQRLTIARALLADTPILILDeatafa 781
Cdd:PLN03130 698 NILFGSPFDPERyeraiDVTALQHDLDL------LPGGDLTEIgERGVNISGGQKQRVSMARAVYSNSDVYIFD------ 765
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 782 DPES---EYLVQQALGRLID----NRTVLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLANNGRYRRLWE 847
Cdd:PLN03130 766 DPLSaldAHVGRQVFDKCIKdelrGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
597-826 |
6.75e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.06 E-value: 6.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 597 ETELDVIEAPVTADAVAsVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDG 676
Cdd:COG3845 241 EVLLRVEKAPAEPGEVV-LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 677 TDIRTLTPDELY-AKVGFVFQDVQ---LVAG-TVRENIALacpEATDDDVESAA---RDAQIHERILRLPNGYDTVL-DT 747
Cdd:COG3845 320 EDITGLSPRERRrLGVAYIPEDRLgrgLVPDmSVAENLIL---GRYRRPPFSRGgflDRKAIRAFAEELIEEFDVRTpGP 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 748 DT---QLSGGEKQRLTIARALLADTPILI-------LDE-ATAFadpeseylVQQalgRLIDNR----TVLVIAHRLhti 812
Cdd:COG3845 397 DTparSLSGGNQQKVILARELSRDPKLLIaaqptrgLDVgAIEF--------IHQ---RLLELRdagaAVLLISEDL--- 462
|
250
....*....|....*....
gi 491227761 813 aD-----ADQIVVLDHGRV 826
Cdd:COG3845 463 -DeilalSDRIAVMYEGRI 480
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
615-826 |
7.03e-14 |
|
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: 71.54 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPgVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLT-------PDE- 686
Cdd:cd03269 1 LEVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnrigylPEEr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 687 -LYAKVgfvfqdvqlvagTVREN-IALAcpEATDDDVESAARDAQIHERILRLPNGYDTVLDtdtQLSGGEKQRLTIARA 764
Cdd:cd03269 80 gLYPKM------------KVIDQlVYLA--QLKGLKKEEARRRIDEWLERLELSEYANKRVE---ELSKGNQQKVQFIAA 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:cd03269 143 VIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRA 206
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
300-567 |
9.01e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 72.95 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 300 MIAGGVLQAIITMVELAPfvvlVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMAL-----TLWLHVVDLRFSADVR 374
Cdd:cd18778 1 LILTLLCALLSTLLGLVP----PWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALlnflrIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 375 RRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILvyLLT 454
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIP--FLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 455 MMAMMYqsGPKIVEASRWADRMSTESTAYLE----GQPVIRIFG--GAAASSFKRRLDDYLR------FLNDWQRPFIGr 522
Cdd:cd18778 155 LGAWLY--SKKVRPRYRKVREALGELNALLQdnlsGIREIQAFGreEEEAKRFEALSRRYRKaqlramKLWAIFHPLME- 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 523 ktfmdlvtrpttflwLIATAGTLFVV--------SGAMQPVTLLPFLVLGTTF 567
Cdd:cd18778 232 ---------------FLTSLGTVLVLgfggrlvlAGELTIGDLVAFLLYLGLF 269
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
613-839 |
1.50e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELyakVG 692
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 693 FVFQDvqlvagtvrENIALACPEATDDDVESAARDaqiHERILRLPNGYDTVLDTDT---------------QLSGGEKQ 757
Cdd:PRK15056 82 YVPQS---------EEVDWSFPVLVEDVVMMGRYG---HMGWLRRAKKRDRQIVTAAlarvdmvefrhrqigELSGGQKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 758 RLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRLHTIADADQIVVLDHGRVAETG-THTDL 835
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGpTETTF 229
|
....
gi 491227761 836 LANN 839
Cdd:PRK15056 230 TAEN 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
626-825 |
1.79e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 626 PGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARF--HDVERGAIRIDGTDIRTLT-PDELYAKVGFVFQDVQLVA 702
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNiRDTERAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 G-TVRENIALACpEATDDDVesaARDAQIHERILRLPNGYDTVLDTDT---QLSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:PRK13549 96 ElSVLENIFLGN-EITPGGI---MDYDAMYLRAQKLLAQLKLDINPATpvgNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491227761 779 AfADPESEYLVQQALGRLIDNRTV--LVIAHRLHTIAD-ADQIVVLDHGR 825
Cdd:PRK13549 172 A-SLTESETAVLLDIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
630-810 |
2.27e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA----KVGFVFQDVQLVAG-T 704
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 705 VRENIALACpeatdddVESAARDAQIHERILRL--PNGYDT-VLDTDTQLSGGEKQRLTIARALLADTPILILDEATAFA 781
Cdd:PRK11629 104 ALENVAMPL-------LIGKKKPAEINSRALEMlaAVGLEHrANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|...
gi 491227761 782 DPESEYLVQQALGRLidNR----TVLVIAHRLH 810
Cdd:PRK11629 177 DARNADSIFQLLGEL--NRlqgtAFLVVTHDLQ 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
610-830 |
4.44e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.40 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 610 DAVASVSFEGVTFGYRPGVpVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA 689
Cdd:PRK10253 3 ESVARLRGEQLTLGYGKYT-VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 KVGFVFQDVQLVAG-TVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLAD 768
Cdd:PRK10253 82 RIGLLAQNATTPGDiTVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 769 TPILILDEATAFADPESEYLVQQALGRLidNR----TVLVIAHRLHTIAD-ADQIVVLDHGRVAETG 830
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSEL--NRekgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
594-831 |
6.20e-13 |
|
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: 73.12 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 594 ALDETE--LDVIEAPVTADAVASVSFEGVTFGYRPGV--------------PVIHDVSLTLRHGTVTALVGPSGSGKSTL 657
Cdd:TIGR01257 893 ALEKTEplTEEMEDPEHPEGINDSFFERELPGLVPGVcvknlvkifepsgrPAVDRLNITFYENQITAFLGHNGAGKTTT 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 658 ASLLARFHDVERGAIRIDGTDIRTlTPDELYAKVGFVFQ-DVQLVAGTVRENIALACP------EATDDDVESAARDAQI 730
Cdd:TIGR01257 973 LSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQhNILFHHLTVAEHILFYAQlkgrswEEAQLEMEAMLEDTGL 1051
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 731 HERilRLPNGYDtvldtdtqLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDNRTVLVIAHRLH 810
Cdd:TIGR01257 1052 HHK--RNEEAQD--------LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD 1121
|
250 260
....*....|....*....|...
gi 491227761 811 TiAD--ADQIVVLDHGRVAETGT 831
Cdd:TIGR01257 1122 E-ADllGDRIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
300-561 |
6.26e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 70.23 E-value: 6.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 300 MIAGGVLQAIITMVELAPfvvlVELTRQLL---AGADEAQLRHTGFVFLVLLVLGATLGMALTLWLH-----VVDLRFSA 371
Cdd:cd18563 1 LILGFLLMLLGTALGLVP----PYLTKILIddvLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRgrllaRLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 372 DVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVy 451
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 452 lltMMAMMYQSGPKI-----VEASRWADRMSTESTAyLEGQPVIRIFG--GAAASSFKRRLDDYL----RFLNDWQRPFI 520
Cdd:cd18563 156 ---VVWGSYFFWKKIrrlfhRQWRRWSRLNSVLNDT-LPGIRVVKAFGqeKREIKRFDEANQELLdaniRAEKLWATFFP 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491227761 521 grktFMDLVTrpTTFLWLIATAGTLFVVSGAMQPVTLLPFL 561
Cdd:cd18563 232 ----LLTFLT--SLGTLIVWYFGGRQVLSGTMTLGTLVAFL 266
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
620-839 |
7.05e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.50 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGYRPGVP----VIHDVSLTLRHGTVTALVGPSGSGKSTL-----ASLL------------------ARFHDVERGAI 672
Cdd:PRK13651 8 IVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFiehlnALLLpdtgtiewifkdeknkkkTKEKEKVLEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 673 RIDGTDIRTLTP-DELYAKVGFVFQ--DVQLVAGTVRENIALAcPEATDDDVESAARDAQIHERILRLPNGYdtvLDTDT 749
Cdd:PRK13651 88 VIQKTRFKKIKKiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDESY---LQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 750 -QLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDN-RTVLVIAHRL-HTIADADQIVVLDHGRV 826
Cdd:PRK13651 164 fELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRTIFFKDGKI 243
|
250
....*....|...
gi 491227761 827 AETGTHTDLLANN 839
Cdd:PRK13651 244 IKDGDTYDILSDN 256
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
614-843 |
8.93e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 69.75 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 614 SVSFEGVT--FGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLT-------P 684
Cdd:COG4152 1 MLELKGLTkrFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 685 DE--LYAKVgfvfqdvqlvagTVRENIA-LAcpeatdddvesaaR-----DAQIHERILRL-------PNGYDTVldtdT 749
Cdd:COG4152 78 EErgLYPKM------------KVGEQLVyLA-------------RlkglsKAEAKRRADEWlerlglgDRANKKV----E 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 750 QLSGGEKQRLTIARALLADTPILILDEatAFA--DPESEYLVQQALGRLIDN-RTVLVIAHRLHTIAD-ADQIVVLDHGR 825
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDE--PFSglDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEElCDRIVIINKGR 206
|
250
....*....|....*...
gi 491227761 826 VAETGTHTDLLANNGRYR 843
Cdd:COG4152 207 KVLSGSVDEIRRQFGRNT 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
627-837 |
1.74e-12 |
|
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: 70.60 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRI------------------DGTDIR----TLTP 684
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIiyhvalcekcgyverpskVGEPCPvcggTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 685 DE-------------LYAKVGFVFQDVQLVAG--TVRENIALACPEA---TDDDVESAA---RDAQIHERILRLPNgydt 743
Cdd:TIGR03269 92 EEvdfwnlsdklrrrIRKRIAIMLQRTFALYGddTVLDNVLEALEEIgyeGKEAVGRAVdliEMVQLSHRITHIAR---- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 744 vldtdtQLSGGEKQRLTIARAlLADTPILIL-DEATAFADPESEYLVQQALGRLIDNR--TVLVIAHRLHTIAD-ADQIV 819
Cdd:TIGR03269 168 ------DLSGGEKQRVVLARQ-LAKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAI 240
|
250
....*....|....*...
gi 491227761 820 VLDHGRVAETGTHTDLLA 837
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
625-831 |
1.81e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDG----------TDIRTLTPDELY----AK 690
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRhvrgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQDVQLVAG---TVRENIALACPEATDDDVESAARDAQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLA 767
Cdd:PRK10261 106 MAMIFQEPMTSLNpvfTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 768 DTPILILDEATAFADPESEYLVQQALGRLIDNRT--VLVIAHRLHTIAD-ADQIVVLDHGRVAETGT 831
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
628-837 |
2.20e-12 |
|
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: 70.60 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIR-------IDGTDIRTLTPDELYAKVGFVFQDVQL 700
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 701 -----VAGTVRENIALACPEatdddvESAARDAQIHERILrlpnGYD-----TVLDTDT-QLSGGEKQRLTIARALLADT 769
Cdd:TIGR03269 377 yphrtVLDNLTEAIGLELPD------ELARMKAVITLKMV----GFDeekaeEILDKYPdELSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 770 PILILDEATAFADPESEYLVQQAL--GRLIDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
637-821 |
2.69e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 637 TLRHGTVTALVGPSGSGKSTLASLLA-----RFHDVERGAI------RIDGTDIRTLTpDELYA---KVGFVFQDVQLVA 702
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSgelipNLGDYEEEPSwdevlkRFRGTELQNYF-KKLYNgeiKVVHKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 ----GTVRENIalacpEATDddvESAARDaqihERILRLpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDEA 777
Cdd:PRK13409 174 kvfkGKVRELL-----KKVD---ERGKLD----EVVERL--GLENILDRDiSELSGGELQRVAIAAALLRDADFYFFDEP 239
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491227761 778 TAFADPESEYLVQQALGRLIDNRTVLVIAHRLhTIAD--ADQIVVL 821
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
634-851 |
3.01e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 634 VSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVErGAIRIDGTDIRTLTPDELYAKVGFVFQDVQ-LVAGTVRENIALA 712
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 713 CPeatdDDVESAARDAQIHERILRLpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTP-------ILILDEATAFADpe 784
Cdd:PRK03695 94 QP----DKTRTEAVASALNEVAEAL--GLDDKLGRSvNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLD-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 785 seyLVQQ-ALGRLID-----NRTVLVIAHRL-HTIADADQIVVLDHGRVAETGTHTDLLANNG-------RYRRL-WEGH 849
Cdd:PRK03695 166 ---VAQQaALDRLLSelcqqGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPENlaqvfgvNFRRLdVEGH 242
|
..
gi 491227761 850 RH 851
Cdd:PRK03695 243 PM 244
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
613-838 |
4.39e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 613 ASVSFEGVTFGYRPgVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTL-TPDELYAKV 691
Cdd:PRK11614 4 VMLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAG-TVRENIALAcpeatdddvESAARDAQIHERILRLPNGYDTVLDTDTQ----LSGGEKQRLTIARALL 766
Cdd:PRK11614 83 AIVPEGRRVFSRmTVEENLAMG---------GFFAERDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 767 ADTPILILDEATAFADPeseYLVQQALGRLIDNRT-----VLVIAHRLHTIADADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAP---IIIQQIFDTIEQLREqgmtiFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
619-807 |
5.24e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 5.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 619 GVTFGYRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLArfhdverGairIDgTDIR---TLTPDelyAKVGFVF 695
Cdd:PRK11819 11 RVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------G---VD-KEFEgeaRPAPG---IKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVAG-TVRENIALACPE---------------ATDDDV--ESAARDAQIHERI------------------LRLPN 739
Cdd:PRK11819 77 QEPQLDPEkTVRENVEEGVAEvkaaldrfneiyaayAEPDADfdALAAEQGELQEIIdaadawdldsqleiamdaLRCPP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 740 GydtvlDTD-TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQAL----GrlidnrTVLVIAH 807
Cdd:PRK11819 157 W-----DAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLhdypG------TVVAVTH 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
320-591 |
5.86e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 67.12 E-value: 5.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 320 VLVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLDKLSRVPLGWFTQRGSGSVKK 399
Cdd:cd18576 18 LAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 400 LIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLipILVYLLTMMAMMYqsGPKIVEASR-WADRMSt 478
Cdd:cd18576 98 RLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLML--ATVPVVVLVAVLF--GRRIRKLSKkVQDELA- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 479 ESTAYLE----GQPVIRIFGGAA--ASSFKRRLDDYLRF------LNDWQRPFIGRKTFMDLVtrptTFLWLiataGTLF 546
Cdd:cd18576 173 EANTIVEetlqGIRVVKAFTREDyeIERYRKALERVVKLalkrarIRALFSSFIIFLLFGAIV----AVLWY----GGRL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 491227761 547 VVSGAMQPVTLLPFLVLGTTFGARLLGIAYGLGSIRGGLESARHI 591
Cdd:cd18576 245 VLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
634-838 |
7.00e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.62 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 634 VSLTLRHGTVTALVGPSGSGKSTLASLLARFHD----VERGAIRIDGTDIRTLTPDELYAKVG----FVFQDVQLV---A 702
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRKIIGreiaMIFQEPSSCldpS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 GTVRENIALACPeatDDDVES------AARDAQI-----------HERILR-LPNgydtvldtdtQLSGGEKQRLTIARA 764
Cdd:COG4170 106 AKIGDQLIEAIP---SWTFKGkwwqrfKWRKKRAiellhrvgikdHKDIMNsYPH----------ELTEGECQKVMIAMA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491227761 765 lLADTP-ILILDEATAFADPESEYLVQQALGRL--IDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLAN 838
Cdd:COG4170 173 -IANQPrLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
641-837 |
7.46e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 641 GTVTALVGPSGSGKSTLASLLA-RFH-DVERGAIRIDGtdiRTLTpDELYAKVGFVFQDVQLVAG-TVRENIA----LAC 713
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANN---RKPT-KQILKRTGFVTQDDILYPHlTVRETLVfcslLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 714 PEATDDDVESAARDAQIHEriLRLPNGYDTVLDTD--TQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQ 791
Cdd:PLN03211 170 PKSLTKQEKILVAESVISE--LGLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVL 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 491227761 792 ALGRLIDN-RTVLVIAH----RLHTIADAdqIVVLDHGRVAETGTHTDLLA 837
Cdd:PLN03211 248 TLGSLAQKgKTIVTSMHqpssRVYQMFDS--VLVLSEGRCLFFGKGSDAMA 296
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
629-838 |
2.02e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.05 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARF--HDVERGAIRIDGTDIRTLTPDElYAKVG--FVFQDVQLVAGT 704
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHLGifLAFQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 705 VREN-IALAC---------PEAtdDDVESaardAQIHERILRLPNGYDTVLDTDTQ--LSGGEKQRLTIARALLADTPIL 772
Cdd:CHL00131 100 SNADfLRLAYnskrkfqglPEL--DPLEF----LEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 773 ILDEATAFADPESEYLVQQALGRLID-NRTVLVIAH--RLHTIADADQIVVLDHGRVAETGTHTdlLAN 838
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE--LAK 240
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
630-836 |
2.67e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLA-------RFHDVE-RGAIRIDGTDIRTLTPDELYAKVGFVFQDVQ-L 700
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggAPRGARvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 701 VAGTVRENIALACPEATDDDVESAARDAQIHERILRLPnGYDTVLDTD-TQLSGGEKQRLTIARAL---------LADTP 770
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDvTTLSGGELARVQFARVLaqlwpphdaAQPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 771 ILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIA-DADQIVVLDHGRVAETGTHTDLL 836
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVL 243
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
632-830 |
4.03e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 632 HDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLtpdELYA------------KVGFVFQDV- 698
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLR---DLYAlseaerrrllrtEWGFVHQHPr 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 699 ---------------QLVA------GTVREnialacpEATD--DDVESAArdaqihERILRLPngydtvldtdTQLSGGE 755
Cdd:PRK11701 100 dglrmqvsaggnigeRLMAvgarhyGDIRA-------TAGDwlERVEIDA------ARIDDLP----------TTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 756 KQRLTIARALLADTPILILDEATAFADPEseylVQqalGRLID---------NRTVLVIAHRLhTIAD--ADQIVVLDHG 824
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQ---ARLLDllrglvrelGLAVVIVTHDL-AVARllAHRLLVMKQG 228
|
....*.
gi 491227761 825 RVAETG 830
Cdd:PRK11701 229 RVVESG 234
|
|
| FAD_binding_9 |
pfam08021 |
Siderophore-interacting FAD-binding domain; |
21-118 |
4.13e-11 |
|
Siderophore-interacting FAD-binding domain;
Pssm-ID: 311811 Cd Length: 118 Bit Score: 60.76 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 21 TVVGTAPVAPNCVRITMSAP------TLFED----LL-----HTPAEWLRF----WFPDPDGGTSEHQRAYTIVTTDEDA 81
Cdd:pfam08021 1 QVVRVTRLSPHMRRITFTGPglagfpSDGTDqhikLFfpppgQTPPAVPPTlgedGPIWPPEDQRPVMRTYTVRAYDPEA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 491227761 82 GEFSIDVVIHEPAGPACQWAVAAQPGMTIPVVAFGSA 118
Cdd:pfam08021 81 GELDIDFVLHGDEGPAARWAAQAQPGDVLGIVGPGGA 117
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
628-837 |
4.41e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 65.21 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHD----VERGAIRIDGTDIRTLTPDELYAKVG----FVFQDVQ 699
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLLRLSPRERRKLVGhnvsMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 700 LV---AGTVRENIALACPEATdddveSAARDAQ-IHERILR---------LPNGYDTVLDTDTQLSGGEKQRLTIARALL 766
Cdd:PRK15093 100 SCldpSERVGRQLMQNIPGWT-----YKGRWWQrFGWRKRRaiellhrvgIKDHKDAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 767 ADTPILILDEATAFADPESEYLVQQALGRL--IDNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
629-828 |
4.56e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDgtdirtLTPDELYakvgfvfQDVQLVagtvrEN 708
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFG-------REASLI-----DA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 709 IALACPeaTDDDVESAAR----DAQIherILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADPE 784
Cdd:COG2401 106 IGRKGD--FKDAVELLNAvglsDAVL---WLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491227761 785 SEYLVQQALGRLIDNR--TVLVIAHRLHTIAD--ADQIVVLDHGRVAE 828
Cdd:COG2401 171 TAKRVARNLQKLARRAgiTLVVATHHYDVIDDlqPDLLIFVGYGGVPE 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
625-793 |
4.75e-11 |
|
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: 62.90 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGT 704
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 705 VRENIALACPEATDDDVESAARDAQIherilrlpNGYDTVldTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPE 784
Cdd:cd03231 90 VLENLRFWHADHSDEQVEEALARVGL--------NGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 491227761 785 SEYLVQQAL 793
Cdd:cd03231 160 GVARFAEAM 168
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
640-823 |
5.47e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.62 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 640 HGTVTALVGPSGSGKSTLASLLARFHDV-ERGAIRIDGTDIRTLTPDELYakvgfvfqdvqlvagtvrenialacpeatd 718
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 719 ddvesaardaqiherilrlpngYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLID 798
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180 190
....*....|....*....|....*....|..
gi 491227761 799 -------NRTVLVIAHRLHTIADADQIVVLDH 823
Cdd:smart00382 109 lllksekNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
628-838 |
5.98e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYA---KVGFVFQDV------ 698
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDPyasldp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 699 -QLVAGTVRENIALacpEATDDDVESAARDAQIHERILRLPngyDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEA 777
Cdd:PRK10261 417 rQTVGDSIMEPLRV---HGLLPGKAAAARVAWLLERVGLLP---EHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 778 TAFADPEseyLVQQALGRLIDNRTVLVIAHRL--HTIADADQI----VVLDHGRVAETGTHTDLLAN 838
Cdd:PRK10261 491 VSALDVS---IRGQIINLLLDLQRDFGIAYLFisHDMAVVERIshrvAVMYLGQIVEIGPRRAVFEN 554
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
620-835 |
6.93e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.75 E-value: 6.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 620 VTFGYRPG-VPVIHDVSLTLRHGTVTALVGPSGSGKS----TLASLLARFHDVErGAIRIDGTDIRTLTPDEL----YAK 690
Cdd:PRK09473 20 VTFSTPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLPEKELnklrAEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 691 VGFVFQD------------------VQLVAG---------TVRENIALACPEAtdddvesaardaqiHERILRLPNgydt 743
Cdd:PRK09473 99 ISMIFQDpmtslnpymrvgeqlmevLMLHKGmskaeafeeSVRMLDAVKMPEA--------------RKRMKMYPH---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 744 vldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIAD-ADQIVV 820
Cdd:PRK09473 161 ------EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLV 234
|
250
....*....|....*
gi 491227761 821 LDHGRVAETGTHTDL 835
Cdd:PRK09473 235 MYAGRTMEYGNARDV 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
637-821 |
8.37e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.58 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 637 TLRHGTVTALVGPSGSGKSTLASLLA-----RFHDVERGAI------RIDGTDIRT----LTPDELYA--KVGFVFQDVQ 699
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSgelkpNLGDYDEEPSwdevlkRFRGTELQDyfkkLANGEIKVahKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 700 LVAGTVRENIalacpEATDDdvesaaRDAqIHERILRLpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:COG1245 175 VFKGTVRELL-----EKVDE------RGK-LDELAEKL--GLENILDRDiSELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 491227761 779 AFADpeseylVQQ--ALGRLI-----DNRTVLVIAHRLhTIAD--ADQIVVL 821
Cdd:COG1245 241 SYLD------IYQrlNVARLIrelaeEGKYVLVVEHDL-AILDylADYVHIL 285
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
630-844 |
9.00e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 9.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIrtlTPDELYAK-VGFVFQDVQLVAG-TVRE 707
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRdICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 708 NIALACPEAtddDVESAARDAQIHE--RILRLPNGYDTVLDtdtQLSGGEKQRLTIARALLADTPILILDEATAFADP-- 783
Cdd:PRK11432 98 NVGYGLKML---GVPKEERKQRVKEalELVDLAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEPLSNLDAnl 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 784 -----ESEYLVQQALgrlidNRTVLVIAH-RLHTIADADQIVVLDHGRVAETGTHTDLlanngrYRR 844
Cdd:PRK11432 172 rrsmrEKIRELQQQF-----NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL------YRQ 227
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
633-821 |
9.22e-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: 63.40 E-value: 9.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLrhGTVTALVGPSGSGKS-----TLASLLARF----------HDVERGA------IRIDGTDI-RTLTPDEL-YA 689
Cdd:cd03271 15 DVDIPL--GVLTCVTGVSGSGKSslindTLYPALARRlhlkkeqpgnHDRIEGLehidkvIVIDQSPIgRTPRSNPAtYT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 KVgF-----VFQDV--------QLVAGTVR-ENIALACPEATDDDVESAARDAQIHERILRLPN---GYDTVLDTDTQLS 752
Cdd:cd03271 93 GV-FdeireLFCEVckgkrynrETLEVRYKgKSIADVLDMTVEEALEFFENIPKIARKLQTLCDvglGYIKLGQPATTLS 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 753 GGEKQRLTIARALL-ADT--PILILDEATA---FADpeseylVQQ---ALGRLIDN-RTVLVIAHRLHTIADADQIVVL 821
Cdd:cd03271 172 GGEAQRIKLAKELSkRSTgkTLYILDEPTTglhFHD------VKKlleVLQRLVDKgNTVVVIEHNLDVIKCADWIIDL 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
629-837 |
9.65e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLA-SLLARFHD--VE--RGAIRIDGTDIRTLTPDELYA----KVGFVFQD-- 697
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSppVVypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQL-----VAGTVRENIAL---ACPEATDDDVESAARDAQIHERILRLPngydtvlDTDTQLSGGEKQRLTIARALLADT 769
Cdd:PRK15134 103 VSLnplhtLEKQLYEVLSLhrgMRREAARGEILNCLDRVGIRQAAKRLT-------DYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 770 PILILDEATAFADPESEYLVQQALGRLID--NRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
615-840 |
9.96e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 65.53 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDI-----RtltpDELYA 689
Cdd:NF033858 2 ARLEGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarhR----RAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 690 KVGFVFQdvqlvaG---------TVRENIalacpeatdddvESAAR-----DAQIHERILRL------------PNGydt 743
Cdd:NF033858 77 RIAYMPQ------GlgknlyptlSVFENL------------DFFGRlfgqdAAERRRRIDELlratglapfadrPAG--- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 744 vldtdtQLSGGEKQRLTIARALLADTPILILDEATAFADPeseylvqqaLGR-----LIDN-R------TVLViahrlht 811
Cdd:NF033858 136 ------KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP---------LSRrqfweLIDRiRaerpgmSVLV------- 193
|
250 260 270
....*....|....*....|....*....|....*..
gi 491227761 812 iADA--------DQIVVLDHGRVAETGTHTDLLANNG 840
Cdd:NF033858 194 -ATAymeeaerfDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
626-824 |
1.27e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 626 PGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP-DELYAKVGFVFQDVQLVAG- 703
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPkSSQEAGIGIIHQELNLIPQl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALAcPEAT------DDDVESAARDAQIHEriLRLPNGYDTVLdtdTQLSGGEKQRLTIARALLADTPILILDEA 777
Cdd:PRK10762 95 TIAENIFLG-REFVnrfgriDWKKMYAEADKLLAR--LNLRFSSDKLV---GELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 491227761 778 T-AFADPESEylvqqALGRLI-----DNRTVLVIAHRLHTIAD-ADQIVVLDHG 824
Cdd:PRK10762 169 TdALTDTETE-----SLFRVIrelksQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
627-833 |
1.42e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.50 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHD--VERGAIRIDGTDIRTLTPDELYAKVGFV-FQDVQLVAG 703
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRAGEGIFMaFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALACPEATDDDVESAARDA-----QIHERI--LRLPNGYDTvLDTDTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:PRK09580 93 VSNQFFLQTALNAVRSYRGQEPLDRfdfqdLMEEKIalLKMPEDLLT-RSVNVGFSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 777 ATAFADPESEYLVQQALGRLID-NRTVLVIAH--RLHTIADADQIVVLDHGRVAETGTHT 833
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFT 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
621-829 |
1.90e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 621 TFgyrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARF--HDVERGAIRIDGT-----DIRTltpDElyaKVGF 693
Cdd:NF040905 10 TF---PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEvcrfkDIRD---SE---ALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 694 VF--QDVQLVAG-TVRENIALACPEATD---DDVESAARDAQIHERIlrlpnGYDTVLDTD-TQLSGGEKQRLTIARALL 766
Cdd:NF040905 81 VIihQELALIPYlSIAENIFLGNERAKRgviDWNETNRRARELLAKV-----GLDESPDTLvTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 767 ADTPILILDEATA-FADPESEYLvqqaLGRLIDNR----TVLVIAHRLHTIAD-ADQIVVLDHGRVAET 829
Cdd:NF040905 156 KDVKLLILDEPTAaLNEEDSAAL----LDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIET 220
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
621-825 |
2.19e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.08 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 621 TFGyrpGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARF--HDVERGAIRIDGTDIRTLTPDELYAK-VGFVFQD 697
Cdd:TIGR02633 10 TFG---GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTERAgIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQLVAG-TVRENIALA----CPEATDDDVESAARdAQIHERILRLPNGYDTVLDTDtqLSGGEKQRLTIARALLADTPIL 772
Cdd:TIGR02633 87 LTLVPElSVAENIFLGneitLPGGRMAYNAMYLR-AKNLLRELQLDADNVTRPVGD--YGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 773 ILDEATAfADPESEYLVQQALGRLIDNRTV--LVIAHRLHTI-ADADQIVVLDHGR 825
Cdd:TIGR02633 164 ILDEPSS-SLTEKETEILLDIIRDLKAHGVacVYISHKLNEVkAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
629-837 |
4.01e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.56 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDI----RTLTPdeLYAKVGFVFQDV-QLVAG 703
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLA--LRQQVATVFQDPeQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TvrenialacpeATDDDVESAARDAQIHE-RILRLPNGYDTVLDTD-------TQLSGGEKQRLTIARALLADTPILILD 775
Cdd:PRK13638 93 T-----------DIDSDIAFSLRNLGVPEaEITRRVDEALTLVDAQhfrhqpiQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 776 EATAFADPESEYLVQQALGRLI-DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
626-826 |
4.74e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 4.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 626 PGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLA-SLLARFHDVERGAIRIDGTDIRTLTP-DELYAKVGFVFQD------ 697
Cdd:PRK13549 273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVqCLFGAYPGRWEGEIFIDGKPVKIRNPqQAIAQGIAMVPEDrkrdgi 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQLVAgtVRENIALACPE--ATDDDVESAARDAQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:PRK13549 353 VPVMG--VGKNITLAALDrfTGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILD 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 776 EATAFADPESEY--------LVQQALGrlidnrtVLVIAHRLHTIAD-ADQIVVLDHGRV 826
Cdd:PRK13549 431 EPTRGIDVGAKYeiyklinqLVQQGVA-------IIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
308-591 |
5.58e-10 |
|
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: 61.42 E-value: 5.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 308 AIITMVELAPFVVLVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLDKLSRVPLG 387
Cdd:cd18557 6 LISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 388 WFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLtmMAMMYqsGPKIV 467
Cdd:cd18557 86 FFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLI--ASKIY--GRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 468 EASR-WADRMSTESTAYLE---GQPVIRIFGG--AAASSFKRRLDDYLRflndwqrpfIGRK------TFMDLvtrpTTF 535
Cdd:cd18557 162 KLSKeVQDALAKAGQVAEEslsNIRTVRSFSAeeKEIRRYSEALDRSYR---------LARKkalanaLFQGI----TSL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 536 LWLIATAGTLF-----VVSGAMQPVTLLPFLVLGTTFGARLLGIAYGLGSIRGGLESARHI 591
Cdd:cd18557 229 LIYLSLLLVLWyggylVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
627-808 |
7.17e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 62.84 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 627 GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGairidgtdirTLTPDElYAKVGFVFQDVQLVAGTVR 706
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG----------RLTKPA-KGKLFYVPQRPYMTLGTLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 707 ENIALacPEATDDDVESAARDAQIH--------ERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEAT 778
Cdd:TIGR00954 533 DQIIY--PDSSEDMKRRGLSDKDLEqildnvqlTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|..
gi 491227761 779 AFADPEseylVQQALGRLIDNR--TVLVIAHR 808
Cdd:TIGR00954 611 SAVSVD----VEGYMYRLCREFgiTLFSVSHR 638
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
625-785 |
1.51e-09 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 58.52 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDelyakvgfvFQDVQLVAG- 703
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE---------PHENILYLGh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 --------TVRENIALACP--EATDDDVESAARDAQIHERILRLPNgydtvldtdtQLSGGEKQRLTIARALLADTPILI 773
Cdd:TIGR01189 81 lpglkpelSALENLHFWAAihGGAQRTIEDALAAVGLTGFEDLPAA----------QLSAGQQRRLALARLWLSRRPLWI 150
|
170
....*....|..
gi 491227761 774 LDEATAFADPES 785
Cdd:TIGR01189 151 LDEPTTALDKAG 162
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
632-848 |
1.55e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 632 HDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDelyakvgfvFQDVQLVAG-------- 703
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------YHQDLLYLGhqpgikte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 -TVRENIALACP---EATDDDVESAARDAQIHERiLRLPNGydtvldtdtQLSGGEKQRLTIARALLADTPILILDEA-T 778
Cdd:PRK13538 89 lTALENLRFYQRlhgPGDDEALWEALAQVGLAGF-EDVPVR---------QLSAGQQRRVALARLWLTRAPLWILDEPfT 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 779 AfadpeseylvqqalgrlIDNRTVLVIAHRLHTIADADQIVVLdhgrvaeTgTHTDLLANNGRYRRLWEG 848
Cdd:PRK13538 159 A-----------------IDKQGVARLEALLAQHAEQGGMVIL-------T-THQDLPVASDKVRKLRLG 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
618-826 |
1.59e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.69 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVT--FGYRPgvpVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDelyakVGFVF 695
Cdd:PRK11247 16 NAVSkrYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVA-GTVRENIALACPEATDDDVESAARDAQIHERILRLPngydtvldtdTQLSGGEKQRLTIARALLADTPILIL 774
Cdd:PRK11247 88 QDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP----------AALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 775 DEATAFADPESEYLVQQALGRLIDNR--TVLVIAHRL-HTIADADQIVVLDHGRV 826
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
631-826 |
1.71e-09 |
|
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: 60.99 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKS-TLASLLARFHDVERGAIRIDGTDIRTLTP-DELYAKVGFVFQD------VQLVA 702
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPaQAIRAGIAMVPEDrkrhgiVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 703 gtVRENIALACPE--ATDDDVESAARDAQIHERILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDEATAF 780
Cdd:TIGR02633 356 --VGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 491227761 781 ADPESEYLVQQALGRLI-DNRTVLVIAHRL-HTIADADQIVVLDHGRV 826
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAqEGVAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
628-845 |
1.72e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.10 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 628 VPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLArfhdverGAIRIDGTDIRTL--TP----DELYAKVGFVF-QDVQL 700
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT-------GILVPTSGEVRVLgyVPfkrrKEFARRIGVVFgQRSQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 701 VAgtvrenialacpeatddDVesAARDA-QIHERILRLPNG-YDTVLDT-----------DT---QLSGGEKQRLTIARA 764
Cdd:COG4586 108 WW-----------------DL--PAIDSfRLLKAIYRIPDAeYKKRLDElvelldlgellDTpvrQLSLGQRMRCELAAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 765 LLADTPILILDEATAFADPESEYLVQQALGRLidNR----TVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLANN 839
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRergtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERF 246
|
....*.
gi 491227761 840 GRYRRL 845
Cdd:COG4586 247 GPYKTI 252
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
635-819 |
2.86e-09 |
|
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: 56.98 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 635 SLTLRHGTVTALVGPSGSGKSTLasllarfhdvergairidgtdirtltpdelyakvgfvFQDVQLVAGtvRENIALACP 714
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTI-------------------------------------LDAIGLALG--GAQSATRRR 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 715 EATDDDVESAARDAqihERILRLPngydtvldtdtQLSGGEKQRLTIARAL----LADTPILILDEATAFADPESEYLVQ 790
Cdd:cd03227 56 SGVKAGCIVAAVSA---ELIFTRL-----------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|
gi 491227761 791 QALGRLIDN-RTVLVIAHRLHTIADADQIV 819
Cdd:cd03227 122 EAILEHLVKgAQVIVITHLPELAELADKLI 151
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
629-778 |
3.75e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP-DELYAKVGFVFQDVQ---LVAG- 703
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLANGIVYISEDRKrdgLVLGm 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALAC----------------PEATDD-----DVESAARDAQIHErilrlpngydtvldtdtqLSGGEKQRLTIA 762
Cdd:PRK10762 346 SVKENMSLTAlryfsraggslkhadeQQAVSDfirlfNIKTPSMEQAIGL------------------LSGGNQQKVAIA 407
|
170
....*....|....*.
gi 491227761 763 RALLADTPILILDEAT 778
Cdd:PRK10762 408 RGLMTRPKVLILDEPT 423
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
308-562 |
7.24e-09 |
|
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: 57.82 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 308 AIITMV-----ELAPFVVLVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLDKLS 382
Cdd:cd18552 4 AILGMIlvaatTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 383 RVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLI--PILVYLLTMMammy 460
Cdd:cd18552 84 RLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVvlPLAALPIRRI---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 461 qsGPKIVEASRWADRMSTESTAYLE----GQPVIRIFGGAA--ASSFKRRLDDYLRFLNdwqrpfigRKTFMDLVTRPTT 534
Cdd:cd18552 160 --GKRLRKISRRSQESMGDLTSVLQetlsGIRVVKAFGAEDyeIKRFRKANERLRRLSM--------KIARARALSSPLM 229
|
250 260 270
....*....|....*....|....*....|....
gi 491227761 535 -FLWLIATAGTLF-----VVSGAMQPVTLLPFLV 562
Cdd:cd18552 230 eLLGAIAIALVLWyggyqVISGELTPGEFISFIT 263
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
630-825 |
1.35e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTL----ASLLARFHDVERGAIRIDGtdirtLTPDELY----AKVGFVFQ-DVQL 700
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDG-----ITPEEIKkhyrGDVVYNAEtDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 701 VAGTVRENI--ALAC------PEATDDDvESAARDAQIHERILRLPNGYDTVLDTD--TQLSGGEKQRLTIARALLADTP 770
Cdd:TIGR00956 151 PHLTVGETLdfAARCktpqnrPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNDfvRGVSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 771 ILILDEATAFADPESEYLVQQALgrlidnRTVLVIAHRLHTIA------DA----DQIVVLDHGR 825
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRAL------KTSANILDTTPLVAiyqcsqDAyelfDKVIVLYEGY 288
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
300-459 |
1.69e-08 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 56.67 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 300 MIAGGVLQAIITMVELA-PFvvlveLTRQLL-AGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRL 377
Cdd:cd18551 1 LILALLLSLLGTAASLAqPL-----LVKNLIdALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 378 LDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMMA 457
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
|
..
gi 491227761 458 MM 459
Cdd:cd18551 156 LG 157
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
631-807 |
1.89e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 55.31 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVS-LTLRHGtVTALVGPSGSGKSTL--ASLLARFHDVERGAIRIDGTD--IRTltpdelyakvgfvfqdvqlvaGTV 705
Cdd:cd03240 12 FHERSeIEFFSP-LTLIVGQNGAGKTTIieALKYALTGELPPNSKGGAHDPklIRE---------------------GEV 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIALACPEATDDDVEsAARDAQIHERILRLPNG--YDTVLDTDTQLSGGEKQ------RLTIARALLADTPILILDEA 777
Cdd:cd03240 70 RAQVKLAFENANGKKYT-ITRSLAILENVIFCHQGesNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEP 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 491227761 778 TAFADPESeylVQQALGRLID------NRTVLVIAH 807
Cdd:cd03240 149 TTNLDEEN---IEESLAEIIEerksqkNFQLIVITH 181
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
625-826 |
2.05e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.35 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 625 RPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDverGAIRIDGtDIR--TLTPDELYAK----VGFVFQ-D 697
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEG-DIHynGIPYKEFAEKypgeIIYVSEeD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 698 VQLVAGTVRENIALACpeatdddvesaarDAQIHErILRlpngydtvldtdtQLSGGEKQRLTIARALLADTPILILDEA 777
Cdd:cd03233 93 VHFPTLTVRETLDFAL-------------RCKGNE-FVR-------------GISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 778 TafadpeseylvqqalgRLIDNRTVLVIAHRLHTIADA--------------------DQIVVLDHGRV 826
Cdd:cd03233 146 T----------------RGLDSSTALEILKCIRTMADVlktttfvslyqasdeiydlfDKVLVLYEGRQ 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
630-808 |
2.07e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 58.32 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLASLLA--RFHDVERGAIRIDGTDIRtltpDELYAKV-GFVFQ-DVQLVAGTV 705
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKK----QETFARIsGYCEQnDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIA----LACPEATDDDVESAARDaQIHErILRLPNGYDTV--LDTDTQLSGGEKQRLTIARALLADTPILILDEATA 779
Cdd:PLN03140 971 RESLIysafLRLPKEVSKEEKMMFVD-EVME-LVELDNLKDAIvgLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190
....*....|....*....|....*....|
gi 491227761 780 FADPESEYLVQQALGRLIDN-RTVLVIAHR 808
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTgRTVVCTIHQ 1078
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
639-821 |
3.34e-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: 3.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 639 RHGTVTALVGPSGSGKSTLASLLA--------RFHDVE--RGAIR-IDGTDIRT----LTPDELYA--KVGFVFQDVQLV 701
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPdwDEILDeFRGSELQNyftkLLEGDVKVivKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 702 AGTVRENIalacpEATDDDvesaardAQIHERILRLpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDEATAF 780
Cdd:cd03236 104 KGKVGELL-----KKKDER-------GKLDELVDQL--ELRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 491227761 781 ADPESEYLVQQALGRLI-DNRTVLVIAHRLhTIAD--ADQIVVL 821
Cdd:cd03236 170 LDIKQRLNAARLIRELAeDDNYVLVVEHDL-AVLDylSDYIHCL 212
|
|
| FNR_like |
cd00322 |
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ... |
23-198 |
1.44e-07 |
|
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).
Pssm-ID: 99778 [Multi-domain] Cd Length: 223 Bit Score: 53.22 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 23 VGTAPVAPNCVRITMSAPTLFEdllHTPAEWLRFWFPDPDGGTSehqRAYTIVTTDEDAGEFSIDVVIHePAGPACQWAV 102
Cdd:cd00322 1 VATEDVTDDVRLFRLQLPNGFS---FKPGQYVDLHLPGDGRGLR---RAYSIASSPDEEGELELTVKIV-PGGPFSAWLH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 103 AAQPGMTIPVVAFGSaRFEVPADLPSGFLLIGDSASIPAINSIVAALPAEVDIE----VYLERHSPD----DELIPL-TT 173
Cdd:cd00322 74 DLKPGDEVEVSGPGG-DFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGeitlLYGARTPADllflDELEELaKE 152
|
170 180
....*....|....*....|....*.
gi 491227761 174 HPRRRLHWV-DRIDETSLAAAIEGRD 198
Cdd:cd00322 153 GPNFRLVLAlSRESEAKLGPGGRIDR 178
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
634-835 |
1.45e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 634 VSLTLRHGTVTALVGPSGSGKS--TLA--SLLARFHDVERGAIRIDGTDIRTLTPDE----LYAKVGFVFQDVQLVAG-- 703
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvsSLAimGLIDYPGRVMAEKLEFNGQDLQRISEKErrnlVGAEVAMIFQDPMTSLNpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 -TVRENIALACpeatddDVESAARDAQIHERILRL------PNGYDTVLDTDTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:PRK11022 106 yTVGFQIMEAI------KVHQGGNKKTRRQRAIDLlnqvgiPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491227761 777 ATAFADPESEYLVQQALGRLI--DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVAETGTHTDL 835
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
633-821 |
1.47e-07 |
|
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: 55.40 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTL---------ASLL-------ARFHDVErGA------IRIDG-------------- 676
Cdd:TIGR00630 626 NITVSIPLGLFTCITGVSGSGKSTLindtlypalANRLngaktvpGRYTSIE-GLehldkvIHIDQspigrtprsnpaty 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 677 ----TDIRTL---TPDEL---YAKVGFVFQ-----------------------------DVQLVAGTVRE---------N 708
Cdd:TIGR00630 705 tgvfDEIRELfaeTPEAKvrgYTPGRFSFNvkggrceacqgdgvikiemhflpdvyvpcEVCKGKRYNREtlevkykgkN 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 709 IA----LACPEATD--DDVESAARDAQIherILRLPNGYDTVLDTDTQLSGGEKQRLTIARALLA-DT--PILILDEATA 779
Cdd:TIGR00630 785 IAdvldMTVEEAYEffEAVPSISRKLQT---LCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKrSTgrTLYILDEPTT 861
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 491227761 780 ---FADpeseylVQQ---ALGRLIDN-RTVLVIAHRLHTIADADQIVVL 821
Cdd:TIGR00630 862 glhFDD------IKKlleVLQRLVDKgNTVVVIEHNLDVIKTADYIIDL 904
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
631-834 |
2.74e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.02 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP-DELYAKVGFVFQDVQ----LVAGTV 705
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITESRRdngfFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIALAcPEATDDDVESA---------ARDAQIHERILRLPNGydTVLDTDTQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:PRK09700 359 AQNMAIS-RSLKDGGYKGAmglfhevdeQRTAENQRELLALKCH--SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 777 ATAFADPESEYLVQQALGRLIDN-RTVLVIAHRL-HTIADADQIVVLDHGRVAETGTHTD 834
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
626-825 |
3.02e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 626 PGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE-LYAKVGFVFQDVQLVAG- 703
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 TVRENIALACPEATDDDVEsaardaqiHERILRLPNGYDTVLDTD-------TQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:PRK10982 89 SVMDNMWLGRYPTKGMFVD--------QDKMYRDTKAIFDELDIDidprakvATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 491227761 777 AT-AFADPESEYLVQqaLGRLIDNR--TVLVIAHRLHTIAD-ADQIVVLDHGR 825
Cdd:PRK10982 161 PTsSLTEKEVNHLFT--IIRKLKERgcGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
631-824 |
3.14e-07 |
|
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: 51.17 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 631 IHDVSLTLRHGTVTALVGPSGSGKSTLAS-LLArfhdvERGAIRIDGTDirtltpdELYAKVGFVFQDvQLvagtvreni 709
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLY-----ASGKARLISFL-------PKFSRNKLIFID-QL--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 710 alacpeatdddvesaardaqihERILRLPNGYDTvLDTDTQ-LSGGEKQRLTIARALLADTP--ILILDEATAFADPESE 786
Cdd:cd03238 69 ----------------------QFLIDVGLGYLT-LGQKLStLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*....
gi 491227761 787 YLVQQALGRLID-NRTVLVIAHRLHTIADADQIVVLDHG 824
Cdd:cd03238 126 NQLLEVIKGLIDlGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
615-840 |
4.12e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 615 VSFEGVTFGYRPGvPVIHDVSLTLRHGTVTALVGPSGSGKSTLasllarfhdvergairidgtdIRTLtpdelyakVGfv 694
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTL---------------------LRTL--------VG-- 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 fqDVQLVAGTVR--ENIALA-CPEATDDDVE-------------SAARDAQIHERIL-RLPNGYDTVLDTDTQLSGGEKQ 757
Cdd:PRK15064 368 --ELEPDSGTVKwsENANIGyYAQDHAYDFEndltlfdwmsqwrQEGDDEQAVRGTLgRLLFSQDDIKKSVKVLSGGEKG 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 758 RLTIARALLADTPILILDEATAFADPESEYLVQQAL----GRLI----DNRTVLVIAHRLhtiadadqIVVLDHGRVAET 829
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALekyeGTLIfvshDREFVSSLATRI--------IEITPDGVVDFS 517
|
250
....*....|.
gi 491227761 830 GTHTDLLANNG 840
Cdd:PRK15064 518 GTYEEYLRSQG 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
622-834 |
6.23e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.99 E-value: 6.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 622 FGYRP--------------GVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTP-DE 686
Cdd:PRK11288 246 YGYRPrplgevrlrldglkGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 687 LYAKVGFVFQDVQ---LVAG-TVRENIALACPEAT-------DDDVESAARDAQIHERILRLPNGydtvlDTDT-QLSGG 754
Cdd:PRK11288 326 IRAGIMLCPEDRKaegIIPVhSVADNINISARRHHlragcliNNRWEAENADRFIRSLNIKTPSR-----EQLImNLSGG 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 755 EKQRLTIARALLADTPILILDEATAFAD--PESE-YLVQQALGRliDNRTVLVIAHRL-HTIADADQIVVLDHGRVAETG 830
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHEiYNVIYELAA--QGVAVLFVSSDLpEVLGVADRIVVMREGRIAGEL 478
|
....
gi 491227761 831 THTD 834
Cdd:PRK11288 479 AREQ 482
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
738-822 |
7.62e-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: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 738 PNGYDTVLDTDT--------QLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLIDN--RTVLVIAH 807
Cdd:cd03222 51 PNGDNDEWDGITpvykpqyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEH 130
|
90
....*....|....*..
gi 491227761 808 RLhTIAD--ADQIVVLD 822
Cdd:cd03222 131 DL-AVLDylSDRIHVFE 146
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
630-778 |
8.40e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 630 VIHDVSLTLRHGTVTALVGPSGSGKSTLA-SLLARFHDV-ERGAIRIDGTDIRTLT-PDELYAKVGFVFQDVQ---LVAG 703
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTvSDAIDAGLAYVTEDRKgygLNLI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 704 -TVRENIALA-CPEATDDDVESAARDAQIHERI-----LRLPNGYDTVLdtdtQLSGGEKQRLTIARALLADTPILILDE 776
Cdd:NF040905 355 dDIKRNITLAnLGKVSRRGVIDENEEIKVAEEYrkkmnIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
..
gi 491227761 777 AT 778
Cdd:NF040905 431 PT 432
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
635-837 |
8.42e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 8.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 635 SLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFVFQdvqlvagtvRENIALACP 714
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQ---------RNNTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 715 EATD----------DDVESAARDAQIHERIlrlpnGYDTVLDTD-TQLSGGEKQRLTIARALLADTPILILDEATAFADP 783
Cdd:PRK10938 94 GEDDtgrttaeiiqDEVKDPARCEQLAQQF-----GITALLDRRfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 491227761 784 ESEYLVQQALGRLIDNRTVLV-IAHRLHTIAD-ADQIVVLDHGRVAETGTHTDLLA 837
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
641-807 |
1.55e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 641 GTVTALVGPSGSGKSTLASLLArfhdvER--GAIRIDGTDIRTLTP-DELYAK-VGFVFQ-DVQLVAGTVRENIALACPE 715
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLA-----ERvtTGVITGGDRLVNGRPlDSSFQRsIGYVQQqDLHLPTSTVRESLRFSAYL 863
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 716 ATDDDVESAARDAQIHE--RILRLPNGYDTVLDTDTQ-LSGGEKQRLTIARALLADTPILI-LDEATAFADPESEYLVQQ 791
Cdd:TIGR00956 864 RQPKSVSKSEKMEYVEEviKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICK 943
|
170
....*....|....*..
gi 491227761 792 ALGRLIDN-RTVLVIAH 807
Cdd:TIGR00956 944 LMRKLADHgQAILCTIH 960
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
749-819 |
2.45e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 51.57 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 749 TQLSGGEKQRLTIARALL-ADTP--ILILDEATA---FADpeseylVQQ---ALGRLIDN-RTVLVIAHRLHTIADADQI 818
Cdd:COG0178 825 TTLSGGEAQRVKLASELSkRSTGktLYILDEPTTglhFHD------IRKlleVLHRLVDKgNTVVVIEHNLDVIKTADWI 898
|
.
gi 491227761 819 V 819
Cdd:COG0178 899 I 899
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
300-591 |
2.95e-06 |
|
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: 50.09 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 300 MIAGGVLQAIITMVeLAPFVVLVELTRQLLAGADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLD 379
Cdd:cd18547 8 AIISTLLSVLGPYL-LGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 380 KLSRVPLGWFTQRGSGSV-KKLIQD-DTMSLhyLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMMA 457
Cdd:cd18547 87 KLQRLPLSYFDTHSHGDImSRVTNDvDNISQ--ALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 458 MMYQSGPKIVEASRWADRMstesTAYLE----GQPVIRIFGG--AAASSFKRRLDDYLRflndwqrpfIGRK-TFMDLVT 530
Cdd:cd18547 165 IAKRSQKYFRKQQKALGEL----NGYIEemisGQKVVKAFNReeEAIEEFDEINEELYK---------ASFKaQFYSGLL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491227761 531 RPTTFLW------LIATAGTLFVVSGAMQPVTLLPFLVLGTTFGARLLGIAYGLGSIRGGLESARHI 591
Cdd:cd18547 232 MPIMNFInnlgyvLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
619-793 |
4.04e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 619 GVTFGyRPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKVGFV---F 695
Cdd:PRK13543 16 ALAFS-RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLpglK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 696 QDVQLVagtvrENIALACPEATdddvESAARDAQIHERILRLPNGYDTVLdtdTQLSGGEKQRLTIARALLADTPILILD 775
Cdd:PRK13543 95 ADLSTL-----ENLHFLCGLHG----RRAKQMPGSALAIVGLAGYEDTLV---RQLSAGQKKRLALARLWLSPAPLWLLD 162
|
170
....*....|....*...
gi 491227761 776 EATAFADPESEYLVQQAL 793
Cdd:PRK13543 163 EPYANLDLEGITLVNRMI 180
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
629-817 |
7.03e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 7.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFH------DV-----ERGAiridGT---DIRTltpdelyaKVGFV 694
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysnDLtlfgrRRGS----GEtiwDIKK--------HIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 695 FQDVQL---VAGTVReNIALacpeatdddveSAARDA-----QIHERILRLPNGYDTVLDTDTQ--------LSGGEkQR 758
Cdd:PRK10938 342 SSSLHLdyrVSTSVR-NVIL-----------SGFFDSigiyqAVSDRQQKLAQQWLDILGIDKRtadapfhsLSWGQ-QR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491227761 759 LT-IARALLADTPILILDEATAFADPESEYLVQQALGRLIDN-RTVLV------------IAHRLHTIADADQ 817
Cdd:PRK10938 409 LAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFVPDGDI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
618-807 |
7.11e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 618 EGVTFGYrPGVPVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIdGTDIR---------TLTPDEly 688
Cdd:PRK11147 323 ENVNYQI-DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvayfdqhraELDPEK-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 689 akvgfvfqdvqlvagTVRENIALACPEAT----DDDVESAARDAQIHERILRLPngydtVldtdTQLSGGEKQRLTIARA 764
Cdd:PRK11147 399 ---------------TVMDNLAEGKQEVMvngrPRHVLGYLQDFLFHPKRAMTP-----V----KALSGGERNRLLLARL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 491227761 765 LLADTPILILDEATAFADPESEYLvqqaLGRLIDNR--TVLVIAH 807
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVETLEL----LEELLDSYqgTVLLVSH 495
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
305-504 |
1.39e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 47.66 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 305 VLQAIITMVELAPFVVLVELTRQLLAGADEAQLrhtgFVFLVLLVLGATLGMALTLWLHVVDLRFSADV----RRRLLDK 380
Cdd:cd18561 3 LLGLLITALYIAQAWLLARALARIFAGGPWEDI----MPPLAGIAGVIVLRAALLWLRERVAHRAAQRVkqhlRRRLFAK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 381 LSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLIPILVYLLTMmaMMY 460
Cdd:cd18561 79 LLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSP--ALW 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 491227761 461 QSGPKIVEASRWA--DRMSTESTAYLEGQPVIRIFGgaaASSFKRR 504
Cdd:cd18561 157 DRLAKDTGRRHWAayGRLSAQFLDSLQGMTTLKAFG---ASKRRGN 199
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
342-450 |
1.96e-05 |
|
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: 47.56 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 342 FVFLVLLVLGATLGMALTLWLHVVDLRFSA-----DVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSI 416
Cdd:cd18565 53 LWLLGGLTVAAFLLESLFQYLSGVLWRRFAqrvqhDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGA 132
|
90 100 110
....*....|....*....|....*....|....
gi 491227761 417 PDAVAAVVGPVAVLVYLFVIEWRMALILLIPILV 450
Cdd:cd18565 133 NSIIRVVVTVLGIGAILFYLNWQLALVALLPVPL 166
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
315-561 |
2.62e-05 |
|
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: 47.00 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 315 LAPFVVLVELTRQLLAG-----------ADEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLDKLSR 383
Cdd:cd18544 7 LLLLATALELLGPLLIKraiddyivpgqGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 384 VPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILL--IPILVYLltmmAMMYQ 461
Cdd:cd18544 87 LPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLlvLPLLLLA----TYLFR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 462 SgpKIVEASRWADRMSTESTAYL----EGQPVIRIFG--GAAASSFKRRLDDYLRFLNdwqrpfigRKTFMDLVTRPTT- 534
Cdd:cd18544 163 K--KSRKAYREVREKLSRLNAFLqesiSGMSVIQLFNreKREFEEFDEINQEYRKANL--------KSIKLFALFRPLVe 232
|
250 260 270
....*....|....*....|....*....|..
gi 491227761 535 FLWLIATAGTLF-----VVSGAMQPVTLLPFL 561
Cdd:cd18544 233 LLSSLALALVLWygggqVLSGAVTLGVLYAFI 264
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
633-827 |
3.61e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDELYAKvGFVF--QDVQlVAG-----TV 705
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-GLVYlpEDRQ-SSGlyldaPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIalaCPEATDDD--VESAARDAQIHERILRLPN----GYDTVLDTdtqLSGGEKQRLTIARALLADTPILILDEATA 779
Cdd:PRK15439 359 AWNV---CALTHNRRgfWIKPARENAVLERYRRALNikfnHAEQAART---LSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 491227761 780 FADPESEYLVQQALGRLI-DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVA 827
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAaQNVAVLFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
299-561 |
4.24e-05 |
|
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: 46.31 E-value: 4.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 299 QMIAGGVLQAIITMVELA-PFVVLVELTRQLLAGaDEAQLRHTGFVFLVLLVLGATLGMALTLWLHVVDLRFSADVRRRL 377
Cdd:cd18545 1 KLLLALLLMLLSTAASLAgPYLIKIAIDEYIPNG-DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 378 LDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILLI--PILVYLLTM 455
Cdd:cd18545 80 FSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAvlPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 456 MammyqsGPKIVEASRWADRMSTESTAYLE----GQPVIRIFG--GAAASSFKRRLDDYLR------FLNDWQRPFIGrk 523
Cdd:cd18545 160 L------RRRARKAWQRVRKKISNLNAYLHesisGIRVIQSFAreDENEEIFDELNRENRKanmravRLNALFWPLVE-- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 491227761 524 tfmdlvtrpttFLWLIATA-----GTLFVVSGAMQPVTLLPFL 561
Cdd:cd18545 232 -----------LISALGTAlvywyGGKLVLGGAITVGVLVAFI 263
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
646-690 |
4.74e-05 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 45.05 E-value: 4.74e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491227761 646 LVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPD--ELYAK 690
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHPHyrELQAA 62
|
|
| RecA-like_ClpX |
cd19497 |
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ... |
646-726 |
9.41e-05 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410905 [Multi-domain] Cd Length: 251 Bit Score: 44.90 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 646 LVGPSGSGKSTLASLLARFHDVERgAIridgTDIRTLTpdelyaKVGFVFQDVqlvagtvrENIALACPEATDDDVESAA 725
Cdd:cd19497 55 LIGPTGSGKTLLAQTLAKILDVPF-AI----ADATTLT------EAGYVGEDV--------ENILLKLLQAADYDVERAQ 115
|
.
gi 491227761 726 R 726
Cdd:cd19497 116 R 116
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
629-809 |
9.53e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.55 E-value: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTlTPDELYAKVGFVFQ-DV--QLVAGtv 705
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfDAidDLLTG-- 2029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 706 RENIALACpEATDDDVESAARDAQIHERILRLPNGYDTVLDTdtqLSGGEKQRLTIARALLADTPILILDEATAFADPES 785
Cdd:TIGR01257 2030 REHLYLYA-RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180
....*....|....*....|....*
gi 491227761 786 EYLVQQALGRLI-DNRTVLVIAHRL 809
Cdd:TIGR01257 2106 RRMLWNTIVSIIrEGRAVVLTSHSM 2130
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
749-819 |
9.70e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 749 TQLSGGEKQRLTIARALLA-DT--PILILDEATA---FADpeseylVQQ---ALGRLIDN-RTVLVIAHRLHTIADADQI 818
Cdd:PRK00349 829 TTLSGGEAQRVKLAKELSKrSTgkTLYILDEPTTglhFED------IRKlleVLHRLVDKgNTVVVIEHNLDVIKTADWI 902
|
.
gi 491227761 819 V 819
Cdd:PRK00349 903 I 903
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
297-486 |
1.18e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 44.78 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 297 KKQMIAGGVLQAIITMVElapfVVLVELTRQLLagaDEAQLRHT--GFVFLVLLVLGATLGMALTLWL-----HVVDLRF 369
Cdd:cd18540 1 KKLLILLIILMLLVALLD----AVFPLLTKYAI---DHFITPGTldGLTGFILLYLGLILIQALSVFLfirlaGKIEMGV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 370 SADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVVGPVAVLVYLFVIEWRMALILL--IP 447
Cdd:cd18540 74 SYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLavVP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 491227761 448 ILVYLltmmAMMYQSgpKIVEASRWADRMSTEST-AYLEG 486
Cdd:cd18540 154 VLAVV----SIYFQK--KILKAYRKVRKINSRITgAFNEG 187
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
751-837 |
1.51e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.66 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 751 LSGGEKQ------RLTIARALLADTPILILDEATAFADPeseylvqqalgrliDNRTVL--VIAHRLHTIADADQIVVLD 822
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDE--------------DRRTNLkdIIEYSLKDSSDIPQVIMIS 867
|
90
....*....|....*
gi 491227761 823 HgrvaetgtHTDLLA 837
Cdd:PRK01156 868 H--------HRELLS 874
|
|
| clpX |
PRK05342 |
ATP-dependent Clp protease ATP-binding subunit ClpX; |
646-726 |
3.56e-04 |
|
ATP-dependent Clp protease ATP-binding subunit ClpX;
Pssm-ID: 235422 [Multi-domain] Cd Length: 412 Bit Score: 43.99 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 646 LVGPSGSGKSTLASLLARFHDVERgAIrIDGTdirTLTpdelyaKVGFVFQDVqlvagtvrENIALACPEATDDDVESAA 725
Cdd:PRK05342 113 LIGPTGSGKTLLAQTLARILDVPF-AI-ADAT---TLT------EAGYVGEDV--------ENILLKLLQAADYDVEKAQ 173
|
.
gi 491227761 726 R 726
Cdd:PRK05342 174 R 174
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
633-819 |
5.57e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 42.24 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 633 DVSLTLRHGTVTALVGPSGSGKSTLA----------------SLLARFH-------DVER-----GAIRIDGTDIR---- 680
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslSAYARQFlgqmdkpDVDSieglsPAIAIDQKTTSrnpr 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 681 ----TLTpdELYAKVGFVFqdvqlvagtvrenialacpeatdddvesaARDAqIHERILRLPN---GYDTVLDTDTQLSG 753
Cdd:cd03270 93 stvgTVT--EIYDYLRLLF-----------------------------ARVG-IRERLGFLVDvglGYLTLSRSAPTLSG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491227761 754 GEKQRLTIARALLAD-TPIL-ILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIADADQIV 819
Cdd:cd03270 141 GEAQRIRLATQIGSGlTGVLyVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
629-827 |
5.89e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 629 PVIHDVSLTLRHGTVTALVGPSGSGKSTLASLLARFHDVERGAIRIDGTDIRTLTPDE-----------------LYAKV 691
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalvteerrstgIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 692 GFVFQDVQLVAGTVRENIALAcpeaTDDDVESaarDAQ--IHERILRLPnGYDTVLDTdtqLSGGEKQRLTIARALLADT 769
Cdd:PRK10982 342 DIGFNSLISNIRNYKNKVGLL----DNSRMKS---DTQwvIDSMRVKTP-GHRTQIGS---LSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 770 PILILDEATAFADPESEYLVQQALGRLI-DNRTVLVIAHRL-HTIADADQIVVLDHGRVA 827
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITDRILVMSNGLVA 470
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
751-821 |
8.94e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 8.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491227761 751 LSGGEKQRLTIARALLADTP---ILILDEATAFADPESEYLVQQALGRLID-NRTVLVIAHRLHTIADADQIVVL 821
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHqGHTVVIIEHNMHVVKVADYVLEL 884
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
646-694 |
9.51e-04 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 41.23 E-value: 9.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 646 LVGPSGSGKSTLASLLA-RFHDVERGAIRIDGTDIRT-LTPD---------ELYAKVGFV 694
Cdd:COG0529 21 FTGLSGSGKSTLANALErRLFERGRHVYLLDGDNVRHgLNKDlgfskedrdENIRRIGEV 80
|
|
| APS_kinase |
pfam01583 |
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ... |
641-693 |
1.29e-03 |
|
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.
Pssm-ID: 396247 [Multi-domain] Cd Length: 154 Bit Score: 40.38 E-value: 1.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 491227761 641 GTVTALVGPSGSGKSTLASLLAR-FHDVERGAIRIDGTDIRTltpdELYAKVGF 693
Cdd:pfam01583 2 GCTIWLTGLSGAGKSTIANALERkLFEQGRSVYVLDGDNVRH----GLNKDLGF 51
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
750-852 |
1.87e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 750 QLSGGEKQRLTIARALLADTPILILDEATAFADPESEYLVQQALGRLI-DNRTVLVIAHRLHTIAD-ADQIVVLDHGRVA 827
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVrDGATVLLTTQYMEEAEQlAHELTVIDRGRVI 223
|
90 100
....*....|....*....|....*.
gi 491227761 828 ETGTHTDLLAN-NGRYRRLWEGHRHE 852
Cdd:NF000106 224 ADGKVDELKTKvGGRTLQIRPAHAAE 249
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
345-452 |
2.30e-03 |
|
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: 40.93 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 345 LVLLVLGATLGMALTLWLHVVDLRFSADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDDTMSLHYLITHSIPDAVAAVV 424
Cdd:cd18550 46 VAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV 125
|
90 100 110
....*....|....*....|....*....|
gi 491227761 425 GPVAVLVYLFVIEWRMALI--LLIPILVYL 452
Cdd:cd18550 126 TLVATLVAMLALDWRLALLslVLLPLFVLP 155
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
605-663 |
2.35e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 41.47 E-value: 2.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 605 APVTADAVAS-VSFEGVTFGYRPGV---------PVIHD--VSLTLRHGTVtalVGPSGSGKSTLASLLAR 663
Cdd:COG3451 159 RLLTTSNLAAlFPFHSFELGDPWGIyllntrsgtPVFFDfhDGLDNGNTLI---LGPSGSGKSFLLKLLLL 226
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
336-510 |
2.77e-03 |
|
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: 40.47 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 336 QLRHTGFVFLVLLVLGATLGMALT--LW---LHVVDLRFSADVRRRLLDKLSRVPLGWFTQRGSGSVKKLIQDD----TM 406
Cdd:cd18541 33 TLTASQLLRYALLILLLALLIGIFrfLWrylIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDlnavRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 407 SLHYLITHSIpdavAAVVGPVAVLVYLFVIEWRMALILLIPILVylltMMAMMYQSGPKIVEASRWA----DRMSTESTA 482
Cdd:cd18541 113 ALGPGILYLV----DALFLGVLVLVMMFTISPKLTLIALLPLPL----LALLVYRLGKKIHKRFRKVqeafSDLSDRVQE 184
|
170 180 190
....*....|....*....|....*....|
gi 491227761 483 YLEGQPVIRIFG--GAAASSFKRRLDDYLR 510
Cdd:cd18541 185 SFSGIRVIKAFVqeEAEIERFDKLNEEYVE 214
|
|
| AAA_5 |
pfam07728 |
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ... |
646-740 |
3.41e-03 |
|
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.
Pssm-ID: 400191 [Multi-domain] Cd Length: 135 Bit Score: 38.43 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 646 LVGPSGSGKSTLASLLARfhdvergaiRIDGTDIRT------LTPDEL-----YAKVGFVFQDVQLVAGTVRENIALacp 714
Cdd:pfam07728 4 LVGPPGTGKTELAERLAA---------ALSNRPVFYvqltrdTTEEDLfgrrnIDPGGASWVDGPLVRAAREGEIAV--- 71
|
90 100 110
....*....|....*....|....*....|..
gi 491227761 715 eatDDDVESAARDAQ------IHERILRLPNG 740
Cdd:pfam07728 72 ---LDEINRANPDVLnsllslLDERRLLLPDG 100
|
|
| ClpX |
COG1219 |
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ... |
646-726 |
3.63e-03 |
|
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440832 [Multi-domain] Cd Length: 409 Bit Score: 40.80 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 646 LVGPSGSGKSTLASLLARFHDVERgAIrIDGTdirTLTpdElyAkvGFVFQDVqlvagtvrENIALACPEATDDDVESAA 725
Cdd:COG1219 114 LIGPTGSGKTLLAQTLARILDVPF-AI-ADAT---TLT--E--A--GYVGEDV--------ENILLKLLQAADYDVEKAE 174
|
.
gi 491227761 726 R 726
Cdd:COG1219 175 R 175
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
432-567 |
3.80e-03 |
|
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: 40.12 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 432 YLFVIEWRMALILLIPILVYLLTMMAMMyqsgPKIVEASRwaDRM--STESTAYL----EGQPVIRIFGgaAASSFKRRL 505
Cdd:cd18570 135 ILFFYNWKLFLITLLIIPLYILIILLFN----KPFKKKNR--EVMesNAELNSYLieslKGIETIKSLN--AEEQFLKKI 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491227761 506 DD-YLRFLND---------WQRpfigrkTFMDLVTR--PTTFLWLiataGTLFVVSGAMQPVTLLPFLVLGTTF 567
Cdd:cd18570 207 EKkFSKLLKKsfklgklsnLQS------SIKGLISLigSLLILWI----GSYLVIKGQLSLGQLIAFNALLGYF 270
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
726-839 |
5.02e-03 |
|
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: 40.77 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 726 RDAQIHERIL-----RLPNGYDTVLD------TDTQLSGGEKQRLTIARALLAD-TPIL-ILDEatafadPeSEYLVQQA 792
Cdd:TIGR00630 453 EEKKIAEEVLkeireRLGFLIDVGLDylslsrAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDE------P-SIGLHQRD 525
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491227761 793 LGRLIDN--------RTVLVIAHRLHTIADADQIVVL-----DH-GRVAETGTHTDLLANN 839
Cdd:TIGR00630 526 NRRLINTlkrlrdlgNTLIVVEHDEDTIRAADYVIDIgpgagEHgGEVVASGTPEEILANP 586
|
|
| apsK |
TIGR00455 |
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion ... |
641-685 |
6.42e-03 |
|
adenylyl-sulfate kinase; This protein, adenylylsulfate kinase, is often found as a fusion protein with sulfate adenylyltransferase. Important residue (active site in E.coli) is residue 100 of the seed alignment. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 129547 Cd Length: 184 Bit Score: 38.60 E-value: 6.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 491227761 641 GTVTALVGPSGSGKSTLASLLAR-FHDVERGAIRIDGTDIRT-LTPD 685
Cdd:TIGR00455 18 GVVIWLTGLSGSGKSTIANALEKkLESKGYRVYVLDGDNVRHgLNKD 64
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
648-681 |
6.96e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 37.85 E-value: 6.96e-03
10 20 30
....*....|....*....|....*....|....
gi 491227761 648 GPSGSGKSTLASLLARfhdvERGAIRIDGTDIRT 681
Cdd:cd02020 6 GPAGSGKSTVAKLLAK----KLGLPYLDTGGIRT 35
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
643-686 |
7.05e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 37.67 E-value: 7.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 491227761 643 VTALVGPSGSGKSTLASLLARfhdvERGAIRIDGTDIR-TLTPDE 686
Cdd:pfam13671 1 LILLVGLPGSGKSTLARRLLE----ELGAVRLSSDDERkRLFGEG 41
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
632-657 |
8.66e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 35.27 E-value: 8.66e-03
10 20
....*....|....*....|....*.
gi 491227761 632 HDVSLTLRHGTVTALVGPSGSGKSTL 657
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTL 38
|
|
| AAA |
pfam00004 |
ATPase family associated with various cellular activities (AAA); AAA family proteins often ... |
646-705 |
9.06e-03 |
|
ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.
Pssm-ID: 459627 [Multi-domain] Cd Length: 130 Bit Score: 37.19 E-value: 9.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491227761 646 LVGPSGSGKSTLASLLARFHDVErgAIRIDGTDIRTLTPDELYAKVGFVFQDVQLVAGTV 705
Cdd:pfam00004 3 LYGPPGTGKTTLAKAVAKELGAP--FIEISGSELVSKYVGESEKRLRELFEAAKKLAPCV 60
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
643-675 |
9.67e-03 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 37.97 E-value: 9.67e-03
10 20 30
....*....|....*....|....*....|...
gi 491227761 643 VTALVGPSGSGKSTLASLLARfhdvERGAIRID 675
Cdd:COG0645 1 LILVCGLPGSGKSTLARALAE----RLGAVRLR 29
|
|
| |
