|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
62-625 |
1.80e-171 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 513.17 E-value: 1.80e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 62 LMILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTntTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSL 141
Cdd:COG1132 22 LLILALLLLLLSALLELLLPLLLGRIIDALLAGGD--LSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 142 YLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAG 221
Cdd:COG1132 100 LFEHLLRLPLSFFD-RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 222 ALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCS 301
Cdd:COG1132 179 RLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 302 YALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETIERRPNIDSySTNGKVLDDIK 381
Cdd:COG1132 259 LALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:COG1132 338 GEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:COG1132 416 IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDP 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIRL 621
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRL 574
|
....
gi 1063707070 622 QEEK 625
Cdd:COG1132 575 QFGE 578
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
384-622 |
4.20e-141 |
|
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: 421.18 E-value: 4.20e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKdPEGAYSQLIRLQ 622
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
112-622 |
6.78e-134 |
|
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: 415.64 E-value: 6.78e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 112 LGIGTFAAAFLQLSgwmiSGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLAT 191
Cdd:TIGR02204 71 LALGTAARFYLVTW----LGERVVADIRRAVFAHLISLSPSFFD-KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALM 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 192 FVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNK 271
Cdd:TIGR02204 146 CIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 272 HLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQ 351
Cdd:TIGR02204 226 AVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 352 AAAYKMFETIERRPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSL 431
Cdd:TIGR02204 306 GAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 432 IERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQG 511
Cdd:TIGR02204 386 LLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEG 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 512 LDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIA 591
Cdd:TIGR02204 466 YDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIV 545
|
490 500 510
....*....|....*....|....*....|.
gi 1063707070 592 VIHQGKIVEKGSHTELLKDpEGAYSQLIRLQ 622
Cdd:TIGR02204 546 VMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
110-622 |
1.59e-127 |
|
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: 403.45 E-value: 1.59e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 110 VWLGIGTFAAAFLQ-----LSGWMIS--GERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSgDTVLIQDAM-GEK 181
Cdd:COG2274 196 WVLAIGLLLALLFEgllrlLRSYLLLrlGQRIDLRLSSRFFRHLLRLPLSFFE-SRSVGDLASRFR-DVESIREFLtGSL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 182 VGKAIQLLATFVGGFVIAFVrGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTG 261
Cdd:COG2274 274 LTALLDLLFVLIFLIVLFFY-SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGA 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 262 EKQAISNYNKHLVTAYKAGV-IEGGSTGLGLGTLFLVVFcSYALAVWYGGKLILDKGYTGGQVL--NIIIAVLTGSM-SL 337
Cdd:COG2274 353 ESRFRRRWENLLAKYLNARFkLRRLSNLLSTLSGLLQQL-ATVALLWLGAYLVIDGQLTLGQLIafNILSGRFLAPVaQL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 338 GQtspcLSAFAAGQAAAYKMFETIERRPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVAL 417
Cdd:COG2274 432 IG----LLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAI 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 418 VGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAE 497
Cdd:COG2274 507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAAR 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 498 LANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVV 577
Cdd:COG2274 587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1063707070 578 AHRLSTVRNADMIAVIHQGKIVEKGSHTELLKdPEGAYSQLIRLQ 622
Cdd:COG2274 667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQQQ 710
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
112-619 |
1.06e-125 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 398.71 E-value: 1.06e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 112 LGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLAT 191
Cdd:TIGR00958 210 LSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD-ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVM 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 192 FVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYN- 270
Cdd:TIGR00958 289 LLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKe 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 271 --KHLVTAYKAGVIEGGSTGLGLGTLFLVVFcsyALAVWYGGKLILDKGYTGGQvlniIIAVLTGSMSLGQTSPCLSAFA 348
Cdd:TIGR00958 369 alEETLQLNKRKALAYAGYLWTTSVLGMLIQ---VLVLYYGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRVLSYVY 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 349 AGQAAAY----KMFETIERRPNIDSysTNGKVLDDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSG 424
Cdd:TIGR00958 442 SGMMQAVgaseKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSG 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 425 KSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKF 504
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDF 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 505 VDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEalDRIMVNRTTVVVAHRLSTV 584
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTV 677
|
490 500 510
....*....|....*....|....*....|....*
gi 1063707070 585 RNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLI 619
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHLV 711
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
384-618 |
4.51e-116 |
|
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: 355.77 E-value: 4.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQL 618
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
48-622 |
2.18e-111 |
|
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: 356.33 E-value: 2.18e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 48 FYKLFAFADSFDFLLmILGTLGSIGNGLGFPLMTLLFGDLID-AFGENQTNTTDKVS-KVALKFVWLGIGTFAAAFL--Q 123
Cdd:TIGR02203 2 FRRLWSYVRPYKAGL-VLAGVAMILVAATESTLAALLKPLLDdGFGGRDRSVLWWVPlVVIGLAVLRGICSFVSTYLlsW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 124 LSGWMISGerqaarIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRG 203
Cdd:TIGR02203 81 VSNKVVRD------IRVRMFEKLLGLPVSFFD-RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 204 WLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKhlVTAYKAGVIE 283
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDA--VSNRNRRLAM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 284 GGSTGLGLGTLFLVVFCSYALAV--WYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETI 361
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVvlFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 362 ERRPNIDsysTNGKVLDDIKGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG 441
Cdd:TIGR02203 312 DSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 442 DVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGK-EDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHG 520
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENG 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 521 TQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
|
570 580
....*....|....*....|..
gi 1063707070 601 KGSHTELLkDPEGAYSQLIRLQ 622
Cdd:TIGR02203 548 RGTHNELL-ARNGLYAQLHNMQ 568
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
710-984 |
7.50e-110 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 342.89 E-value: 7.50e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 710 AALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQP-PKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAG 788
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 789 CKLVQRIRSMCFEKVVHMEVGWFDEPENSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVV 868
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 869 LAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIG 948
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063707070 949 FGFSFFVLFSSYAASFYVGARLVDDGKTTFDSVFRV 984
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIV 276
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
63-345 |
1.67e-107 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 335.98 E-value: 1.67e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTDK------VSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAA 136
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeflddVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 137 RIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD-KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 217 LVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFL 296
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063707070 297 VVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLS 345
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
356-634 |
5.29e-107 |
|
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: 345.65 E-value: 5.29e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 356 KMFETIERRPNIDSySTNGKVLDDIKGDIELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF 435
Cdd:COG5265 331 RMFDLLDQPPEVAD-APDAPPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 436 YDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTM 515
Cdd:COG5265 408 YDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTR 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 516 VGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQ 595
Cdd:COG5265 488 VGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEA 567
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063707070 596 GKIVEKGSHTELLKDpEGAYSQLIRLQEEKKSDENAAEE 634
Cdd:COG5265 568 GRIVERGTHAELLAQ-GGLYAQMWARQQEEEEAEEALAA 605
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
384-622 |
1.11e-101 |
|
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: 318.02 E-value: 1.11e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLkDPEGAYSQLIRLQ 622
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
373-622 |
2.42e-99 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 324.28 E-value: 2.42e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 373 NGK-VLDDIKGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK 451
Cdd:PRK11176 330 EGKrVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 452 EFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDA-TTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQR 530
Cdd:PRK11176 409 DYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQR 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
250
....*....|..
gi 1063707070 611 pEGAYSQLIRLQ 622
Cdd:PRK11176 569 -NGVYAQLHKMQ 579
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
382-609 |
4.50e-97 |
|
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: 305.69 E-value: 4.50e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
46-982 |
1.80e-95 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 331.22 E-value: 1.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 46 VPFYKLFAFADSFDFLLMILGTLGSIGNGLGFPLMTLLFGDLIdafgeNQTNTTDKVSKVALKFVWLGIGTFAAAFLQLS 125
Cdd:PTZ00265 45 IPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIM-----KNMNLGENVNDIIFSLVLIGIFQFILSFISSF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 126 GWMISGERQAARIRSLYLKTILRQDIAFFDidTNTGEVVgRMSGDTVLIQ--DAMGEKVGKAIQLLATFVGGFVIAFVRG 203
Cdd:PTZ00265 120 CMDVVTTKILKTLKLEFLKSVFYQDGQFHD--NNPGSKL-TSDLDFYLEQvnAGIGTKFITIFTYASAFLGLYIWSLFKN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 204 WLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYN--KHLVTAY--KA 279
Cdd:PTZ00265 197 ARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNlsEKLYSKYilKA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 280 GVIEGGSTGLGLGtlflVVFCSYALAVWYGGKLIL--------DKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQ 351
Cdd:PTZ00265 277 NFMESLHIGMING----FILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 352 AAAYKMFETIERRPNIDSySTNGKVLDDIKgDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSL 431
Cdd:PTZ00265 353 EATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKL 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 432 IERFYDPQAGDVLI-DGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYG--------------KEDA--------- 487
Cdd:PTZ00265 431 IERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDGndsqenknk 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 488 --------------------TTEEIKAA--------AELANASK------FVDKLPQGLDTMVGEHGTQLSGGQKQRIAV 533
Cdd:PTZ00265 511 rnscrakcagdlndmsnttdSNELIEMRknyqtikdSEVVDVSKkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISI 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRNADMIAVIHQGkivEKGSHTELLKDP 611
Cdd:PTZ00265 591 ARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNR---ERGSTVDVDIIG 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 612 EGAYSQLIRLQEEKKSDE----NAAEEQKMSS-----IESFKQSSLRKSSLG---------RSLSKGGSSRGN------- 666
Cdd:PTZ00265 668 EDPTKDNKENNNKNNKDDnnnnNNNNNNKINNagsyiIEQGTHDALMKNKNGiyytminnqKVSSKKSSNNDNdkdsdmk 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 667 SSRHSFNMFGF-PAGIDGNVVQDQE----------EDDTTQPKTEPKKVSIFRIAALNKPEIP----------------- 718
Cdd:PTZ00265 748 SSAYKDSERGYdPDEMNGNSKHENEsasnkksckmSDENASENNAGGKLPFLRNLFKRKPKAPnnlrivyreifsykkdv 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 719 VLILGSISAAanGVILPIFGILISSVIKAFFQpPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSM 798
Cdd:PTZ00265 828 TIIALSILVA--GGLYPVFALLYAKYVSTLFD-FANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRR 904
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 799 CFEKVVHMEVGWFDEPENSSGTIGARLSADAATIR-GLVGDSLaqtvqnlssILAGLIIAFLACWQLAFVvlaMLPLI-A 876
Cdd:PTZ00265 905 LFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKtGLVNNIV---------IFTHFIVLFLVSMVMSFY---FCPIVaA 972
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 877 LNGFLYMKFMKGFSADAK-------------------------KMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKC 931
Cdd:PTZ00265 973 VLTGTYFIFMRVFAIRARltankdvekkeinqpgtvfaynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAI 1052
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 932 EGPMKNGIRQGIVSGIGFGFS-----FFVLFSSYAASFYV--GARLVDD-GKTTFDSVF 982
Cdd:PTZ00265 1053 DYSNKGQKRKTLVNSMLWGFSqsaqlFINSFAYWFGSFLIrrGTILVDDfMKSLFTFLF 1111
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
356-609 |
7.33e-93 |
|
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: 306.30 E-value: 7.33e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 356 KMFETIERrPNIDSYSTNGKVLDDIKGDIELKDVYFTYPARpdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF 435
Cdd:COG4988 310 KIFALLDA-PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 436 YDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTM 515
Cdd:COG4988 387 LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTP 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 516 VGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQ 595
Cdd:COG4988 467 LGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDD 546
|
250
....*....|....
gi 1063707070 596 GKIVEKGSHTELLK 609
Cdd:COG4988 547 GRIVEQGTHEELLA 560
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
377-635 |
2.09e-91 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 303.42 E-value: 2.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 377 LDDIKGDIELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLK 456
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 457 WIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARA 536
Cdd:PRK13657 406 SLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLkDPEGAYS 616
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV-ARGGRFA 564
|
250 260
....*....|....*....|...
gi 1063707070 617 QLIR----LQEEKKSDENAAEEQ 635
Cdd:PRK13657 565 ALLRaqgmLQEDERRKQPAAEGA 587
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
378-598 |
1.95e-87 |
|
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: 279.74 E-value: 1.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 378 DDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW 457
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 458 IRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
384-622 |
3.06e-86 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 277.06 E-value: 3.06e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYpaRPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKI 462
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 543 ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLkDPEGAYSQLIRLQ 622
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELL-AENGLYAYLYQLQ 237
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
382-621 |
2.83e-85 |
|
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: 285.89 E-value: 2.83e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYPARPdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:COG4987 332 PSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:COG4987 411 IAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLIRL 621
Cdd:COG4987 491 PILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQN-GRYRQLYQR 569
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
160-624 |
6.24e-80 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 275.08 E-value: 6.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 160 TGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGgFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAY 239
Cdd:TIGR01846 235 VGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVF-LAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 240 AKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYT 319
Cdd:TIGR01846 314 AAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALS 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 320 GGQVLNIiiavltgSMSLGQ-TSPCLSAFAAgqaaaYKMFE----TIERRPNI-----DSYSTNGKVLDDIKGDIELKDV 389
Cdd:TIGR01846 394 PGQLVAF-------NMLAGRvTQPVLRLAQL-----WQDFQqtgiALERLGDIlnsptEPRSAGLAALPELRGAITFENI 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 390 YFTYpaRPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQE 468
Cdd:TIGR01846 462 RFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQE 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 469 PVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:TIGR01846 540 NVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDE 619
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 549 ATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIRLQEE 624
Cdd:TIGR01846 620 ATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARLWQQQSG 694
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
384-597 |
8.80e-80 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 256.93 E-value: 8.80e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGK 597
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
382-602 |
1.60e-72 |
|
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: 239.03 E-value: 1.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYPARPDEQIfRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
59-367 |
5.66e-72 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 241.20 E-value: 5.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 59 DFLLMILGTLGSIGNGLGFPLMTLLFGDLIDAFGE-NQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAAR 137
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLpDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 138 IRSLYLKTILRQDIAFFDIDTN-TGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18578 87 LRKLAFRAILRQDIAWFDDPENsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 217 LVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFL 296
Cdd:cd18578 167 LLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQS 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 297 VVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLSAFAAGQAAAYKMFETIERRPNI 367
Cdd:cd18578 247 LTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
720-984 |
2.30e-71 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 238.91 E-value: 2.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVILPIFGILISSVIKAF------FQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQ 793
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 794 RIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLP 873
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 874 LIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSF 953
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270
....*....|....*....|....*....|.
gi 1063707070 954 FVLFSSYAASFYVGARLVDDGKTTFDSVFRV 984
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTV 269
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
373-620 |
1.24e-67 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 237.86 E-value: 1.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 373 NGKVLDDIKGDIELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKE 452
Cdd:TIGR01192 324 DAPELPNVKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 453 FQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIA 532
Cdd:TIGR01192 402 VTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpE 612
Cdd:TIGR01192 482 IARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-D 560
|
....*...
gi 1063707070 613 GAYSQLIR 620
Cdd:TIGR01192 561 GRFYKLLR 568
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
382-603 |
4.19e-64 |
|
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: 215.82 E-value: 4.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYpaRPDEQ-IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTASIKDNIAYGKEdATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 541 PRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGS 603
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
71-621 |
1.25e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 236.08 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 71 IGNGLgFPLMTLLF----GDLIDaFGENQTNTtdkvSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTI 146
Cdd:PTZ00265 836 VAGGL-YPVFALLYakyvSTLFD-FANLEANS----NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENI 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 147 LRQDIAFFDIDTNTGEVvgrmsgdtvliqdaMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLV-MLSSIPLLVMAGALLA 225
Cdd:PTZ00265 910 LYQEISFFDQDKHAPGL--------------LSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVsMVMSFYFCPIVAAVLT 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 226 ----IVIAKTASRGQTAYAKaaTVVEQTIGSIRTVASFTGEKQAISN---------YNKHLVTAYK-----AGVIEGG-- 285
Cdd:PTZ00265 976 gtyfIFMRVFAIRARLTANK--DVEKKEINQPGTVFAYNSDDEIFKDpsfliqeafYNMNTVIIYGledyfCNLIEKAid 1053
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 286 -----STGLGLGTLFLVVFCSYA------LAVWYGGKLIldkgyTGGQVL------NIIIAVLTGSMSlGQTSPCLSAFA 348
Cdd:PTZ00265 1054 ysnkgQKRKTLVNSMLWGFSQSAqlfinsFAYWFGSFLI-----RRGTILvddfmkSLFTFLFTGSYA-GKLMSLKGDSE 1127
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 349 AGQAAAYKMFETIERRPNIDSYSTNG---KVLDDIKGDIELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGK 425
Cdd:PTZ00265 1128 NAKLSFEKYYPLIIRKSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGK 1207
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 426 STVVSLIERFYD------------------------------------------------------PQAGDVLIDGINLK 451
Cdd:PTZ00265 1208 STVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDIC 1287
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 452 EFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRI 531
Cdd:PTZ00265 1288 DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRI 1367
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 532 AVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRNADMIAVIHQ----GKIVE-KGSH 604
Cdd:PTZ00265 1368 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTH 1447
|
650
....*....|....*..
gi 1063707070 605 TELLKDPEGAYSQLIRL 621
Cdd:PTZ00265 1448 EELLSVQDGVYKKYVKL 1464
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
359-620 |
2.70e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 225.09 E-value: 2.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 359 ETIERRPNIdSYSTNGKVLDDiKGDIELKDVYFTYPARPDeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDP 438
Cdd:PRK11160 316 EITEQKPEV-TFPTTSTAAAD-QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 439 QAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKlPQGLDTMVGE 518
Cdd:PRK11160 393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 519 HGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
250 260
....*....|....*....|..
gi 1063707070 599 VEKGSHTELLKDpEGAYSQLIR 620
Cdd:PRK11160 552 IEQGTHQELLAQ-QGRYYQLKQ 572
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
384-593 |
7.43e-63 |
|
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: 222.55 E-value: 7.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:TIGR02857 322 LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVI 593
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
382-622 |
2.98e-62 |
|
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: 224.84 E-value: 2.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYpaRPD-EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:TIGR03797 450 GAIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRR 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTASIKDNIAyGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:TIGR03797 528 QLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRK 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 541 PRILLLDEATSALDAESERVVQEALDRIMVNRttVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIR 620
Cdd:TIGR03797 607 PRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR-EGLFAQLAR 683
|
..
gi 1063707070 621 LQ 622
Cdd:TIGR03797 684 RQ 685
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
406-624 |
1.35e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 220.49 E-value: 1.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKE 485
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNP 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 486 DATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEAL 565
Cdd:PRK11174 449 DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQAL 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 566 DRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLIRLQEE 624
Cdd:PRK11174 529 NAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG-GLFATLLAHRQE 586
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
107-634 |
1.69e-61 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 219.97 E-value: 1.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 107 LKFVWLgIGTFAAAFlQLsgwmisgerqAARIRSLYLKTILRQDIAFFdIDTNTGEVVGRMSGDTVLIQDAMGEKVgkaI 186
Cdd:PRK10789 52 LRYVWR-VLLFGASY-QL----------AVELREDFYRQLSRQHPEFY-LRHRTGDLMARATNDVDRVVFAAGEGV---L 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 187 QLLATFVGGFVIAFVR----GWLLTLvmLSSIPLLVMAgallaIVIAKTASR-------GQTAYAKAATVVEQTIGSIRT 255
Cdd:PRK10789 116 TLVDSLVMGCAVLIVMstqiSWQLTL--LALLPMPVMA-----IMIKRYGDQlherfklAQAAFSSLNDRTQESLTSIRM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 256 VASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVwyggklildkgyTGGQVLniiiaVLTGSM 335
Cdd:PRK10789 189 IKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAI------------GGGSWM-----VVNGSL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 336 SLGQ-TS----------PCLSAFAagqaaaykMFETIER--------------RPNIDSYStngKVLDDIKGDIELKDVY 390
Cdd:PRK10789 252 TLGQlTSfvmylglmiwPMLALAW--------MFNIVERgsaaysriramlaeAPVVKDGS---EPVPEGRGELDVNIRQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 391 FTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPV 470
Cdd:PRK10789 321 FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 LFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEAT 550
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 551 SALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPeGAYSQLIRLQ--EEKKSD 628
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQqlEAALDD 558
|
....*.
gi 1063707070 629 ENAAEE 634
Cdd:PRK10789 559 APEIRE 564
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
382-622 |
4.30e-58 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 210.73 E-value: 4.30e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNIAYGKeDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDpEGAYSQLIRL 621
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQL 574
|
.
gi 1063707070 622 Q 622
Cdd:PRK10790 575 Q 575
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
63-342 |
1.19e-57 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 201.35 E-value: 1.19e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAF---GENQTNTT---------------DKVSKVALKFVWLGIGTFAAAFLQL 124
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtngGMTNITGNssglnssagpfekleEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 125 SGWMISGERQAARIRSLYLKTILRQDIAFFDIDTnTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGW 204
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVND-TGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 205 LLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEG 284
Cdd:cd18558 160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 285 GSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSP 342
Cdd:cd18558 240 ITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVP 297
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
60-619 |
2.18e-55 |
|
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: 205.36 E-value: 2.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSignglgfplmtLLFGDLIDAFGENQTNTTDKVSKVALKFVWL--GIGTFAAAFLQlsgwMISGERQAAR 137
Cdd:TIGR01193 166 IIVTLISIAGS-----------YYLQKIIDTYIPHKMMGTLGIISIGLIIAYIiqQILSYIQIFLL----NVLGQRLSID 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 138 IRSLYLKTILRQDIAFFDIdTNTGEVVGRMSgDTVLIQDAMGEKVGKAIQLLATFVG-GFVIAFvRGWLLTLVMLSSIPL 216
Cdd:TIGR01193 231 IILSYIKHLFELPMSFFST-RRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIvGLFLVR-QNMLLFLLSLLSIPV 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 217 LvmagALLAIVIAKTASRGQTAYAKAATVVEQTI----GSIRTVASFTGEKQA-------ISNYNKHLVTAYKAGVIEGG 285
Cdd:TIGR01193 308 Y----AVIIILFKRTFNKLNHDAMQANAVLNSSIiedlNGIETIKSLTSEAERyskidseFGDYLNKSFKYQKADQGQQA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 286 STGLGLGTLFLVVfcsyalaVWYGGKLILDKGYTGGQVL--NIIIAVLTGSM-SLGQTSPCLSAFAAGQAAAYKMF--ET 360
Cdd:TIGR01193 384 IKAVTKLILNVVI-------LWTGAYLVMRGKLTLGQLItfNALLSYFLTPLeNIINLQPKLQAARVANNRLNEVYlvDS 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 361 IERRPNIDSYSTNgkvlddIKGDIELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA 440
Cdd:TIGR01193 457 EFINKKKRTELNN------LNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 441 GDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYG-KEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEH 519
Cdd:TIGR01193 529 GEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEE 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 520 GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRiMVNRTTVVVAHRLSTVRNADMIAVIHQGKIV 599
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKII 687
|
570 580
....*....|....*....|
gi 1063707070 600 EKGSHTELLKDpEGAYSQLI 619
Cdd:TIGR01193 688 EQGSHDELLDR-NGFYASLI 706
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
720-982 |
1.81e-53 |
|
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: 187.85 E-value: 1.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMC 799
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:pfam00664 81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSS 959
Cdd:pfam00664 159 AVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260
....*....|....*....|...
gi 1063707070 960 YAASFYVGARLVDDGKTTFDSVF 982
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLV 261
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
720-971 |
3.94e-53 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 188.25 E-value: 3.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVILPIFGILISSVIKAFFQ------------------PPKKLKEDTSFWAIIFMVLGFASIIAYPAQT 781
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 782 FFFAIAGCKLVQRIRSMCFEKVVHMEVGWFdePENSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLAC 861
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 862 WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQ 941
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270
....*....|....*....|....*....|
gi 1063707070 942 GIVSGIGFGFSFFVLFSSYAASFYVGARLV 971
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLV 268
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
63-335 |
5.44e-53 |
|
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: 186.69 E-value: 5.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLY 142
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 143 LKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGA 222
Cdd:pfam00664 81 FKKILRQPMSFFD-TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 223 LLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSY 302
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1063707070 303 ALAVWYGGKLILDKGYTGGQ--VLNIIIAVLTGSM 335
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
381-609 |
1.70e-52 |
|
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: 193.81 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 381 KGDIELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLkeFQlkWIRS 460
Cdd:COG4618 328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADL--SQ--WDRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 K----IGLVSQEPVLFTASIKDNIAyGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARA 536
Cdd:COG4618 403 ElgrhIGYLPQDVELFDGTIAENIA-RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARA 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
95-581 |
1.05e-51 |
|
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: 190.65 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 95 QTNTTDKVSKVALKFVWLGigtFAAAFLQLSGWMIS----------------GERQAARIRSL--YLKTILRQDIAF--- 153
Cdd:TIGR02868 9 KPRRRRLALAVLLGALALG---SAVALLGVSAWLISraaemppvlylsvaavAVRAFGIGRAVfrYLERLVGHDAALrsl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 154 -------FDIDT----------NTGEVVGRMSGDTvliqDAMGEKVGKAIQ--LLATFVGGFVIAFVrGWLLT---LVML 211
Cdd:TIGR02868 86 galrvrvYERLArqalagrrrlRRGDLLGRLGADV----DALQDLYVRVIVpaGVALVVGAAAVAAI-AVLSVpaaLILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 212 SSIPLLVMAGALLAIVIAKTA----SRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGViegGST 287
Cdd:TIGR02868 161 AGLLLAGFVAPLVSLRAARAAeqalARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAA---AAT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 288 GLGLGTLFLVVFCSYALAVWYGGKlildkGYTGGQVLNIIIAV-----LTGSMSLGQTSPCLSAFAAGQAAAYKMFETIE 362
Cdd:TIGR02868 238 ALGAALTLLAAGLAVLGALWAGGP-----AVADGRLAPVTLAVlvllpLAAFEAFAALPAAAQQLTRVRAAAERIVEVLD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 363 -RRPNIDSYSTNGKVLDDIKGDIELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG 441
Cdd:TIGR02868 313 aAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 442 DVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGT 521
Cdd:TIGR02868 391 EVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGA 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 522 QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRL 581
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
384-612 |
5.34e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 179.07 E-value: 5.34e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPV--LFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
384-617 |
6.02e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 176.25 E-value: 6.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE--QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWI 458
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 459 RSKIGLVSQEPV--LFTA-SIKDNIAYG---KEDATTEEIKA-AAELANA----SKFVDKLPQgldtmvgehgtQLSGGQ 527
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRErVAELLERvglpPDLADRYPH-----------ELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSH 604
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
250
....*....|...
gi 1063707070 605 TELLKDPEGAYSQ 617
Cdd:COG1123 490 EEVFANPQHPYTR 502
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
381-609 |
1.45e-46 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 176.00 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 381 KGDIELKDVYFTyPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:TIGR01842 314 EGHLSVENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 541 PRILLLDEATSALDAESERVVQEALDRIMVNR-TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
384-603 |
5.84e-46 |
|
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: 164.66 E-value: 5.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD-----PQAGDVLIDG--INLKEFQLK 456
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 457 WIRSKIGLVSQEPVLFTASIKDNIAYG-------KEDATTEEIKAAAELANASKFV-DKLpqgldtmvgeHGTQLSGGQK 528
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVkDRL----------HALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 603
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGP 223
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
384-598 |
2.17e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 162.29 E-value: 2.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIA----YGKEDATTEEIKAAAELANaskfvdkLPQG-LDTMVGEhgtqLSGGQKQRIAVARAIL 538
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLERLG-------LPPDiLDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAH--RLSTvRNADMIAVIHQGKI 598
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
384-612 |
6.02e-45 |
|
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: 161.98 E-value: 6.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIR 459
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SKIGLVSQEPVLFTA-SIKDNIAYGKEDATTE--EIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPkaEIEERVlellELVGLEDKADAYP-----------AQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
....*
gi 1063707070 608 LKDPE 612
Cdd:cd03258 229 FANPQ 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
385-597 |
7.86e-45 |
|
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: 161.10 E-value: 7.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGL 464
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARA 536
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGlenlglPEEEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGK 597
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
384-602 |
8.36e-45 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 159.79 E-value: 8.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQlKWIRSKIG 463
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
384-598 |
1.65e-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: 158.53 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
384-617 |
1.62e-43 |
|
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: 158.43 E-value: 1.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQ-IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKI 462
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPvlfTAS------IKDNIA-----YGKEDaTTEEIKAAAELAN-ASKFVDKLPqgldtmvgeHgtQLSGGQKQR 530
Cdd:COG1124 82 QMVFQDP---YASlhprhtVDRILAeplriHGLPD-REERIAELLEQVGlPPSFLDRYP---------H--QLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 531 IAVARAILKDPRILLLDEATSALDAeserVVQ----EALDRIMVNR--TTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 603
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDV----SVQaeilNLLKDLREERglTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELT 222
|
250
....*....|....
gi 1063707070 604 HTELLKDPEGAYSQ 617
Cdd:COG1124 223 VADLLAGPKHPYTR 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
382-603 |
1.84e-43 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 156.80 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYpaRPD-EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:cd03369 5 GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTASIKDNI-AYGKEDatTEEIKAAAElanaskfvdklpqgldtmVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 540 DPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGS 603
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
384-602 |
1.15e-42 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 155.36 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLKWIR 459
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SKIGLVSQEPvlFTA-----SIKDNIA-----YGKEDATTEEIKAAAELA----NASKFVDKLPQgldtmvgehgtQLSG 525
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAeplriHGKLSKKEARKEAVLLLLvgvgLPEEVLNRYPH-----------ELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
79-338 |
4.06e-42 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 156.26 E-value: 4.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 79 LMTLLFGDLIDAFgENQTNTTDKVSKVALK---FVWLGIGTFAAAFLQLSGWM--ISGERQAARIRSLYLKTILRQDIAF 153
Cdd:cd18780 14 ALPYFFGQVIDAV-TNHSGSGGEEALRALNqavLILLGVVLIGSIATFLRSWLftLAGERVVARLRKRLFSAIIAQEIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 154 FDIdTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTAS 233
Cdd:cd18780 93 FDV-TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 234 RGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLI 313
Cdd:cd18780 172 KFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLV 251
|
250 260
....*....|....*....|....*
gi 1063707070 314 LDKGYTGGQVLNIIIAVLTGSMSLG 338
Cdd:cd18780 252 IDGELTTGLLTSFLLYTLTVAMSFA 276
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
60-345 |
7.56e-42 |
|
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: 155.03 E-value: 7.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTntTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIR 139
Cdd:cd18557 2 LLFLLISSAAQL-------LLPYLIGRLIDTIIKGGD--LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 140 SLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVM 219
Cdd:cd18557 73 RDLFSSLLRQEIAFFD-KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 220 AGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVF 299
Cdd:cd18557 152 ASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1063707070 300 CSYALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTSPCLS 345
Cdd:cd18557 232 LSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLA 277
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
384-609 |
1.16e-41 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 152.66 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTA-SIKDNIAYGKEDATT---EEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRlseEEIREIVleklEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
384-609 |
1.36e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 152.53 E-value: 1.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTA-SIKDNI-----AYGKEDATTEEikAAAELAnasKFVDkLPQGLDTMVGehgtQLSGGQKQRIAVARAI 537
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARE--RIDELL---ELFG-LTDAADRKVG----TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
384-602 |
3.37e-41 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 150.75 E-value: 3.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLkeFQLKWIRSKIG 463
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARA 536
Cdd:cd03259 76 MVFQDYALFPhLTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKG 602
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
384-612 |
5.56e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 151.81 E-value: 5.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW-IRSKI 462
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEP--VLFTASIKDNIAYGKEDA--TTEEIKA----AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVA 534
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENLgvPREEMRKrvdeALKLVGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
384-612 |
7.20e-41 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 153.69 E-value: 7.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDGIN---LKEFQLK 456
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInllER---PTSGSVLVDGVDltaLSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 457 WIRSKIGLVSQEPVLFTA-SIKDNIAYGKEDA--TTEEIKA-AAELAnasKFVdklpqGLDTMVGEHGTQLSGGQKQRIA 532
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPLEIAgvPKAEIRKrVAELL---ELV-----GLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDV 228
|
....*
gi 1063707070 608 LKDPE 612
Cdd:COG1135 229 FANPQ 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
384-611 |
8.00e-41 |
|
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: 150.53 E-value: 8.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFT-ASIKDNIA-------YGKedattEEIKA-AAELAnasKFVDKLPQGLdtmVGEHGTQLSGGQKQRIAVA 534
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIAlvpkllkWPK-----EKIRErADELL---ALVGLDPAEF---ADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 535 RAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
112-620 |
1.51e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 163.22 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 112 LGIGTFAAAFLQlSGWMISGERQAA-RIRSLYLKTILRQDIAFFDidTN-TGEVVGRMSGDTVLIQ----DAMGEKVGKA 185
Cdd:PLN03232 959 LGFGQVAVTFTN-SFWLISSSLHAAkRLHDAMLNSILRAPMLFFH--TNpTGRVINRFSKDIGDIDrnvaNLMNMFMNQL 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 186 IQLLATFVggfviafVRGWLLTLVMLSSIPLLVMAGAllAIVIAKTASRG---------QTAYAKAATVVeQTIGSIRTV 256
Cdd:PLN03232 1036 WQLLSTFA-------LIGTVSTISLWAIMPLLILFYA--AYLYYQSTSREvrrldsvtrSPIYAQFGEAL-NGLSSIRAY 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 257 ASF-----TGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVfcSYAlavwyggklILDKGYTGGQVLNIIIAVL 331
Cdd:PLN03232 1106 KAYdrmakINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTA--TFA---------VLRNGNAENQAGFASTMGL 1174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 332 TGSMSLGQTSpCLSAFAAGQAAAYKMFETIERRPN-IDSYSTNGKVLDD--------IKGDIELKDVYFTY-PARPdeQI 401
Cdd:PLN03232 1175 LLSYTLNITT-LLSGVLRQASKAENSLNSVERVGNyIDLPSEATAIIENnrpvsgwpSRGSIKFEDVHLRYrPGLP--PV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNIA 481
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 482 YGKE--DATTEEikaAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:PLN03232 1332 PFSEhnDADLWE---ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDS 1408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 560 VVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIR 620
Cdd:PLN03232 1409 LIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
384-612 |
3.52e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.60 E-value: 3.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL--KEFQLKWIRSK 461
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFT-ASIKDNIAYG--------KEDAtteEIKAAAELAN---ASKfVDKLPqgldtmvgehgTQLSGGQKQ 529
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEA---EERAMELLERvglADK-ADAYP-----------AQLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALDAEserVVQEALDrIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGS 603
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
....*....
gi 1063707070 604 HTELLKDPE 612
Cdd:COG1126 220 PEEFFENPQ 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
384-600 |
4.23e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.88 E-value: 4.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKST---VVSLIERfydPQAGDVLIDGIN---LKEFQL- 455
Cdd:COG1136 5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDissLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 456 KWIRSKIGLVSQEPVLF-TASIKDNIA----YGKEDATtEEIKAAAELANA---SKFVDKLPqgldtmvgehgTQLSGGQ 527
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLpELTALENVAlpllLAGVSRK-ERRERARELLERvglGDRLDHRP-----------SQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
384-609 |
4.31e-40 |
|
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: 148.20 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTA-SIKDNIAYG-KE--DATTEEIKAAAELanaskfvdKLpqgldTMVGEHGT------QLSGGQKQR 530
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREhtDLSEAEIRELVLE--------KL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELrdELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 1063707070 608 LK 609
Cdd:COG1127 230 LA 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
384-597 |
1.88e-39 |
|
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: 145.30 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQ--IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerfydpqagdvlidginLKEFQLK----W 457
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----------------LGELEKLsgsvS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 458 IRSKIGLVSQEPVLFTASIKDNIAYGKE-DattEE-----IKAAAELANaskfVDKLPQGLDTMVGEHGTQLSGGQKQRI 531
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENILFGKPfD---EEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 532 AVARAILKDPRILLLDEATSALDAES-----ERVVQEALdriMVNRTTVVVAHRLSTVRNADMIAVIHQGK 597
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
384-613 |
3.37e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.52 E-value: 3.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEFQLKWIRS 460
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEP--VLFTASIKDNIAYGKE--DATTEEIKAAAElaNASKFVdklpqGLDTMVGEHGTQLSGGQKQRIAVARA 536
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVL--ELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEG 613
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
384-597 |
7.36e-39 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 142.71 E-value: 7.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL--KEFQLKWIRSK 461
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFT-ASIKDNIAYGkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKD 540
Cdd:cd03229 78 IGMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 541 PRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGK 597
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
384-600 |
1.72e-38 |
|
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: 143.00 E-value: 1.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKI 462
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVV-VAHRLS-TVRNADMIAVIHQ--GKIVE 600
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWReTGKTVLlVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
1.73e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 144.75 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEP--VLFTASIKDNIAYGKEDA--TTEEIKA----AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKkvPPKKMKDiiddLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA--HRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
402-551 |
2.23e-38 |
|
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: 140.09 E-value: 2.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLF-TASIKDNI 480
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 481 AYGKEDATTEEIKAAAELANASKFVDkLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 551
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
381-609 |
3.66e-38 |
|
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: 155.49 E-value: 3.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 381 KGDIELKDVYFTYpaRPD-EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIR 459
Cdd:TIGR00957 1282 RGRVEFRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SKIGLVSQEPVLFTASIKDNI-AYGKedATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:TIGR00957 1360 FKITIIPQDPVLFSGSLRMNLdPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALL 1437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
382-620 |
4.95e-38 |
|
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: 143.13 E-value: 4.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYPA--RPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIR 459
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SKIGLVSQEPVLFTASIKDNIAYGKEdATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 540 DPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLI 619
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
.
gi 1063707070 620 R 620
Cdd:cd03288 254 R 254
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
725-977 |
8.55e-38 |
|
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: 143.47 E-value: 8.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 725 ISAAANGVILPIFGILISSVIKaffqppKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVV 804
Cdd:cd18557 7 ISSAAQLLLPYLIGRLIDTIIK------GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 805 HMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18557 81 RQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 885 FMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASF 964
Cdd:cd18557 159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVL 238
|
250
....*....|...
gi 1063707070 965 YVGARLVDDGKTT 977
Cdd:cd18557 239 WYGGYLVLSGQLT 251
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
725-977 |
1.86e-37 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 142.77 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 725 ISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVV 804
Cdd:cd18780 7 VSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 805 HMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18780 87 AQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 885 FMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASF 964
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVL 244
|
250
....*....|...
gi 1063707070 965 YVGARLVDDGKTT 977
Cdd:cd18780 245 WYGGRLVIDGELT 257
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
384-608 |
4.32e-37 |
|
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: 140.18 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVL-FTASIKDNIAYG------------KEDAttEEIKAAAELANASKFVDKLpqgldtmVgehgTQLSGGQKQR 530
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGryphlglfgrpsAEDR--EAVEEALERTGLEHLADRP-------V----DELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 1063707070 608 L 608
Cdd:COG1120 226 L 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
382-641 |
5.49e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 151.81 E-value: 5.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYpaRPD-EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRS 460
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTASIKDNIAYGKE--DATTEEikaAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEhnDADLWE---SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQL 618
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
250 260 270
....*....|....*....|....*....|....*
gi 1063707070 619 IR------------LQEEKKSDENAAEEQKMSSIE 641
Cdd:PLN03130 1471 VQstgaanaqylrsLVFGGDEDRLAREESKALDGQ 1505
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
383-611 |
7.00e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 142.54 E-value: 7.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 383 DIELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQlkwiR 459
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdvTGLPPEK----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 sKIGLVSQEPVLF---TasIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQR 530
Cdd:COG3842 78 -NVGMVFQDYALFphlT--VAENVAFGlrmrgvPKAEIRARVAELLELVGLEGLADRYP-----------HQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 531 IAVARAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHT 605
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQreLGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPE 221
|
....*.
gi 1063707070 606 ELLKDP 611
Cdd:COG3842 222 EIYERP 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
385-597 |
1.15e-36 |
|
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: 135.45 E-value: 1.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGL 464
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQepvlftasikdniaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRIL 544
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 545 LLDEATSALDAESERVVQEALDRIMV-NRTTVVVAHRLSTVRNA-DMIAVIHQGK 597
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
384-609 |
1.41e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 139.38 E-value: 1.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEP--VLFTASIKDNIAYGKE------DATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLEnigvprEEMVERVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 536 AILKDPRILLLDEATSALDAESErvvQEALD--RIMVNRTTVVV---AHRLSTVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGR---REVLEtvRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
384-612 |
2.74e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 140.67 E-value: 2.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDG----INL--KEfq 454
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIaglET---PDSGRIVLNGrdlfTNLppRE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 455 lkwiRsKIGLVSQEPVLF-TASIKDNIAYG--KEDATTEEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQ 527
Cdd:COG1118 75 ----R-RVGFVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVeellELVQLEGLADRYP-----------SQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 528 KQRIAVARAILKDPRILLLDEATSALDA----ESERVVQEALDRImvNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKG 602
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|
gi 1063707070 603 SHTELLKDPE 612
Cdd:COG1118 217 TPDEVYDRPA 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
384-598 |
3.10e-36 |
|
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: 136.47 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF----QLKWI 458
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLsekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 459 RSKIGLVSQEPVL---FTAsiKDNIAYGKEDATTEEIKAAAELANASKFVDkLPQGLDTMVGehgtQLSGGQKQRIAVAR 535
Cdd:cd03255 81 RRHIGFVFQSFNLlpdLTA--LENVELPLLLAGVPKKERRERAEELLERVG-LGDRLNHYPS----ELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRNADMIAVIHQGKI 598
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
384-579 |
5.45e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.14 E-value: 5.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKI 462
Cdd:COG1116 8 LELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVV-VAH 579
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLfVTH 197
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
384-609 |
9.32e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 136.14 E-value: 9.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLF-TASIKDNIAY------GKEDATTEEIKAAAELANASKFVDKLpqgldtmVGEhgtqLSGGQKQRIAVARA 536
Cdd:COG4555 78 VLPDERGLYdRLTVRENIRYfaelygLFDEELKKRIEELIELLGLEEFLDRR-------VGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELRE 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
384-612 |
1.03e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 136.32 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD--PQA---GDVLIDGINL--KEFQLK 456
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 457 WIRSKIGLVSQEPVLFTASIKDNIAYG------KEDATTEEI-----KAAA---ELAnaskfvDKLpqgldtmvGEHGTQ 522
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslRKAAlwdEVK------DRL--------KKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 523 LSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEK 601
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEF 234
|
250
....*....|.
gi 1063707070 602 GSHTELLKDPE 612
Cdd:COG1117 235 GPTEQIFTNPK 245
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
384-598 |
1.51e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 134.19 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSK 461
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFT-ASIKDNIAYG-----KEDatteeiKAAAElANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVAR 535
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikvkGMS------KAEAE-ERALELLEKV--GLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 536 AILKDPRILLLDEATSALDAEserVVQEALDrIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
385-602 |
4.78e-35 |
|
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: 131.79 E-value: 4.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGL 464
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQepvlftasikdniaygkedatteeikaAAELANASKFVDKlpqgldtmvgeHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADR-----------PFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 545 LLDEATSALDAES-----ERVVQEALDRimvNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKG 602
Cdd:cd03214 120 LLDEPTSHLDIAHqiellELLRRLARER---GKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
384-611 |
5.32e-35 |
|
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: 136.34 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEF---QLK 456
Cdd:COG0444 2 LEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 457 WIRSK-IGLVSQEPvlFTA-----SIKDNIAYG---KEDATTEEIKAAAE-------LANASKFVDKLPqgldtmvgeHg 520
Cdd:COG0444 82 KIRGReIQMIFQDP--MTSlnpvmTVGDQIAEPlriHGGLSKAEARERAIellervgLPDPERRLDRYP---------H- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 521 tQLSGGQKQRIAVARAILKDPRILLLDEATSALDAeserVVQ----EALDRIMVNR-TTVV-VAHRLSTVRN-ADMIAVI 593
Cdd:COG0444 150 -ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaqilNLLKDLQRELgLAILfITHDLGVVAEiADRVAVM 224
|
250
....*....|....*...
gi 1063707070 594 HQGKIVEKGSHTELLKDP 611
Cdd:COG0444 225 YAGRIVEEGPVEELFENP 242
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
384-606 |
7.29e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 132.87 E-value: 7.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQE-PVLFTASIKDNIAY-----GKEDATTEE-IKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAV 533
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 534 ARAILKDPRILLLDEATSALDAE-SERVVqEALDRImvNR--TTVVVA-HRLSTVRNADM-IAVIHQGKIVEKGSHTE 606
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEI--NRrgTTVLIAtHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
406-615 |
1.48e-34 |
|
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: 133.54 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLKWIRSK-IGLVSQEPVLFT-ASIKDNI 480
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiAAMSRKELRELRRKkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AYGKE----DATTEEIKA--AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:cd03294 124 AFGLEvqgvPRAEREERAaeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 555 AESERVVQEALDRI--MVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
384-611 |
1.61e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 135.31 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIR 459
Cdd:PRK11153 2 IELKNISKVFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SKIGLVSQEPVLFTA-SIKDNIAYGKEDATT--EEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALPLELAGTpkAEIKARVtellELVGLSDKADRYP-----------AQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRImvNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVSEV 228
|
....
gi 1063707070 608 LKDP 611
Cdd:PRK11153 229 FSHP 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
384-598 |
2.17e-34 |
|
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: 129.44 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwIRSKIG 463
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLF-TASIKDNIaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtQLSGGQKQRIAVARAILKDPR 542
Cdd:cd03230 77 YLPEEPSLYeNLTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 543 ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKI 598
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
2.48e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.94 E-value: 2.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13647 5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGShTELLKDPE 612
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
719-977 |
1.01e-33 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 131.52 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 719 VLILGSISAAANGVILPIFGILISSVIkaffqpPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSM 798
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVI------PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 799 CFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALN 878
Cdd:cd07346 78 LFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 879 GFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFS 958
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....*....
gi 1063707070 959 SYAASFYVGARLVDDGKTT 977
Cdd:cd07346 236 GTALVLLYGGYLVLQGSLT 254
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
384-598 |
1.61e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.44 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKIG 463
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVL---FTASIKDNIA------------YGKEDAttEEIKAAAELANASKFVDKLpqgldtmVGEhgtqLSGGQK 528
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVLmgrygrrglfrrPSRADR--EAVDEALERVGLEDLADRP-------IGE----LSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVR-NADMIAVIHQGKI 598
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVReYFDRVLLLNRGLV 217
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
720-974 |
5.61e-33 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 129.56 E-value: 5.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPKKLKEDTSFwAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMC 799
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTF-ALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:cd18573 81 FKSILRQDAAFFDK--NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSS 959
Cdd:cd18573 159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
|
250
....*....|....*
gi 1063707070 960 YAASFYVGARLVDDG 974
Cdd:cd18573 239 LLSVLYYGGSLVASG 253
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
403-611 |
1.83e-32 |
|
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: 126.30 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqLKWIRSKIGLVSQEPVLFT-ASIKDNIA 481
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFPhMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 482 YGKEDATTEEIKAAAELANASKFVdklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVV 561
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 562 QEALDRIM-VNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:cd03299 169 REELKKIRkEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
158-896 |
1.95e-32 |
|
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: 137.00 E-value: 1.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 158 TNTGEVVGRMSGDTVLIQDamgekvgkaiqlLATFVG-------GFVIAFVRGWL-LTLVMLSSIPLLVMAGALLAIVIA 229
Cdd:TIGR00957 412 STVGEIVNLMSVDAQRFMD------------LATYINmiwsaplQVILALYFLWLnLGPSVLAGVAVMVLMVPLNAVMAM 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 230 KTASRgQTAYAKAA----TVVEQTIGSIRTVASFTGE----KQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCS 301
Cdd:TIGR00957 480 KTKTY-QVAHMKSKdnriKLMNEILNGIKVLKLYAWElaflDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALIT 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 302 YALAVWYGGKLILD--KGYTGGQVLNI-----------IIAVLTGSMSLGQTSPCLSAFAAGQaaaykmfETIERRPnid 368
Cdd:TIGR00957 559 FAVYVTVDENNILDaeKAFVSLALFNIlrfplnilpmvISSIVQASVSLKRLRIFLSHEELEP-------DSIERRT--- 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 369 systngkVLDDIKGDIELKDVYFTYpARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGi 448
Cdd:TIGR00957 629 -------IKPGEGNSITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG- 699
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 449 nlkefqlkwirsKIGLVSQEPVLFTASIKDNIAYGK---EDATTEEIKAAAELANaskfVDKLPQGLDTMVGEHGTQLSG 525
Cdd:TIGR00957 700 ------------SVAYVPQQAWIQNDSLRENILFGKalnEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSG 763
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEAL---DRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG 602
Cdd:TIGR00957 764 GQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 843
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 603 SHTELLkDPEGAYSQLIRLQEEKKSDENAAEEQKMSSIESFKQSSLRKSS----------LGRSLSKGGSSRGNSSRHsf 672
Cdd:TIGR00957 844 SYQELL-QRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIENGmlvtdvvgkqLQRQLSASSSDSGDQSRH-- 920
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 673 nmfgfpagidgnvVQDQEEDDTTQPKTEPKKVSIFRIAALNKPEIPVLILGSISAAANGVILPIFGILISSV-------- 744
Cdd:TIGR00957 921 -------------HGSSAELQKAEAKEETWKLMEADKAQTGQVELSVYWDYMKAIGLFITFLSIFLFVCNHVsalasnyw 987
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 745 IKAFFQPP--KKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDepENSSGTIG 822
Cdd:TIGR00957 988 LSLWTDDPmvNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLV 1065
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 823 ARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACwQLAFVVlamLPLIALNGFLYMKFMKGFSADAKKM 896
Cdd:TIGR00957 1066 NRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLAT-PIAAVI---IPPLGLLYFFVQRFYVASSRQLKRL 1135
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
384-608 |
3.86e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 125.25 E-value: 3.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpdEQIFRgFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKE---FQlkwiRs 460
Cdd:COG3840 2 LRLDDLTYRYG----DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlppAE----R- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTA-SIKDNIAYGKEDA---TTEE---IKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAV 533
Cdd:COG3840 72 PVSMLFQENNLFPHlTVAQNIGLGLRPGlklTAEQraqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 534 ARAILKDPRILLLDEATSALD----AESERVVQEALDRimVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELL 608
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
699-978 |
6.12e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 132.60 E-value: 6.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 699 TEPKKVSIFRIAALNKPEIPVLILGSISAAANGVILPIFGILISSVIKAFFQPPkklkeDTS---FWAIIFMVLGFASII 775
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-----DLSallLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 776 AYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLI 855
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 856 IAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPM 935
Cdd:COG1132 155 VLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELR 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063707070 936 KNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTF 978
Cdd:COG1132 235 RANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTV 277
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
404-617 |
7.34e-32 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.16 E-value: 7.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRSKIGLVSQEPvlfTAS----- 475
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVFQDP---YASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 -IKDNIAYG---KEDATTEEIKA-AAELanaskfvdklpqgLDtMVG---EHGT----QLSGGQKQRIAVARAILKDPRI 543
Cdd:COG4608 113 tVGDIIAEPlriHGLASKAERRErVAEL-------------LE-LVGlrpEHADryphEFSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 544 LLLDEATSALD----AEserVV------QEALdrimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:COG4608 179 IVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARPL 250
|
....*
gi 1063707070 613 GAYSQ 617
Cdd:COG4608 251 HPYTQ 255
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
384-607 |
7.39e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.00 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEP--VLFTASIKDNIAYGKE------DATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVAR 535
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLEnkgiphEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 536 AILKDPRILLLDEATSALDAESE----RVVQEALDRimVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
382-611 |
9.63e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 9.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSK 461
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLF-TASIKDNIAYG----KEDAttEEIKA----AAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIA 532
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPK--AEIDRrvreAAELLGLEDLLDRKP-----------KQLSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESeRV--------VQEALdrimvNRTTVVVAH------RLstvrnADMIAVIHQGKI 598
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRI 212
|
250
....*....|...
gi 1063707070 599 VEKGSHTELLKDP 611
Cdd:COG3839 213 QQVGTPEELYDRP 225
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
384-612 |
1.00e-31 |
|
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: 123.89 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefQLKWIRSKIG 463
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARA 536
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEEP 222
|
.
gi 1063707070 612 E 612
Cdd:cd03300 223 A 223
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
64-336 |
1.56e-31 |
|
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: 125.29 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 64 ILGTLGSIGNGLGFPLmtlLFGDLIDAFgeNQTNTTDKVSKVALkfVWLGIGTFAAAFLQLSGWMIS--GERQAARIRSL 141
Cdd:cd18576 2 LILLLLSSAIGLVFPL---LAGQLIDAA--LGGGDTASLNQIAL--LLLGLFLLQAVFSFFRIYLFArvGERVVADLRKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 142 YLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAG 221
Cdd:cd18576 75 LYRHLQRLPLSFFH-ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 222 ALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCS 301
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063707070 302 YALAVWYGGKLILDKGYTGGQVLNIII--AVLTGSMS 336
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVAFLLytLFIAGSIG 270
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
403-615 |
1.59e-31 |
|
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: 123.60 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIGLVSQEPVLFT-ASIKDNIA 481
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 482 YGKEDATTEEIKAAAELANASKFVDKLPQgLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDA----ES 557
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRAKVHELLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkEL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 558 ERVVQEALDRIMVnrTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:cd03296 176 RRWLRRLHDELHV--TTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
384-602 |
2.29e-31 |
|
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: 122.36 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIG 463
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARA 536
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQqrLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
725-975 |
2.71e-31 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 124.58 E-value: 2.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 725 ISAAANgVILPIF-GILISSVIKAffqppkklKEDTSFW-AIIFMV-LGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFE 801
Cdd:cd18572 7 VAALSE-LAIPHYtGAVIDAVVAD--------GSREAFYrAVLLLLlLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 802 KVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFL 881
Cdd:cd18572 78 SLLRQDIAFFDA--TKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 882 YMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYA 961
Cdd:cd18572 156 YGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQV 235
|
250
....*....|....
gi 1063707070 962 ASFYVGARLVDDGK 975
Cdd:cd18572 236 LVLFYGGHLVLSGR 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
384-607 |
4.20e-31 |
|
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: 122.68 E-value: 4.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI---NLKEFQLKWIRS 460
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFT-ASIKDNIAYGKEDATT-----------EEIKAAAELanaskfVDKLpqGLDTMVGEHGTQLSGGQK 528
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRRStwrslfglfpkEEKQRALAA------LERV--GLLDKAYQRADQLSGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVR-NADMIAVIHQGKIVEKGSHT 605
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230
|
..
gi 1063707070 606 EL 607
Cdd:cd03256 231 EL 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
384-623 |
6.57e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 6.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK--EFQLKWIRSK 461
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLF---TASikDNIAYGKEDaTTEEIKAAAElANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK09493 79 AGMVFQQFYLFphlTAL--ENVMFGPLR-VRGASKEEAE-KQARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 539 KDPRILLLDEATSALDAESE----RVVQEALDRIMvnrTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEg 613
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRhevlKVMQDLAEEGM---TMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPP- 228
|
250
....*....|
gi 1063707070 614 aySQliRLQE 623
Cdd:PRK09493 229 --SQ--RLQE 234
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
385-578 |
1.10e-30 |
|
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: 120.05 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARPDeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLkwiRSKIGL 464
Cdd:cd03226 1 RIENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQEP--VLFTASIKDNIAYGKEDAtteeikaAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKEL-------DAGNEQAETVLKDL--DLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063707070 543 ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA 578
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVI 182
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
384-578 |
1.84e-30 |
|
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: 119.82 E-value: 1.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI---NLKEFQLKWIRS 460
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQE-PVLFTASIKDNIAYGKE--DATTEEI----KAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAV 533
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEvtGVPPREIrkrvPAALELVGLSHKHRALPA-----------ELSGGEQQRVAI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063707070 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA 578
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
384-612 |
3.81e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.06 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGD---VLIDGINLKEFQLKWIRS 460
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEP--VLFTASIKDNIAYGKED---ATTEEIKAAAELAN---ASKFVDKLPQgldtmvgehgtQLSGGQKQRIA 532
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENravPRPEMIKIVRDVLAdvgMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMV--NRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
..
gi 1063707070 611 PE 612
Cdd:PRK13640 234 VE 235
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
384-612 |
1.28e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTY-PARPDEQI-FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL--KEFQLKWIR 459
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SKIGLVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANAS--KFVDKLPqgldtmvgehgTQLSGGQKQ 529
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGpinlglSEEEIENRVKRAMNIVGLDyeDYKDKSP-----------FELSGGQKR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALDAESErvvQEALDRIM-----VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGS 603
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
....*....
gi 1063707070 604 HTELLKDPE 612
Cdd:PRK13637 229 PREVFKEVE 237
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
385-598 |
1.91e-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: 116.86 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFqlkwiRSKIGL 464
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQEPVL---FTASIKDNIA------------YGKEDAttEEIKAAAELANASKFVDKlpqgldtmvgeHGTQLSGGQKQ 529
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLmglyghkglfrrLSKADK--AKVDEALERVGLSELADR-----------QIGELSGGQQQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTV-RNADMIAVIHQGKI 598
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
384-649 |
2.29e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.55 E-value: 2.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYP-ARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF-QLKWIRSK 461
Cdd:PRK13644 2 IRLENVSYSYPdGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEP--VLFTASIKDNIAYGKEDATTE--EIKAAAELANASKfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEI-------GLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY- 615
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTl 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1063707070 616 ----SQLIRLQEEKKSDENAAEEQKMSSIESFKQSSLR 649
Cdd:PRK13644 232 gltpPSLIELAENLKMHGVVIPWENTSSPSSFAEEICR 269
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
112-322 |
3.75e-29 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 118.41 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 112 LGIGTFAAAFLqlSGW-----MISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAI 186
Cdd:cd18572 42 LLLLSVLSGLF--SGLrggcfSYAGTRLVRRLRRDLFRSLLRQDIAFFD-ATKTGELTSRLTSDCQKVSDPLSTNLNVFL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 187 QLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAI 266
Cdd:cd18572 119 RNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 267 SNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQ 322
Cdd:cd18572 199 RRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
404-602 |
5.66e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 115.47 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFIS---SGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWI----RSKIGLVSQEPVLFT-AS 475
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRKIGLVFQQYALFPhLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGKEDATTEEIKaaaelanasKFVDKLPQ--GLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:cd03297 92 VRENLAFGLKRKRNREDR---------ISVDELLDllGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 554 DAESERVVQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03297 163 DRALRLQLLPELKQIKknLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
68-345 |
8.64e-29 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 117.23 E-value: 8.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 68 LGSIGNGLGFPLmtlLFGDLIDAFGENQTNTTD-KVSKVALKFVWLGIGTFAAAFLQLSGWM--ISGERQAARIRSLYLK 144
Cdd:cd18573 6 LVSSAVTMSVPF---AIGKLIDVASKESGDIEIfGLSLKTFALALLGVFVVGAAANFGRVYLlrIAGERIVARLRKRLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 145 TILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALL 224
Cdd:cd18573 83 SILRQDAAFFD-KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 225 AIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYAL 304
Cdd:cd18573 162 GRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLS 241
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063707070 305 AVWYGGKLILDKGYTGGQVLNIII-AVLTGSmSLGQTSPCLS 345
Cdd:cd18573 242 VLYYGGSLVASGELTVGDLTSFLMyAVYVGS-SVSGLSSFYS 282
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
383-612 |
1.39e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 116.66 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 383 DIELKDVYFTYPAR-PdeqiFRGFSLF-----ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KE 452
Cdd:PRK13634 2 DITFQKVEHRYQYKtP----FERRALYdvnvsIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 453 FQLKWIRSKIGLVSQ--EPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdklpqGLDTMVGEHGT-QLSGGQKQ 529
Cdd:PRK13634 78 KKLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV-----GLPEELLARSPfELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTE 606
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
|
....*.
gi 1063707070 607 LLKDPE 612
Cdd:PRK13634 233 IFADPD 238
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
384-612 |
1.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.35 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEP--VLFTASIKDNIAYGKED---ATTEEIKAAAELANASKFVDklpqgldtMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgiPREEMIKRVDEALLAVNMLD--------FKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 539 KDPRILLLDEATSALD----AESERVVQEALDRIMVnrTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13642 157 LRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
384-602 |
1.60e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 114.21 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTvALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEP-----------VLFTASIKDnIAYGKEDAtteEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIA 532
Cdd:cd03264 76 YLPQEFgvypnftvrefLDYIAWLKG-IPSKEVKA---RVDEVLELVNLGDRAKKKIG-----------SLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
398-612 |
3.70e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 114.46 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG-----DVLIDG---INLKEFQLKWIRSKIGLVSQEP 469
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarsLSQQKGLIRQLRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 470 VLFT-ASIKDNIAYGKEdATTEEIKAAAElANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK11264 95 NLFPhRTVLENIIEGPV-IVKGEPKEEAT-ARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 549 ATSALDAEserVVQEALDRIMV----NRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK11264 171 PTSALDPE---LVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
384-663 |
6.30e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 122.15 E-value: 6.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIdginlkefqlkwIRSKIG 463
Cdd:PLN03130 615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIAYGKE-DATTEEikAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PLN03130 683 YVPQVSWIFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 543 ILLLDEATSALDAESER-VVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEgAYSQLIR- 620
Cdd:PLN03130 761 VYIFDDPLSALDAHVGRqVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGP-LFQKLMEn 839
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1063707070 621 --LQEEKKSDENAAEEQKMSS--IESFKQSSLRKSSLGRSLSKGGSS 663
Cdd:PLN03130 840 agKMEEYVEENGEEEDDQTSSkpVANGNANNLKKDSSSKKKSKEGKS 886
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
404-611 |
9.44e-28 |
|
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: 115.98 E-value: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSL---FISSGTTV-ALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEFQLKWIRSKIGLVSQEPVLFT-A 474
Cdd:TIGR02142 11 DFSLdadFTLPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 SIKDNIAYGKEDATTEEIKAAAElanasKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:TIGR02142 91 SVRGNLRYGMKRARPSERRISFE-----RVIELL--GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 555 AESERVVQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:TIGR02142 164 DPRKYEILPYLERLHaeFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
401-619 |
1.29e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 121.42 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNI 480
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AYGKEdATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK-DPRILLLDEATSALDAESER 559
Cdd:PTZ00243 1405 DPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDR 1483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 560 VVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLI 619
Cdd:PTZ00243 1484 QIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMV 1543
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
720-977 |
1.62e-27 |
|
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: 113.35 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPkkLKEDTSFWAIIFMVLGFASIIaypaQTFFFAIAGCKLVQRIRSMC 799
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTAS--LNQIALLLLGLFLLQAVFSFF----RIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:cd18576 76 YRHLQRLPLSFFHE--RRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSS 959
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250
....*....|....*...
gi 1063707070 960 YAASFYVGARLVDDGKTT 977
Cdd:cd18576 234 IVAVLWYGGRLVLAGELT 251
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
393-891 |
2.96e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 120.27 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 393 YPARPDEqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginlkefqlkWIRSKIGLVSQEPVLF 472
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 473 TASIKDNIAYGKEDAtteeikaAAELANASKF------VDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PTZ00243 734 NATVRGNILFFDEED-------AARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 547 DEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDP--EGAYSQLIRLQE 623
Cdd:PTZ00243 807 DDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSlyATLAAELKENKD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 624 EKKSDENaAEEQKMSSIESFKQSSLRKSSLGRSLSKGGSSRgnssrhsfnmfGFPAgIDGNVVQDQEEDDTTQP-KTepk 702
Cdd:PTZ00243 887 SKEGDAD-AEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGA-----------ALDA-AAGRLMTREEKASGSVPwST--- 950
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 703 KVSIFRIAAlnkpeipvlilgsiSAAANGVILPIFG----ILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYP 778
Cdd:PTZ00243 951 YVAYLRFCG--------------GLHAAGFVLATFAvtelVTVSSGVWLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVP 1016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 779 AQTFFFAIA---GCKLVQRIrsmCFEKVVHMEVGWFDepENSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLI 855
Cdd:PTZ00243 1017 LRFFLSYEAmrrGSRNMHRD---LLRSVSRGTMSFFD--TTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSIL 1091
|
490 500 510
....*....|....*....|....*....|....*.
gi 1063707070 856 IAFLAcwqLAFVVLAMLPLialnGFLYMKFMKGFSA 891
Cdd:PTZ00243 1092 VTSAS---QPFVLVALVPC----GYLYYRLMQFYNS 1120
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
406-615 |
4.75e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.75 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF---QLKWIR-SKIGLVSQEPVLFT-ASIKDNI 480
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRrKKIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AYGKEDATTeeikAAAElaNASKFVDKLPQ-GLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:PRK10070 128 AFGMELAGI----NAEE--RREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 560 VVQEALDRIMV--NRTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK10070 202 EMQDELVKLQAkhQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
402-612 |
6.75e-27 |
|
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: 113.27 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGFSL-----FISSGTTvALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDG---------INLK-EfqlkwiRSKIG 463
Cdd:COG4148 11 RGGFTLdvdftLPGRGVT-ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGevlqdsargIFLPpH------RRRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLF-TASIKDNIAYGkedatteeIKAAAELANASKF---VDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:COG4148 81 YVFQEARLFpHLSVRGNLLYG--------RKRAPRAERRISFdevVELL--GIGHLLDRRPATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 540 DPRILLLDEATSALDAES--------ERVVQEAldRIMVnrttVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:COG4148 151 SPRLLLMDEPLAALDLARkaeilpylERLRDEL--DIPI----LYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLSR 224
|
..
gi 1063707070 611 PE 612
Cdd:COG4148 225 PD 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
406-611 |
8.22e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.89 E-value: 8.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIGLVSQEPVLFT-ASIKDNIAYG- 483
Cdd:PRK11432 26 NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPhMSLGENVGYGl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 484 ------KEDaTTEEIKAAAELANASKFVDKLpqgLDtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:PRK11432 104 kmlgvpKEE-RKQRVKEALELVDLAGFEDRY---VD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 558 ERVVQEALDRIM--VNRTTVVVAHRLS---TVrnADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK11432 172 RRSMREKIRELQqqFNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-612 |
1.06e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.00 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVS----LIERFYDPQ-AGDVLIDGINLKEFQLKWI 458
Cdd:PRK14247 4 IEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 459 RSKIGLVSQEP-VLFTASIKDNIAYG-------KEDATTEE-IKAAAELAnasKFVDKLPQGLDTMVGehgtQLSGGQKQ 529
Cdd:PRK14247 81 RRRVQMVFQIPnPIPNLSIFENVALGlklnrlvKSKKELQErVRWALEKA---QLWDEVKDRLDAPAG----KLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
....
gi 1063707070 609 KDPE 612
Cdd:PRK14247 234 TNPR 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
384-610 |
1.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.02 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTY-PARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEFQLKW 457
Cdd:PRK13646 3 IRFDNVSYTYqKGTPYEhQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 458 IRSKIGLVSQ--EPVLFTASIKDNIAYGKED--ATTEEIKAAA-----ELANASKFVDKLPqgldtmvgehgTQLSGGQK 528
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYAhrllmDLGFSRDVMSQSP-----------FQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 529 QRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMV--NRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHT 605
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPK 231
|
....*
gi 1063707070 606 ELLKD 610
Cdd:PRK13646 232 ELFKD 236
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
384-611 |
1.25e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 113.12 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefQLKWIRSKIG 463
Cdd:PRK09452 15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFT-ASIKDNIAYGKEDATTEEIKAAAELANASKFVDklpqgLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQ-----LEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 543 ILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAH----RLSTvrnADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQrkLGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
60-310 |
1.38e-26 |
|
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: 110.60 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIGnGLGFPLMTllfGDLIDAFGENQTNTTdkvskvalkFVWLGIGTF-AAAFLQ-LSGWMIS--GERQA 135
Cdd:cd18551 2 ILALLLSLLGTAA-SLAQPLLV---KNLIDALSAGGSSGG---------LLALLVALFlLQAVLSaLSSYLLGrtGERVV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 136 ARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIP 215
Cdd:cd18551 69 LDLRRRLWRRLLRLPVSFFD-RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 216 LLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLF 295
Cdd:cd18551 148 LAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMG 227
|
250
....*....|....*
gi 1063707070 296 LVVFCSYALAVWYGG 310
Cdd:cd18551 228 LAVQLALLVVLGVGG 242
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
60-341 |
1.64e-26 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 110.65 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIGNGLGFplmtllfgdLIDA-FGENQTNTTDKvSKVALKFVWLGIGTFAAAFLQLSGWMisGERQAARI 138
Cdd:cd18575 4 ALLIAAAATLALGQGLRL---------LIDQgFAAGNTALLNR-AFLLLLAVALVLALASALRFYLVSWL--GERVVADL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 139 RSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLV 218
Cdd:cd18575 72 RKAVFAHLLRLSPSFFE-TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 219 MAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVV 298
Cdd:cd18575 151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLV 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1063707070 299 FCSYALAVWYGGKLILDKGYTGGQVLNIII-AVLTGSmSLGQTS 341
Cdd:cd18575 231 FGAIVFVLWLGAHDVLAGRMSAGELSQFVFyAVLAAG-SVGALS 273
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
395-592 |
2.96e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.18 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWiRSKIGLVSQEPVLFTA 474
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 -SIKDNIAY----GKEDATTEEIKAAAELANaskfvdkLPQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:COG4133 90 lTVRENLRFwaalYGLRADREAIDEALEAVG-------LAGLADLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1063707070 550 TSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRNADMIAV 592
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
398-623 |
7.43e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 107.75 E-value: 7.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN----------LKEF---QLKWIRSKIGL 464
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLKVAdknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQEPVLFT-ASIKDNIAYGKEDATTEEIKAAAElaNASKFVDKLpqGLDTMV-GEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PRK10619 97 VFQHFNLWShMTVLENVMEAPIQVLGLSKQEARE--RAVKYLAKV--GIDERAqGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 543 ILLLDEATSALDAEserVVQEALdRIMVN-----RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAys 616
Cdd:PRK10619 173 VLLFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQSP-- 246
|
....*..
gi 1063707070 617 qliRLQE 623
Cdd:PRK10619 247 ---RLQQ 250
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
404-617 |
1.30e-25 |
|
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: 112.47 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKST----VVSLIerfydPQAGDVLIDGIN---LKEFQLKWIRSKIGLVSQEPvlFTA-- 474
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDldgLSRRALRPLRRRMQVVFQDP--FGSls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 ---SIKDNIAYG------KEDATTEEIKAAAELANAskfvdklpqGLD-TMVGEHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:COG4172 377 prmTVGQIIAEGlrvhgpGLSAAERRARVAEALEEV---------GLDpAARHRYPHEFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 545 LLDEATSALDaeseRVVQ----EALDRIMVNR--TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:COG4172 448 VLDEPTSALD----VSVQaqilDLLRDLQREHglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTR 523
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
382-610 |
1.69e-25 |
|
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: 107.25 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFTYpARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDGINLKEFQLKWIRSK 461
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNI-AYGKEdaTTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 541 PRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-617 |
1.99e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.67 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF---YDPQA---GDVLIDGINLKEFQLKWIRSKIGLVSQEPVL 471
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKIkvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 FT-ASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEAT 550
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 551 SALDAESERVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSPKNELTE 249
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
406-616 |
2.02e-25 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 109.54 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKefQLKWIRSKIGLVSQEPVLFT-ASIKDNIAYG- 483
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFPhMTVEQNIAFGl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 484 KEDATTE-EIKAAAE----LANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE-S 557
Cdd:PRK11607 117 KQDKLPKaEIASRVNemlgLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 558 ERVVQEALDRI-MVNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYS 616
Cdd:PRK11607 186 DRMQLEVVDILeRVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
379-624 |
2.29e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.40 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 379 DIKGDIELKDVYFTYPAR-PDEqiFRGF---SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG----INL 450
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKtPFE--FKALnntSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 451 KEF-QLKWIRSKIGLVSQEP--VLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdKLPQgldTMVGEHGTQLSGGQ 527
Cdd:PRK13645 80 KKIkEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPE---DYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVN--RTTVVVAHRLSTV-RNADMIAVIHQGKIVEKG-- 602
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGsp 235
|
250 260 270
....*....|....*....|....*....|
gi 1063707070 603 ----SHTELLK----DPEGAYSQLIRLQEE 624
Cdd:PRK13645 236 feifSNQELLTkieiDPPKLYQLMYKLKNK 265
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
4.33e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 105.93 E-value: 4.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSK 461
Cdd:PRK13639 2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAV 533
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
.
gi 1063707070 612 E 612
Cdd:PRK13639 229 E 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
384-613 |
4.50e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.99 E-value: 4.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYpaRPDEQI-FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKI 462
Cdd:PRK13648 8 IVFKNVSFQY--QSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPV-LFTASI-KDNIAYGKE------DATTEEIKAAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAVA 534
Cdd:PRK13648 86 GIVFQNPDnQFVGSIvKYDVAFGLEnhavpyDEMHRRVSEALKQVDMLERADYEPNAL-----------SGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
.
gi 1063707070 613 G 613
Cdd:PRK13648 235 E 235
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
384-599 |
6.78e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 105.17 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFT-YPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQlkwi 458
Cdd:COG1101 2 LELKNLSKTfNPGTVNEkRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 459 RSK-IGLVSQEPVLFTA---SIKDN--IAYGKEDA-------TTEEIKAAAELanaskfVDKLPQGL----DTMVGehgt 521
Cdd:COG1101 78 RAKyIGRVFQDPMMGTApsmTIEENlaLAYRRGKRrglrrglTKKRRELFREL------LATLGLGLenrlDTKVG---- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 522 QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRImVNR---TTVVVAHRLS-TVRNADMIAVIHQGK 597
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKI-VEEnnlTTLMVTHNMEqALDYGNRLIMMHEGR 226
|
..
gi 1063707070 598 IV 599
Cdd:COG1101 227 II 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
384-602 |
9.63e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 103.34 E-value: 9.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqiFRgFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIG 463
Cdd:cd03298 1 VRLDKIRFSYGEQP----MH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFT-ASIKDNIAYGKEDAT--TEEIKAAAELANASkfvdklpQGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGLklTAEDRQAIEVALAR-------VGLAGLEKRLPGELSGGERQRVALARVLVRD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 541 PRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03298 147 KPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
384-596 |
1.75e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 102.79 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK-- 461
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 --IGLVSQEPVLFTASIKDNIAYGKEdATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:cd03290 79 ysVAYAAQKPWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 540 DPRILLLDEATSALDAE-SERVVQEALDRIMVN--RTTVVVAHRLSTVRNADMIAVIHQG 596
Cdd:cd03290 158 NTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
404-617 |
2.34e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.05 E-value: 2.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKSTV---VSLIERfydPQAGDVLIDGINLKEF---QLKWIRSKIGLVSQEPvlftasik 477
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNP-------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 478 dniaYG------KEDATTEE-------IKAAAELANASKFVDKLpqGLDTmvgEHGTQ----LSGGQKQRIAVARAILKD 540
Cdd:PRK11308 102 ----YGslnprkKVGQILEEpllintsLSAAERREKALAMMAKV--GLRP---EHYDRyphmFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 541 PRILLLDEATSALDAEservVQ-EALDRIM-----VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEG 613
Cdd:PRK11308 173 PDVVVADEPVSALDVS----VQaQVLNLMMdlqqeLGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNPRH 248
|
....
gi 1063707070 614 AYSQ 617
Cdd:PRK11308 249 PYTQ 252
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
384-657 |
2.38e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 110.84 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVS--LIERfydPQAGDVLIDginlkefqlkwIRSK 461
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISamLGEL---SHAETSSVV-----------IRGS 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNIAYGkEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:PLN03232 681 VAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 542 RILLLDEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEgAYSQLIR 620
Cdd:PLN03232 760 DIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGS-LFKKLME 838
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1063707070 621 -------LQEEKKSDENAAEEQKMSSIESFKQS--SLRKSSLGRSL 657
Cdd:PLN03232 839 nagkmdaTQEVNTNDENILKLGPTVTIDVSERNlgSTKQGKRGRSV 884
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
403-603 |
2.54e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.71 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD--PQA---GDVLIDGINL--KEFQLKWIRSKIGLVSQEPVLFTAS 475
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGKE--------DATTEEIKAAAELANASKfvDKLPQGldtmvgehGTQLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:PRK14243 107 IYDNIAYGARingykgdmDELVERSLRQAALWDEVK--DKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 548 EATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQgKIVEKGS 603
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFNV-ELTEGGG 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
384-607 |
2.97e-24 |
|
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: 102.20 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:cd03263 1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTA-SIKDNIAY-----GKEDatTEEIKAAAELANASKFVDKLpqglDTMVGehgtQLSGGQKQRIAVARAI 537
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPK--SEIKEEVELLLRVLGLTDKA----NKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
384-624 |
3.12e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.86 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAG-DVLIDGINLKEFQLKWIRSKI 462
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVS---QEPVLFTASIKDNIAYGKED-------ATTEEIKAAAELANASkfvdklpqGLDTMVGEHGTQLSGGQKQRIA 532
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyrePTDEQRERARELLELL--------GLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVN--RTTVVVAHRLStvrnaDMIAVIH------QGKIVEKGSH 604
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVE-----EIPPGIThvlllkDGRVVAAGPK 227
|
250 260
....*....|....*....|..
gi 1063707070 605 TELLKDP--EGAYSQLIRLQEE 624
Cdd:COG1119 228 EEVLTSEnlSEAFGLPVEVERR 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
382-580 |
3.24e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 382 GDIELKDVYFtypARPDEQ-IFRGFSLFISSGTTVALVGQSGSGKSTVV-SL----------IERfydPQAGDVLidgin 449
Cdd:COG4178 361 GALALEDLTL---RTPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTLLrAIaglwpygsgrIAR---PAGARVL----- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 450 lkefqlkwirskigLVSQEPVLFTASIKDNIAY--GKEDATTEEIKAAAELANASKFVDKLPQGLDTmvgehGTQLSGGQ 527
Cdd:COG4178 430 --------------FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGE 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 528 KQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVAHR 580
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
384-608 |
3.81e-24 |
|
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: 102.96 E-value: 3.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYP------ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF---Q 454
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 455 LKWIRSKIGLVSQE-PVLFTA--SIKDNIA-----YGKEDATTEEIKAAAELANA---SKFVDKLPQgldtmvgehgtQL 523
Cdd:TIGR02769 83 RRAFRRDVQLVFQDsPSAVNPrmTVRQIIGeplrhLTSLDESEQKARIAELLDMVglrSEDADKLPR-----------QL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 524 SGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTT--VVVAHRLSTV-RNADMIAVIHQGKIVE 600
Cdd:TIGR02769 152 SGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
....*...
gi 1063707070 601 KGSHTELL 608
Cdd:TIGR02769 232 ECDVAQLL 239
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
725-977 |
4.84e-24 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 103.33 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 725 ISAAANGVIlpifGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFAsiIAYPAQTFFFAIAGCKLVQRIRSMCFEKVV 804
Cdd:cd18575 7 IAAAATLAL----GQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLA--LASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 805 HMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18575 81 RLSPSFFET--TRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 885 FMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASF 964
Cdd:cd18575 159 RVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVL 238
|
250
....*....|...
gi 1063707070 965 YVGARLVDDGKTT 977
Cdd:cd18575 239 WLGAHDVLAGRMS 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
384-610 |
4.92e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 4.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPA-RPdeqiFRGFSLF-----ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEF 453
Cdd:PRK13649 3 INLQNVSYTYQAgTP----FEGRALFdvnltIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 454 QLKWIRSKIGLVSQ--EPVLFTASIKDNIAYG-------KEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLS 524
Cdd:PRK13649 79 DIKQIRKKVGLVFQfpESQLFEETVLKDVAFGpqnfgvsQEEAEALAREKLALVGISESLFEKNP-----------FELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
....*...
gi 1063707070 603 SHTELLKD 610
Cdd:PRK13649 228 KPKDIFQD 235
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
399-602 |
4.95e-24 |
|
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: 100.70 E-value: 4.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 399 EQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI--ERFYDPQAGDVLIDGINLKefqLKWIRSKIGLVSQEPVLF-TAS 475
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHpTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYgkedatteeikaAAELanaskfvdklpQGldtmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:cd03213 99 VRETLMF------------AAKL-----------RG-----------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 556 ESERVVQEALdRIMV--NRTTVVVAHRLST--VRNADMIAVIHQGKIVEKG 602
Cdd:cd03213 145 SSALQVMSLL-RRLAdtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
400-612 |
5.21e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 104.78 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKIGLVSQEPVLFT-ASIKD 478
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 479 NIAYG------KEDATTEEIKAAA----ELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK10851 94 NIAFGltvlprRERPNAAAIKAKVtqllEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 549 ATSALDAEservVQEALDRIM------VNRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK10851 163 PFGALDAQ----VRKELRRWLrqlheeLKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
400-617 |
5.42e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 107.46 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKS----TVVSLIERFYDPQAGDVLIDGINL---KEFQLKWIR-SKIGLVSQEPV- 470
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgNRIAMIFQEPMt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 ----LFTasIKDNIA--------YGKEDATTEEIKAAAE--LANASKFVDKLPqgldtmvgeHgtQLSGGQKQRIAVARA 536
Cdd:COG4172 104 slnpLHT--IGKQIAevlrlhrgLSGAAARARALELLERvgIPDPERRLDAYP---------H--QLSGGQRQRVMIAMA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 537 ILKDPRILLLDEATSALDAeserVVQ----EALDRIMVNRTTVVV--AHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4172 171 LANEPDLLIADEPTTALDV----TVQaqilDLLKDLQRELGMALLliTHDLGVVRRfADRVAVMRQGEIVEQGPTAELFA 246
|
....*...
gi 1063707070 610 DPEGAYSQ 617
Cdd:COG4172 247 APQHPYTR 254
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
763-977 |
8.65e-24 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 102.77 E-value: 8.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 763 AIIFM-VLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLA 841
Cdd:cd18784 38 AIIIMgLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDT--VKTGDITSRLTSDTTTMSDTVSLNLN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 842 QTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18784 116 IFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 922 KVMNMYSKKCEGPMKNGIRQGIVSGiGFGFSFFVLFSSYAAS-FYVGARLVDDGKTT 977
Cdd:cd18784 196 GEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELALTVStLYYGGHLVITGQIS 251
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
416-612 |
9.71e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.39 E-value: 9.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 416 ALVGQSGSGKSTVVSLIERFYD--PQ---AGDVLIDGINLKEFQLKW--IRSKIGLVSQEPVLFTASIKDNIAYG----- 483
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPMSIYENVVYGlrlkg 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 484 ---KE--DATTEEIKAAAELANASKfvDKLPqglDTMVGehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:PRK14239 115 ikdKQvlDEAVEKSLKGASIWDEVK--DRLH---DSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISA 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 559 RVVQEALDRIMVNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK14239 185 GKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
400-610 |
1.31e-23 |
|
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: 100.20 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLkwIRSKIGLVSQEPVLF-TAS 475
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrdiTGLPPHER--ARAGIGYVPEGRRIFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGKEDATTEEIKAAAElanasKFVDKLPQgLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALda 555
Cdd:cd03224 92 VEENLLLGAYARRRAKRKARLE-----RVYELFPR-LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL-- 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 556 eSERVVQEALDRIM-VNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:cd03224 164 -APKIVEEIFEAIReLRDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
403-612 |
1.54e-23 |
|
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: 100.59 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQlkwiRSKIGLVS--QEPVLFTA-SI 476
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGediTGLPPHE----IARLGIGRtfQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 477 KDNIAYG---------KEDATTEEIKAAAELANAS-KFVdKLPQGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLL 546
Cdd:cd03219 93 LENVMVAaqartgsglLLARARREEREARERAEELlERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 547 DEATSAL-DAESERVVqEALDRIMV-NRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:cd03219 168 DEPAAGLnPEETEELA-ELIRELRErGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
63-322 |
1.64e-23 |
|
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: 101.86 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQTNTTdkvskvalkFVWLGIGTFAAAFLQ-----LSGWMIS--GERQA 135
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL---------LLWIALLLLLLALLRallsyLRRYLAArlGQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 136 ARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIP 215
Cdd:cd07346 72 FDLRRDLFRHLQRLSLSFFD-RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 216 LLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLF 295
Cdd:cd07346 151 LYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
|
250 260
....*....|....*....|....*..
gi 1063707070 296 LVVFCSYALAVWYGGKLILDKGYTGGQ 322
Cdd:cd07346 231 LLTALGTALVLLYGGYLVLQGSLTIGE 257
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
395-608 |
2.53e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.92 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF---QLKWIRSKIGLVSQEPvl 471
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDS-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 FTA-----SIKDNIAY----------GKEDATTEEIKAAAELANAskFVDKLPQgldtmvgehgtQLSGGQKQRIAVARA 536
Cdd:PRK10419 99 ISAvnprkTVREIIREplrhllsldkAERLARASEMLRAVDLDDS--VLDKRPP-----------QLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 537 ILKDPRILLLDEATSALDaeseRVVQ----EALDRIMVNRTT--VVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQagviRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVETQPVGDKL 240
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
384-605 |
2.57e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.09 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPArpdEQIFRGFSLFISSGTTVALVGQSGSGKST---VVSLIERfydPQAGDVLIDGINL------KEFQ 454
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNHFdfsktpSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 455 LKWIRSKIGLVSQE----PVLftaSIKDNI--------AYGKEDATTEEIKAAAELaNASKFVDKLPQgldtmvgehgtQ 522
Cdd:PRK11124 77 IRELRRNVGMVFQQynlwPHL---TVQQNLieapcrvlGLSKDQALARAEKLLERL-RLKPYADRFPL-----------H 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 523 LSGGQKQRIAVARAILKDPRILLLDEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVE 600
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVE 221
|
....*
gi 1063707070 601 KGSHT 605
Cdd:PRK11124 222 QGDAS 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
384-612 |
3.63e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.55 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYpARPDEQIFR----GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW-I 458
Cdd:PRK13633 5 IKCKNVSYKY-ESNEESTEKlaldDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 459 RSKIGLVSQEP--VLFTASIKDNIAYGKED--ATTEEIKAAAELA----NASKFVDKLPQgldtmvgehgtQLSGGQKQR 530
Cdd:PRK13633 84 RNKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 531 IAVARAILKDPRILLLDEATSALDAESERvvqEALDRIM-VNR----TTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHT 605
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRR---EVVNTIKeLNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*..
gi 1063707070 606 ELLKDPE 612
Cdd:PRK13633 230 EIFKEVE 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
384-612 |
3.90e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTY-PARPDEQI-FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG----INLKEFQLKW 457
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 458 IRSKIGLVSQ--EPVLFTASIKDNIAYGKED--ATTEEIKAAAelanaSKFVDKLpqGLDTMVGEHGT-QLSGGQKQRIA 532
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKA-----LKWLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAES-ERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
..
gi 1063707070 611 PE 612
Cdd:PRK13641 236 KE 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-612 |
3.99e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.92 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYD--PQA---GDVLIDGINLKEFQLKWI--RSKIGLVSQEPV 470
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSPDVDPIevRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 LFT-ASIKDNIAYGKEdaTTEEIKAAAELANASKFVDK---LPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PRK14267 96 PFPhLTIYDNVAIGVK--LNGLVKSKKELDERVEWALKkaaLWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 547 DEATSALDAESERVVQEALDRIMVNRTTVVVAHR-LSTVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPE 240
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
384-602 |
4.34e-23 |
|
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: 98.59 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTY-PARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwIRSKI 462
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE-ARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPVLFT-ASIKDNIAY-----G-KEDATTEEIKAAAELANASKFVDKLPQGLDTmvgehgtqlsgGQKQRIAVAR 535
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfaglyGlKGDELTARLEELADRLGMEELLDRRVGGFST-----------GMRQKVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03266 150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
385-556 |
5.45e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.94 E-value: 5.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEFQLKwiRSK 461
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFT-ASIKDNIAYG-KEDATTEEIKAAAE--LANAskfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFAlPPTIGRAQRRARVEqaLEEA---------GLAGFADRDPATLSGGQRARVALLRAL 148
|
170
....*....|....*....
gi 1063707070 538 LKDPRILLLDEATSALDAE 556
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAA 167
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
384-599 |
1.02e-22 |
|
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: 95.57 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPArpdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwirskig 463
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 lvsqEPVLFtASIKDNIAYGKEdatteeikaaaelanaskfvdklpqgldtMVgehgTQLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03216 62 ----KEVSF-ASPRDARRAGIA-----------------------------MV----YQLSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 544 LLLDEATSAL-DAESERVVqEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIV 599
Cdd:cd03216 104 LILDEPTAALtPAEVERLF-KVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
384-594 |
1.12e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLFTASIKDNIA--YGKEDATTEEIKAAAELAnasKFvdKLPqglDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLE---RF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 542 RILLLDEATSALDAESERVVQEALDRIMVNRTTVV--VAHRLSTVRNADmiAVIH 594
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVlwVTHDKDEINHAD--KVIT 209
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-652 |
1.13e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 105.38 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwirsKIGLVSQEPVLFTASIKDNI 480
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AYG---KEDATTEEIKAAAELANASKFvdklPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:TIGR01271 508 IFGlsyDEYRYTSVIKACQLEEDIALF----PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 558 ERVVQEA-LDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIRLQEekkSDENAAEEQK 636
Cdd:TIGR01271 584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEA---FDNFSAERRN 660
|
250
....*....|....*.
gi 1063707070 637 MSSIESFKQSSLRKSS 652
Cdd:TIGR01271 661 SILTETLRRVSIDGDS 676
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
384-608 |
1.32e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTY---PARpdeqifrgFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRS 460
Cdd:PRK10771 2 LKLTDITWLYhhlPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFT-ASIKDNIAYGKE------DATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAV 533
Cdd:PRK10771 72 PVSMLFQENNLFShLTVAQNIGLGLNpglklnAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
384-611 |
1.44e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.57 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPArpdEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDG--------INLKEFQL 455
Cdd:PRK14258 8 IKVNNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 456 KWIRSKIGLVSQEPVLFTASIKDNIAYGKE----------DATTEEIKAAAELANASKfvdklpqgldTMVGEHGTQLSG 525
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpkleiDDIVESALKDADLWDEIK----------HKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALD--RIMVNRTTVVVAHRLSTV-RNADMIAVIHQ-----GK 597
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQ 233
|
250
....*....|....
gi 1063707070 598 IVEKGSHTELLKDP 611
Cdd:PRK14258 234 LVEFGLTKKIFNSP 247
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
386-598 |
1.68e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 386 LKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlkwIRSKIGLV 465
Cdd:PRK11247 15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 466 SQEPVLFT-ASIKDNIAYG-KEDATTEEIKAAAELanaskfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRI 543
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGlKGQWRDAALQALAAV------------GLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKI 598
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
100-328 |
1.71e-22 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 98.92 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 100 DKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMG 179
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD-TVKTGDITSRLTSDTTTMSDTVS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 180 EKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASF 259
Cdd:cd18784 112 LNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSF 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 260 TGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVLNIII 328
Cdd:cd18784 192 ANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFIL 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
386-643 |
3.34e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 386 LKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIGLV 465
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 466 SQEPVLF-TASIKDNI----------------AYGKEDATTEEIKAAAEL-------------ANASKFVDKL---PQGL 512
Cdd:COG0488 67 PQEPPLDdDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELqeefealggweaeARAEEILSGLgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 513 DTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAEServvQEALDRIMVNR--TTVVVAH-R--LSTVrnA 587
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYpgTVLVVSHdRyfLDRV--A 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 588 DMIAVIHQGKivekgshtelLKDPEGAYS------QLIRLQEEKksdENAAEEQKMSSIESF 643
Cdd:COG0488 217 TRILELDRGK----------LTLYPGNYSayleqrAERLEQEAA---AYAKQQKKIAKEEEF 265
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
384-600 |
3.84e-22 |
|
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: 96.35 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfydPQAGDVLIDGINLkeFQL---- 455
Cdd:COG4181 9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLaglDR---PTSGTVRLAGQDL--FALdeda 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 456 --KWIRSKIGLVSQE----PVLfTAsiKDNIAY-----GKEDATTeeiKAAAELANaskfVdklpqGLDTMVGEHGTQLS 524
Cdd:COG4181 84 raRLRARHVGFVFQSfqllPTL-TA--LENVMLplelaGRRDARA---RARALLER----V-----GLGHRLDHYPAQLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRimVNR---TT-VVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFE--LNRergTTlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
384-612 |
1.35e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVAR 535
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVN--RTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
403-621 |
2.74e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIR----SKIGLVSQEPVLF-TASIK 477
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRdaqaAGIAIIHQELNLVpNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 478 DNIAYGKEDATTEEIKAAAELANASKFVDKLpqGLD----TMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:COG1129 98 ENIFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 554 -DAESER---VVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDpegaysQLIRL 621
Cdd:COG1129 172 tEREVERlfrIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTED------ELVRL 235
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
63-331 |
2.79e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 95.18 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 63 MILGTLGSIGNGLGFPLMTLLFGDLIDAFGENQtnttdkvSKVALKFVWLGI-GTFA----AAFLQ--LSGWMisGERQA 135
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEK-------DLEALLLVPLAIiGLFLlrglASYLQtyLMAYV--GQRVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 136 ARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIP 215
Cdd:cd18552 72 RDLRNDLFDKLLRLPLSFFD-RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 216 LLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGV-IEGGSTGLGLGTL 294
Cdd:cd18552 151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMkIARARALSSPLME 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 1063707070 295 FLVVFCSyALAVWYGGKLILDKGYTGGQVLNIIIAVL 331
Cdd:cd18552 231 LLGAIAI-ALVLWYGGYQVISGELTPGEFISFITALL 266
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
393-588 |
2.94e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 92.30 E-value: 2.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 393 YPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIGLVSQ---EP 469
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 470 VLFTASIKDNIAYG------------KED-ATTEEIKAA---AELANASkfvdklpqgLDTmvgehgtqLSGGQKQRIAV 533
Cdd:NF040873 68 DSLPLTVRDLVAMGrwarrglwrrltRDDrAAVDDALERvglADLAGRQ---------LGE--------LSGGQRQRALL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 534 ARAILKDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAHRLSTVRNAD 588
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRAD 186
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
402-576 |
2.97e-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: 93.65 E-value: 2.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLID----GINL---KEFQLKWIRSK-IGLVSQ------ 467
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaSPREILALRRRtIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 468 ---------EPVLftasikdniAYGKEDATTEEiKAAAELA--NaskfvdkLPQGLdtmvgehgTQL-----SGGQKQRI 531
Cdd:COG4778 107 rvsaldvvaEPLL---------ERGVDREEARA-RARELLArlN-------LPERL--------WDLppatfSGGEQQRV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063707070 532 AVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV 576
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-610 |
3.69e-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: 100.37 E-value: 3.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTASIKDNI 480
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AyGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERV 560
Cdd:TIGR01271 1313 D-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQI 1391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063707070 561 VQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:TIGR01271 1392 IRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
720-982 |
3.70e-21 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 94.80 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVILPIFGILISSVIKAffqppkklKEDTSFWAIIFMVLGFASI--IAYPAQTFFFAIAGCKLVQRIRS 797
Cdd:cd18552 5 ILGMILVAATTAALAWLLKPLLDDIFVE--------KDLEALLLVPLAIIGLFLLrgLASYLQTYLMAYVGQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 798 MCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIAL 877
Cdd:cd18552 77 DLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 878 NGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLF 957
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGA 234
|
250 260
....*....|....*....|....*
gi 1063707070 958 SSYAASFYVGARLVDDGKTTFDSVF 982
Cdd:cd18552 235 IAIALVLWYGGYQVISGELTPGEFI 259
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
384-610 |
4.06e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 4.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQlKWIRSKI- 462
Cdd:PRK13548 3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWS-PAELARRr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPVL-FTASIKDNIAYGKEDATTEEIKAAAELANASKFVDklpqgLDTMVGEHGTQLSGGQKQRIAVARAIL--- 538
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVD-----LAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 539 ---KDPRILLLDEATSALD-AESERVVQEALDRIMVNRTTV-VVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAViVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTP 231
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
401-607 |
4.71e-21 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 94.54 E-value: 4.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwirsKIGLVSQEPVLFTASIKDNI 480
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AYG---KEDATTEEIKAAAELANASKFVDKLpqglDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:cd03291 119 IFGvsyDEYRYKSVVKACQLEEDITKFPEKD----NTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 558 ERVVQEA-LDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
384-568 |
9.71e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.00 E-value: 9.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPA-RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlKWIR--- 459
Cdd:COG4525 4 LTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG--------VPVTgpg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SKIGLVSQEPVLFT-ASIKDNIAYGKEDATteeIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:COG4525 76 ADRGVVFQKDALLPwLNVLDNVAFGLRLRG---VPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190
....*....|....*....|....*....|
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRI 568
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
400-617 |
1.10e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.08 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKS-TVVSLIERFYDPQA----GDVLIDGINL---KEFQLKWIR-SKIGLVSQEPV 470
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVvypsGDIRFHGESLlhaSEQTLRGVRgNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 LFTA---SIKDNIA--------YGKEDATTEEIKAAAELA--NASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAI 537
Cdd:PRK15134 103 VSLNplhTLEKQLYevlslhrgMRREAARGEILNCLDRVGirQAAKRLTDYPH-----------QLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 538 LKDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGA 614
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQqeLNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHP 251
|
...
gi 1063707070 615 YSQ 617
Cdd:PRK15134 252 YTQ 254
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
399-614 |
1.20e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 93.24 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 399 EQIFRGFSlfisSGTTVALVGQSGSGKSTVVSLIERFYDP-----QAGDVLIDGINLKEFQ-LKWIRSKIGLVSQEPVLF 472
Cdd:PRK14271 38 DQVSMGFP----ARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 473 TASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 553 LDAESERVVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDPEGA 614
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPKHA 256
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
403-612 |
1.95e-20 |
|
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: 92.02 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKE--------------FQLkwIRS-------- 460
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphriarlgiartFQN--PRLfpeltvle 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 --KIGLVSQEPVLFTASIKDNIAYGKEDATTEEikAAAELAnasKFVdklpqGLDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:COG0411 99 nvLVAAHARLGRGLLAALLRLPRARREEREARE--RAEELL---ERV-----GLADRADEPAGNLSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 539 KDPRILLLDEATSAL-DAESERVVqEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:COG0411 169 TEPKLLLLDEPAAGLnPEETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRADPR 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
384-610 |
2.63e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTY-PARPdeqiFRGFSLF-----ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL----KEF 453
Cdd:PRK13643 2 IKFEKVNYTYqPNSP----FASRALFdidleVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 454 QLKWIRSKIGLVSQEP--VLFTASIKDNIAYGKED---ATTEEIKAAAE----LANASKFVDKLPqgldtmvgehgTQLS 524
Cdd:PRK13643 78 EIKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgiPKEKAEKIAAEklemVGLADEFWEKSP-----------FELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
....*...
gi 1063707070 603 SHTELLKD 610
Cdd:PRK13643 227 TPSDVFQE 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
398-608 |
2.89e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTA-SI 476
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 477 KDNIAYGKE----------DATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PRK11231 94 RELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLADRRL-----------TDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 547 DEATSALDAeSERVVQEALDRIMVN--RTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK11231 163 DEPTTYLDI-NHQVELMRLMRELNTqgKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
405-624 |
3.46e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.44 E-value: 3.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 405 FSLfiSSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLkwiRSK-IGLVSQEPvlfTASIKDNIA 481
Cdd:COG4167 34 FTL--EAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkLEYGDYKY---RCKhIRMIFQDP---NTSLNPRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 482 YGKedaTTEE-IKAAAELaNASKFVDKLPQGLdTMVG---EHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:COG4167 106 IGQ---ILEEpLRLNTDL-TAEEREERIFATL-RLVGllpEHANfyphMLSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 554 DAeSERV--------VQEALdrimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYSQliRLQEE 624
Cdd:COG4167 181 DM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANPQHEVTK--RLIES 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
375-612 |
3.56e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 92.61 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 375 KVLDDIKGDI--ELKDVYFTYPARPDEQI--FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI-- 448
Cdd:PRK13631 11 KVPNPLSDDIilRVKNLYCVFDEKQENELvaLNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 449 ----------------NLKEFqlKWIRSKIGLVSQEP--VLFTASIKDNIAYGKEDATTEEIKAAAElanASKFVDKLpq 510
Cdd:PRK13631 91 gdkknnhelitnpyskKIKNF--KELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKL---AKFYLNKM-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 511 GLD-TMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER-VVQEALDRIMVNRTTVVVAHRLSTVRN-A 587
Cdd:PRK13631 164 GLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvA 243
|
250 260
....*....|....*....|....*
gi 1063707070 588 DMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13631 244 DEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
721-977 |
9.51e-20 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 90.95 E-value: 9.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 721 ILGSISAAANGVILP-IFGILISSVIKAFFQppkklkedTSFWAIIFMVLGFA---SIIAYpAQTFFFAIAGCKLVQRIR 796
Cdd:cd18542 5 ILALLLATALNLLIPlLIRRIIDSVIGGGLR--------ELLWLLALLILGVAllrGVFRY-LQGYLAEKASQKVAYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 797 SMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIA 876
Cdd:cd18542 76 NDLYDHLQRLSFSFHDK--ARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 877 LNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVL 956
Cdd:cd18542 154 LFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLS 233
|
250 260
....*....|....*....|.
gi 1063707070 957 FSSYAASFYVGARLVDDGKTT 977
Cdd:cd18542 234 GLQIVLVLWVGGYLVINGEIT 254
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
706-977 |
1.25e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.40 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 706 IFRIAALNKPEIPVLILGS---ISAAANGVILPIFGILISSVIKAFFQPPKKLKedtsfwAIIFM-VLGFASIIAYPAQT 781
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFvflTLSSLGEMFIPFYTGRVIDTLGGDKGPPALAS------AIFFMcLLSIASSVSAGLRG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 782 FFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLAC 861
Cdd:TIGR00958 223 GSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 862 WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQ 941
Cdd:TIGR00958 301 PRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRK 380
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1063707070 942 GIVsgigfgFSFFVLFSSYAASF------YVGARLVDDGKTT 977
Cdd:TIGR00958 381 ALA------YAGYLWTTSVLGMLiqvlvlYYGGQLVLTGKVS 416
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
717-974 |
1.45e-19 |
|
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: 90.19 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 717 IPVLILGSISAAAnGVILPIFgilISSVIKAFFqppkklKEDTSFWAIIFMVLGF-ASIIAYPAQTFFFAIAGCKLVQRI 795
Cdd:cd18551 2 ILALLLSLLGTAA-SLAQPLL---VKNLIDALS------AGGSSGGLLALLVALFlLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 796 RSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLI 875
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 876 ALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFV 955
Cdd:cd18551 150 FLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLA 229
|
250
....*....|....*....
gi 1063707070 956 LFSSYAASFYVGARLVDDG 974
Cdd:cd18551 230 VQLALLVVLGVGGARVASG 248
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
402-618 |
1.69e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 89.21 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDV--------LIDGINLKEFQLKWI-RSKIGLVSQEP--- 469
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERRRLlRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 470 VLFTASIKDNIA----------YGKEDATTEEIKAAAELANASkfVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILK 539
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYGDIRATAGDWLERVEIDAAR--IDDLP-----------TTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 540 DPRILLLDEATSALDAEservVQ-EALD--RIMVNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVS----VQaRLLDllRGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDDPQ 244
|
....*.
gi 1063707070 613 GAYSQL 618
Cdd:PRK11701 245 HPYTQL 250
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
385-612 |
1.84e-19 |
|
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: 88.50 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG---INLKEFQLkwIRSK 461
Cdd:COG0410 5 EVENLHAGYGGI---HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGediTGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTA-SIKDNI---AYGKEDAttEEIKAAAELAnaskfVDKLPQgLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLllgAYARRDR--AEVRADLERV-----YELFPR-LKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 538 LKDPRILLLDEATSALdaeSERVVQEALDRIM-VNR--TTVVV----AHRLSTVrnADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:COG0410 152 MSRPKLLLLDEPSLGL---APLIVEEIFEIIRrLNRegVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLAD 226
|
..
gi 1063707070 611 PE 612
Cdd:COG0410 227 PE 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
384-568 |
1.88e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.99 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGInlkefQLKWIRSKIG 463
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQ-EPVLFTASIKDNIAYGKEDATTEEikaAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPR 542
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFGLQLAGVEK---MQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180
....*....|....*....|....*.
gi 1063707070 543 ILLLDEATSALDAESERVVQEALDRI 568
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKL 174
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
388-612 |
1.94e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 388 DVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSKIGLV 465
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 466 SQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAVARAI 537
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSlrnlgvPEAEITRRVDEALTLVDAQHFRHQPIQCL-----------SHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 538 LKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVV-AHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
384-621 |
2.64e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQLKWIRSK 461
Cdd:PRK13636 6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEP--VLFTASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAV 533
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDNALKRTGIEHLKDKPTHCL-----------SFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 534 ARAILKDPRILLLDEATSALD----AESERVVQEALDRIMVnrTTVVVAHRLSTVR-NADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGL--TIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
250
....*....|...
gi 1063707070 609 KDPEGAYSQLIRL 621
Cdd:PRK13636 231 AEKEMLRKVNLRL 243
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
386-611 |
2.80e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 88.69 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 386 LKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLV 465
Cdd:PRK10575 14 LRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 466 SQE-PVLFTASIKDNIA------------YGKEDatTEEIKAAAELANASKFVDKLpqgLDTmvgehgtqLSGGQKQRIA 532
Cdd:PRK10575 91 PQQlPAAEGMTVRELVAigrypwhgalgrFGAAD--REKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
|
..
gi 1063707070 610 DP 611
Cdd:PRK10575 238 GE 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
406-602 |
2.89e-19 |
|
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: 87.27 E-value: 2.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqLKWIRSKIGLVSQEPVLFTA-SIKDNI---- 480
Cdd:cd03268 20 SLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALIEAPGFYPNlTARENLrlla 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 -AYGKEDATTEEIKAAAELANASKfvDKlpqgldtmVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:cd03268 98 rLLGIRKKRIDEVLDVVGLKDSAK--KK--------VK----GFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063707070 560 VVQEALDRIMVNRTTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:cd03268 164 ELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
383-607 |
3.99e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 3.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 383 DIELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKwiRSKI 462
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEPVLFT-ASIKDNIAYGKEDATTE--EIK----AAAELANASKFVDKLPQGLdtmvgehgtqlSGGQKQRIAVAR 535
Cdd:PRK11000 78 GMVFQSYALYPhLSVAENMSFGLKLAGAKkeEINqrvnQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 536 AILKDPRILLLDEATSALDAeSERVVQealdRIMV-------NRTTVVVAH-RLSTVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDA-ALRVQM----RIEIsrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
384-604 |
4.81e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.89 E-value: 4.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVL---FTasIKDN-IAYGKE-DATTEEIKAAaeLANASKFVdKLPQGLDTMVGEhgtqLSGGQKQRIAVARAIL 538
Cdd:PRK13536 118 VVPQFDNLdleFT--VRENlLVFGRYfGMSTREIEAV--IPSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALI 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAHRLSTV-RNADMIAVIHQG-KIVEKGSH 604
Cdd:PRK13536 189 NDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAeRLCDRLCVLEAGrKIAEGRPH 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
384-602 |
5.54e-19 |
|
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: 86.57 E-value: 5.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKwIRSKIG 463
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIA-ARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLF-TASIKDNIAY-------GKEDATTEeikaAAELANASKFVDKLPQGLDtmvgehgtQLSGGQKQRIAVAR 535
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlaqlkglKKEEARRR----IDEWLERLELSEYANKRVE--------ELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV-VAHRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
410-627 |
5.58e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 89.55 E-value: 5.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 410 SSGTTvALVGQSGSGKSTVVSLIERFYDPQAG------DVLID---GINLKEFQlkwirSKIGLVSQEPVLFTA-SIKDN 479
Cdd:PRK11144 23 AQGIT-AIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDaekGICLPPEK-----RRIGYVFQDARLFPHyKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 480 IAYGKEDATTEEIKAAAELANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESER 559
Cdd:PRK11144 97 LRYGMAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 560 VVQEALDRIM--VNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLkdpegaYSQLIR--LQEEKKS 627
Cdd:PRK11144 166 ELLPYLERLAreINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVW------ASSAMRpwLPKEEQS 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
406-599 |
8.06e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.86 E-value: 8.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLK----WIRSKIGLVSQEPVLF-TASIKDNI 480
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRsprdAIALGIGMVHQHFMLVpNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AYGKEDA------TTEEIKAAAELANASKF-VDklpqgLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:COG3845 102 VLGLEPTkggrldRKAARARIRELSERYGLdVD-----PDAKVE----DLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063707070 554 -DAESERVVqEALDRIMVNRTTVV-VAHRLSTVR-NADMIAVIHQGKIV 599
Cdd:COG3845 173 tPQEADELF-EILRRLAAEGKSIIfITHKLREVMaIADRVTVLRRGKVV 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
384-619 |
1.35e-18 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 86.74 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTypaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRS 460
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFT-ASIKDNIAYgkedATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILK 539
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAY----PLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 540 DPRILLLDEATSALDAESERVVQEALDRI--MVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYS 616
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELnsALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQANPDPRVR 240
|
...
gi 1063707070 617 QLI 619
Cdd:PRK11831 241 QFL 243
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
403-579 |
1.46e-18 |
|
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: 85.98 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKE--------FQ----LKWIrskiglvsqepv 470
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdrmvvFQnyslLPWL------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 lftaSIKDNIAYG----KEDATTEEIKAAAE----LANASKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPR 542
Cdd:TIGR01184 70 ----TVRENIALAvdrvLPDLSKSERRAIVEehiaLVGLTEAADKRP-----------GQLSGGMKQRVAIARALSIRPK 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 1063707070 543 ILLLDEATSALDAESERVVQEALDRIMV-NRTTVV-VAH 579
Cdd:TIGR01184 135 VLLLDEPFGALDALTRGNLQEELMQIWEeHRVTVLmVTH 173
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
371-617 |
1.74e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.84 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 371 STNGKVLDDIKG-----DIELKDVYFTYPARPDEQIfRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLI 445
Cdd:PRK15079 2 TEGKKVLLEVADlkvhfDIKDGKQWFWQPPKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 446 DGINL---KEFQLKWIRSKIGLVSQEPVlftAS------IKDNIA-----YgKEDATTEEIKAaaELANASKFVDKLPQg 511
Cdd:PRK15079 81 LGKDLlgmKDDEWRAVRSDIQMIFQDPL---ASlnprmtIGEIIAeplrtY-HPKLSRQEVKD--RVKAMMLKVGLLPN- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 512 ldtMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE-RVVQ--EALDRIMvNRTTVVVAHRLSTVRN-A 587
Cdd:PRK15079 154 ---LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaQVVNllQQLQREM-GLSLIFIAHDLAVVKHiS 229
|
250 260 270
....*....|....*....|....*....|
gi 1063707070 588 DMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:PRK15079 230 DRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
396-617 |
1.81e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.68 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 396 RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG----------INLKEF---QLKWIR-SK 461
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQsaaQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPV-----LFTA------SIKDNIAYGKEDAtteeikaaaeLANASKFVD--KLPQGlDTMVGEHGTQLSGGQK 528
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeqiaeSIRLHQGASREEA----------MVEAKRMLDqvRIPEA-QTILSRYPHQLSGGMR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 529 QRIAVARAILKDPRILLLDEATSALDAESE-------RVVQEALDrimvnRTTVVVAHRLSTVRN-ADMIAVIHQGKIVE 600
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMS-----MGVIFITHDMGVVAEiADRVLVMYQGEAVE 249
|
250
....*....|....*..
gi 1063707070 601 KGSHTELLKDPEGAYSQ 617
Cdd:PRK10261 250 TGSVEQIFHAPQHPYTR 266
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
403-607 |
2.83e-18 |
|
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: 84.73 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN-LKEfqLKWIRSKIGLVSQEPVL---FTAsiKD 478
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVRE--PREVRRRIGIVFQDLSVddeLTG--WE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 479 NIA-----YG-KEDATTEEIKAAAELANASKFVDKLpqgldtmVGEHgtqlSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:cd03265 93 NLYiharlYGvPGAERRERIDELLDFVGLLEAADRL-------VKTY----SGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 553 LDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
384-611 |
2.89e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 88.36 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTypaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:PRK09536 4 IDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVL-FTASIKDNIAYGK----------EDATTEEIKAAAELANASKFVDKlpqgldtmvgeHGTQLSGGQKQRIA 532
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQFADR-----------PVTSLSGGERQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 533 VARAILKDPRILLLDEATSALDAESE-RVVQEALDRIMVNRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:PRK09536 150 LARALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTA 229
|
.
gi 1063707070 611 P 611
Cdd:PRK09536 230 D 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
404-621 |
4.25e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.99 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLfiSSGTTVALVGQSGSGKSTVVSLIERFYDPQaGDVLIDGINLKEF---QLKWIRSKIGLVSQEPV------LFTA 474
Cdd:PRK15134 306 SFTL--RPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLnrrQLLPVRHRIQVVFQDPNsslnprLNVL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 SIkdnIAYGKE------DATTEE---IKAAAELanaskfvdklpqGLD-TMVGEHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:PRK15134 383 QI---IEEGLRvhqptlSAAQREqqvIAVMEEV------------GLDpETRHRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 545 LLDEATSALDaeseRVVQE---ALDRIMVNR---TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAYS- 616
Cdd:PRK15134 448 ILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEYTr 523
|
....*
gi 1063707070 617 QLIRL 621
Cdd:PRK15134 524 QLLAL 528
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
82-341 |
5.05e-18 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 85.67 E-value: 5.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 82 LLFGDLIDAFGENQTNTT----DKVSKVALKFVWL----GIGTFAAAFLqLSgwmISGERQAARIRSLYLKTILRQDIAF 153
Cdd:cd18574 17 LLLGDLVNVISRSLKETNgdfiEDLKKPALKLLGLyllqSLLTFAYISL-LS---VVGERVAARLRNDLFSSLLRQDIAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 154 FDIdTNTGEVVGRMSGDtvlIQD---AMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAK 230
Cdd:cd18574 93 FDT-HRTGELVNRLTAD---VQEfksSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 231 TASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHL--------VTAYKAGVIEGGSTglglgtlfLVVFCSY 302
Cdd:cd18574 169 LSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVekaaklneKLGLGIGIFQGLSN--------LALNGIV 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1063707070 303 ALAVWYGGKLILDKGYTGGQVLNIIIAVLTGSMSLGQTS 341
Cdd:cd18574 241 LGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLS 279
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
384-610 |
5.53e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 84.75 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG 463
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVlFTA--SIKDNIAYG----------KEDAttEEIKAA------AELANasKFVDklpqgldtmvgehgtQLSG 525
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGrfpyskgrltAEDR--EIIDEAiayldlEDLAD--RYLD---------------ELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALdRIMV---NRTTVVVAHRLstvrN-----ADMIAVIHQGK 597
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLL-RRLAdelGKTVVIVLHDI----NfascyADHIVAMKDGR 213
|
250
....*....|....*...
gi 1063707070 598 IVEKGS-----HTELLKD 610
Cdd:COG4604 214 VVAQGTpeeiiTPEVLSD 231
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
60-339 |
6.33e-18 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 85.56 E-value: 6.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIGNGLGFPLmtlLFGDLID-AFGENQTnttDKVSKVALKFVwlGIGTFAAAFLQLSGWM--ISGERQAA 136
Cdd:cd18542 1 YLLAILALLLATALNLLIPL---LIRRIIDsVIGGGLR---ELLWLLALLIL--GVALLRGVFRYLQGYLaeKASQKVAY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 137 RIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18542 73 DLRNDLYDHLQRLSFSFHD-KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 217 LVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFL 296
Cdd:cd18542 152 IALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDF 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063707070 297 VVFCSYALAVWYGGklildkgytggqvlniiIAVLTGSMSLGQ 339
Cdd:cd18542 232 LSGLQIVLVLWVGG-----------------YLVINGEITLGE 257
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
393-617 |
1.38e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.60 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 393 YPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDP----QAGDVLIDGINLKEFQLKWIrsKIGLVSQE 468
Cdd:PRK10418 13 QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRGR--KIATIMQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 469 P--------VLFTASIKDNIAYGKE--DATTEEIKAAAELANAskfvdklpqglDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK10418 88 PrsafnplhTMHTHARETCLALGKPadDATLTAALEAVGLENA-----------ARVLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIMVNRT--TVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKHAV 236
|
..
gi 1063707070 616 SQ 617
Cdd:PRK10418 237 TR 238
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
400-612 |
1.74e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 82.59 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQL-KWIRSKIGLVSQEPVLFtasikd 478
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIF------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 479 niaygkEDATTEE-IKAAAELANASKfvDKLPQGLDTMVGE----H-----GTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:cd03218 88 ------RKLTVEEnILAVLEIRGLSK--KEREEKLEELLEEfhitHlrkskASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 549 ATSALD----AESERVVQEALDR---IMVN----RTTVVVAHRlstvrnadmIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:cd03218 160 PFAGVDpiavQDIQKIIKILKDRgigVLITdhnvRETLSITDR---------AYIIYEGKVLAEGTPEEIAANEL 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
384-600 |
1.75e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.04 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIdGINLKefqlkwirskIG 463
Cdd:COG0488 316 LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVLF--TASIKDNIAYGKEDATTEEIKAAAElanasKF------VDKLpqgldtmVGEhgtqLSGGQKQRIAVAR 535
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLG-----RFlfsgddAFKP-------VGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRImvNRTTVVVAH-R--LSTVrnADMIAVIHQGKIVE 600
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALDDF--PGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
384-599 |
2.12e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 87.09 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPArPDEQI--FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF------QL 455
Cdd:PRK10535 5 LELKDIRRSYPS-GEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadalaQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 456 KwiRSKIGLVSQEPVLFT-ASIKDNIAYGKEDATTEEikaAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVA 534
Cdd:PRK10535 84 R--REHFGFIFQRYHLLShLTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAVIHQGKIV 599
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
400-606 |
2.39e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLKWIRSKIGLVSQEP-VLFTAS 475
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGK--EDATTEEIKAAAELAnaskfVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:PRK10908 96 VYDNVAIPLiiAGASGDDIRRRVSAA-----LDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 554 D-AESERVVQ--EALDRIMVnrTTVVVAHRLSTV-RNADMIAVIHQGKIVEkGSHTE 606
Cdd:PRK10908 169 DdALSEGILRlfEEFNRVGV--TVLMATHDIGLIsRRSYRMLTLSDGHLHG-GVGGE 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
384-597 |
3.52e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.41 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIG 463
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQepvlftasikdniaygkedatteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVARAILKDPRI 543
Cdd:cd03221 67 YFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRImvNRTTVVVAH-R--LSTVrnADMIAVIHQGK 597
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
384-555 |
5.25e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPArpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INlkefQLKWIRSK 461
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVN----ELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFT-ASIKDNIAYG------KEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVA 534
Cdd:PRK11650 78 IAMVFQNYALYPhMSVRENMAYGlkirgmPKAEIEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 1063707070 535 RAILKDPRILLLDEATSALDA 555
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
398-610 |
7.04e-17 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.27 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI---ERfYDPQAGDVLIDGINLkefqLKW---IRSK--IGLVSQEP 469
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDI----LELspdERARagIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 470 V--------LFTASIKDNIAYGKEDATT--EEIKAAAELAN-ASKFVDKlpqGLDtmVGehgtqLSGGQKQRIAVARAIL 538
Cdd:COG0396 87 VeipgvsvsNFLRTALNARRGEELSAREflKLLKEKMKELGlDEDFLDR---YVN--EG-----FSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGSHtELLKD 610
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALE 230
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
721-978 |
7.09e-17 |
|
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: 82.44 E-value: 7.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 721 ILGSISAAANGVILPIfgiLISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCF 800
Cdd:cd18544 5 LLLLLLATALELLGPL---LIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 801 EKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGF 880
Cdd:cd18544 82 SHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 881 LYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSY 960
Cdd:cd18544 160 LFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLAL 239
|
250
....*....|....*...
gi 1063707070 961 AASFYVGARLVDDGKTTF 978
Cdd:cd18544 240 ALVLWYGGGQVLSGAVTL 257
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
409-608 |
8.41e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.57 E-value: 8.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 409 ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVL-FTASIKDNIAYG---- 483
Cdd:PRK10253 30 IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQELVARGryph 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 484 --------KEDAtteeiKAAAELANASKFVDKLPQGLDTmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:PRK10253 110 qplftrwrKEDE-----EAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 556 ESERVVQEALDRImvNR----TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK10253 177 SHQIDLLELLSEL--NRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
60-339 |
1.14e-16 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 81.76 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIGNGLGFPLMTllfGDLIDafGENQTNTTDKVSKVALKFVWLGIGTFAAAFL--QLSGWMISG-ErqaA 136
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLT---RRAID--GPIAHGDRSALWPLVLLLLALGVAEAVLSFLrrYLAGRLSLGvE---H 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 137 RIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGeKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18543 73 DLRTDLFAHLQRLDGAFHD-RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 217 LVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFL 296
Cdd:cd18543 151 LVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063707070 297 VVFCSYALAVWYGGklildkgytggqvlniiIAVLTGSMSLGQ 339
Cdd:cd18543 231 LPELGLAAVLALGG-----------------WLVANGSLTLGT 256
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
404-610 |
1.46e-16 |
|
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: 84.08 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLI----DGINLKE--FQLKWiRSK--IGLVSQEPVLFT-A 474
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKpgPDGRG-RAKryIGILHQEYDLYPhR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 SIKDNIA----------YGKEDATTEEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRIL 544
Cdd:TIGR03269 381 TVLDNLTeaiglelpdeLARMKAVITLKMVGFDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 545 LLDEATSALDAESERVVQEAL--DRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
721-977 |
1.73e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 81.05 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 721 ILGSISAAANGVILP-IFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMC 799
Cdd:cd18574 2 VLSALAAALVNIQIPlLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 800 FEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNG 879
Cdd:cd18574 82 FSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 880 FLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIvsGIGF--GFSFFVLF 957
Cdd:cd18574 160 TLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGL--GIGIfqGLSNLALN 237
|
250 260
....*....|....*....|
gi 1063707070 958 SSYAASFYVGARLVDDGKTT 977
Cdd:cd18574 238 GIVLGVLYYGGSLVSRGELT 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
398-610 |
1.79e-16 |
|
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: 78.72 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF--YDPQAGDVLIDGINLKEFQLKwIRSK--IGLVSQEPVLFt 473
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARlgIFLAFQYPPEI- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 474 asikdniaygkedattEEIKaaaeLANASKFVDklpqgldtmVGehgtqLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:cd03217 90 ----------------PGVK----NADFLRYVN---------EG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 554 DAESERVVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGShTELLKD 610
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
395-565 |
1.95e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 78.69 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTA 474
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 SIKDNIAYGKEDATTEEIKAAAELANASKFVDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGFED-RPVA----------QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170
....*....|.
gi 1063707070 555 AESERVVQEAL 565
Cdd:cd03231 158 KAGVARFAEAM 168
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
384-610 |
2.13e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.29 E-value: 2.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPAR-PDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDV------------------ 443
Cdd:PRK13651 3 IKVKNIVKIFNKKlPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 444 LIDGINLKEF------QLKWIRSKIGLVSQ--EPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdklpqGLDTM 515
Cdd:PRK13651 83 VLEKLVIQKTrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELV-----GLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 516 VGEHGT-QLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTV-RNADMIAV 592
Cdd:PRK13651 158 YLQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTIF 237
|
250
....*....|....*...
gi 1063707070 593 IHQGKIVEKGSHTELLKD 610
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSD 255
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
402-598 |
2.30e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 78.24 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQ-LKWIRSKIGLVSQEP----VLFTASI 476
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 477 KDNIAygkedatteeikaaaelanaskfvdkLPQgldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 556
Cdd:cd03215 96 AENIA--------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063707070 557 SERVVQEALDRIMVNRTTVVVahrLST-----VRNADMIAVIHQGKI 598
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
761-981 |
2.89e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 80.46 E-value: 2.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 761 FWAIIFMVL-GFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAAtirgLVGDS 839
Cdd:cd18590 36 TSAIGLMCLfSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTT----LMSRS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 840 LAQtvqNLSSILAGLIIAFLAC-------WQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIR 912
Cdd:cd18590 110 VAL---NANVLLRSLVKTLGMLgfmlslsWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIR 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 913 TVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTFDSV 981
Cdd:cd18590 187 TVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSL 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
412-617 |
5.94e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.60 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 412 GTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGI---NLKEFQLKWIRSKIGLVSQEPVlftASIKDNIAYGkeDAT 488
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPY---ASLDPRQTVG--DSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 489 TEEIK---------AAAELANASKFVDKLPqgldtmvgEHG----TQLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:PRK10261 425 MEPLRvhgllpgkaAAARVAWLLERVGLLP--------EHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 556 E-SERVVQEALD--RIMvNRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ 617
Cdd:PRK10261 497 SiRGQIINLLLDlqRDF-GIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFENPQHPYTR 561
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
401-582 |
6.74e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 6.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEF----QLKWIRSKIGLVSQEPVL---FT 473
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGFIYQFHHLlpdFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 474 ASikDNIAY-----GKEDATTEEiKAAAELANAskfvdklpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK11629 104 AL--ENVAMplligKKKPAEINS-RALEMLAAV---------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063707070 549 ATSALDAESERVVQEALDRIMVNRTT--VVVAHRLS 582
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQ 207
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
416-633 |
1.16e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.37 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 416 ALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLkEFQLKWIRSKIGLVSQEPVLFT-ASIKDNIA-YGKEDATTEEik 493
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILfYAQLKGRSWE-- 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 494 aAAELANASKFVDKlpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRT 573
Cdd:TIGR01257 1037 -EAQLEMEAMLEDT---GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 574 TVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTeLLKD--PEGAYSQLIRLQEEKKSDENAAE 633
Cdd:TIGR01257 1113 IIMSTHHMDEADLlGDRIAIISQGRLYCSGTPL-FLKNcfGTGFYLTLVRKMKNIQSQRGGCE 1174
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
396-609 |
1.24e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.25 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 396 RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIErFYDPQ----AGDVLIDG--INLKEFQLkwiRSK-------- 461
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGmpIDAKEMRA---ISAyvqqddlf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IG-LVSQEPVLFTASIK--DNIAYGKEDATTEEIKAAAELANASkfvdklpqglDTMVGEHGTQ--LSGGQKQRIAVARA 536
Cdd:TIGR00955 111 IPtLTVREHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCA----------NTRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLST--VRNADMIAVIHQGKIVEKGSHTELLK 609
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
405-611 |
1.40e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.67 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 405 FSLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQAGDVLIDGINLKEFQL-KWIRSKIGLVSQEPVLFTASIKDNIAYG 483
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 484 KEDATTEEIKAAA--ELANASKFVDKLPQGLdtmvgehgTQLSGGQKQRIAVARAILK-DPRI------LLLDEATSALD 554
Cdd:PRK03695 94 QPDKTRTEAVASAlnEVAEALGLDDKLGRSV--------NQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 555 aeserVVQE-ALDRIMV-----NRTTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK03695 166 -----VAQQaALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
403-610 |
1.43e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.61 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKwIRSKIGLVSQEPVLFTA-SIKDNIA 481
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPE-DRRRIGYLPEERGLYPKmKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 482 Y-----GkedatteeIKAAAELANASKFVDKLpqGLdtmvGEHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:COG4152 94 YlarlkG--------LSKAEAKRRADEWLERL--GL----GDRANkkveELSKGNQQKVQLIAALLHDPELLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 553 LDAESERVVQEALDRIMVNRTTVVVA-HRLSTV-RNADMIAVIHQGKIVEKGSHTELLKD 610
Cdd:COG4152 160 LDPVNVELLKDVIRELAAKGTTVIFSsHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
400-607 |
2.42e-15 |
|
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: 76.41 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN---LKEFQLkwIRSKIGLVSQEPVLFTA-S 475
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHER--ARAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGkedatteeikaAAELANASKFVDK----LPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATS 551
Cdd:TIGR03410 92 VEENLLTG-----------LAALPRRSRKIPDeiyeLFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 552 ALD----AESERVVQEALDRImvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTEL 607
Cdd:TIGR03410 161 GIQpsiiKDIGRVIRRLRAEG--GMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
384-610 |
2.71e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.09 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL------KEFQLkw 457
Cdd:PRK15439 12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltpaKAHQL-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 458 irsKIGLVSQEPVLF-TASIKDNIAYG--KEDATTEeiKAAAELANASKFVDklpqgLDTMVGehgtQLSGGQKQRIAVA 534
Cdd:PRK15439 87 ---GIYLVPQEPLLFpNLSVKENILFGlpKRQASMQ--KMKQLLAALGCQLD-----LDSSAG----SLEVADRQIVEIL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 535 RAILKDPRILLLDEATSALD-AESERV---VQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLST 229
|
.
gi 1063707070 610 D 610
Cdd:PRK15439 230 D 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
401-561 |
4.38e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 75.59 E-value: 4.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINL---KEFQLKWIRSK-IGLVSQEPVLF-TAS 475
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmDEEARAKLRAKhVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAY-----GKEDATTEEiKAAAELANA--SKFVDKLPqgldtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDE 548
Cdd:PRK10584 105 ALENVELpallrGESSRQSRN-GAKALLEQLglGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170
....*....|....
gi 1063707070 549 ATSALDAES-ERVV 561
Cdd:PRK10584 173 PTGNLDRQTgDKIA 186
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
719-978 |
4.44e-15 |
|
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: 77.06 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 719 VLILGSISAAANgVILPIF-GILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRS 797
Cdd:cd18547 4 VIILAIISTLLS-VLGPYLlGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 798 MCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIal 877
Cdd:cd18547 83 DLFEKLQRLPLSYFDT--HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 878 ngFLYMKFM-----KGFSADAKKMyGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFS 952
Cdd:cd18547 159 --LLVTKFIakrsqKYFRKQQKAL-GELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIM 235
|
250 260
....*....|....*....|....*.
gi 1063707070 953 FFVLFSSYAASFYVGARLVDDGKTTF 978
Cdd:cd18547 236 NFINNLGYVLVAVVGGLLVINGALTV 261
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
395-566 |
5.80e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.32 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPVLFTA 474
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 SIKDNIAYGKEDATTEE--IKAAAELANASKFVDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQrtIEDALAAVGLTGFED-LPAA----------QLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170
....*....|....
gi 1063707070 553 LDAESERVVQEALD 566
Cdd:TIGR01189 158 LDKAGVALLAGLLR 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
400-627 |
1.56e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.66 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVV----SLIERFYDPQAGDVLIDGINLKEFQL----KWIRSKIGLVSQEPVL 471
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTVQREGRLardiRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 FTA-SIKDNIAYGKEDATTEEIKAAAELANASKfvDKLPQGLdTMVG------EHGTQLSGGQKQRIAVARAILKDPRIL 544
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTPFWRTCFSWFTREQK--QRALQAL-TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 545 LLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELLKDP-EGAYSQLIR 620
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfDHLYRSINR 254
|
....*..
gi 1063707070 621 LQEEKKS 627
Cdd:PRK09984 255 VEENAKA 261
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
395-602 |
1.72e-14 |
|
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: 73.84 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQA---GDVLIDGINLKEFQLKwirSKIGLVSQ---- 467
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQ---KCVAYVRQddil 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 468 -------EPVLFTASIK-DNIAYGKEDATTEEIKAAAELAnaskfvdklpqglDTMVG-EHGTQLSGGQKQRIAVARAIL 538
Cdd:cd03234 93 lpgltvrETLTYTAILRlPRKSSDAIRKKRVEDVLLRDLA-------------LTRIGgNLVKGISGGERRRVSIAVQLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIMV-NRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKG 602
Cdd:cd03234 160 WDPKVLILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
60-324 |
2.07e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 74.85 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMIS--GERQAAR 137
Cdd:cd18563 5 FLLMLLGTALGL-------VPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLArlGERITAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 138 IRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPLL 217
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFD-KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 218 VMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGV-IEGGSTGLGLGTLFL 296
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIrAEKLWATFFPLLTFL 236
|
250 260
....*....|....*....|....*....
gi 1063707070 297 VVFCsyALAVWY-GGKLILDKGYTGGQVL 324
Cdd:cd18563 237 TSLG--TLIVWYfGGRQVLSGTMTLGTLV 263
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
406-611 |
2.30e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.44 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIGLVSQEPvlfTASIKDNIAYGK- 484
Cdd:PRK15112 33 SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISQi 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 485 --------EDATTEEIKAAaeLANASKFVDKLPqgldtmvgEHGT----QLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK15112 110 ldfplrlnTDLEPEQREKQ--IIETLRQVGLLP--------DHASyyphMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 553 LDAEservVQEALDRIMVNR------TTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:PRK15112 180 LDMS----MRSQLINLMLELqekqgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
118-324 |
2.84e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 74.86 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 118 AAAFLQLSGWMISGERQAARIRS-LYlKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMgekVGKAIQLLA---TFV 193
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRdLF-AHLQRLSLSFHD-RRRTGDLLSRLTGDVGAIQDLL---VSGVLPLLTnllTLV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 194 GGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHL 273
Cdd:cd18564 144 GMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAREN 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 274 VTAYKAGVIEGGSTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQVL 324
Cdd:cd18564 224 RKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLL 274
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
406-612 |
2.94e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.39 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKST----VVSLIERfydpQAGDVLIDGINLKEFQL-KWIRSKIGLVSQEPVLFTA-SIKDN 479
Cdd:PRK10895 23 SLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 480 IAYG---KEDATTEEIKAAAELANASKFVDKLPQGLdtmvgehGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 556
Cdd:PRK10895 99 LMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 557 S----ERVVQEALDRIMvnrTTVVVAHRL-STVRNADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK10895 172 SvidiKRIIEHLRDSGL---GVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
384-612 |
5.31e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 5.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKST----VVSLIErfydPQAGDVLIDGINLKEFQLkWIR 459
Cdd:COG1137 4 LEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHLPM-HKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 460 SK--IGLVSQEPVLFTA-SIKDNIaygkedatteeiKAAAELANASKfvDKLPQGLDTMVGE----H-----GTQLSGGQ 527
Cdd:COG1137 76 ARlgIGYLPQEASIFRKlTVEDNI------------LAVLELRKLSK--KEREERLEELLEEfgitHlrkskAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 528 KQRIAVARAILKDPRILLLDEATSALD----AESERVVQEALDR-IMV-----N-RTTvvvahrLSTVRNAdmiAVIHQG 596
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKERgIGVlitdhNvRET------LGICDRA---YIISEG 212
|
250
....*....|....*.
gi 1063707070 597 KIVEKGSHTELLKDPE 612
Cdd:COG1137 213 KVLAEGTPEEILNNPL 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
398-612 |
7.19e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF--YDPQAGDVLIDGINLKEFQLKwIRSKIGL----------- 464
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 -VSQEPVLFTASIKDNIAYGKEDAttEEIKAAAELANASKFVDKLPQGLDTMVGEhgtQLSGGQKQRIAVARAILKDPRI 543
Cdd:CHL00131 98 gVSNADFLRLAYNSKRKFQGLPEL--DPLEFLEIINEKLKLVGMDPSFLSRNVNE---GFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGShTELLKDPE 612
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AELAKELE 243
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
385-599 |
7.43e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.44 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARPDEQI-----------FRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEF 453
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVleveglsvggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 454 QLK----WIRSKIGLVS----QEPVLFTASIKDNIAYGKEDATTEE--IKAAAELANASKFVDKL---PQGLDTMVGehg 520
Cdd:COG1129 317 RIRsprdAIRAGIAYVPedrkGEGLVLDLSIRENITLASLDRLSRGglLDRRRERALAEEYIKRLrikTPSPEQPVG--- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 521 tQLSGGQKQRIAVARAILKDPRILLLDEATSALD--AESE--RVVQEALDR----IMVnrttvvvahrlST-----VRNA 587
Cdd:COG1129 394 -NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIRELAAEgkavIVI-----------SSelpelLGLS 461
|
250
....*....|..
gi 1063707070 588 DMIAVIHQGKIV 599
Cdd:COG1129 462 DRILVMREGRIV 473
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
384-603 |
8.13e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYP------------------ARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVL 444
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrTRREEfWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 445 IDGInlkefqlkwIRSKIGL---VSQEpvlFTAsiKDNI-----AYG---KE-DATTEEIKAAAELANAskfvdklpqgL 512
Cdd:COG1134 85 VNGR---------VSALLELgagFHPE---LTG--RENIylngrLLGlsrKEiDEKFDEIVEFAELGDF----------I 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 513 DTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE----SERVVQEALDRimvNRTTVVVAHRLSTVRN-A 587
Cdd:COG1134 141 DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRlC 213
|
250
....*....|....*.
gi 1063707070 588 DMIAVIHQGKIVEKGS 603
Cdd:COG1134 214 DRAIWLEKGRLVMDGD 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
384-580 |
8.50e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 70.26 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFtypARPDEQIF-RGFSLFISSGTTVALVGQSGSGKSTVVSLI--------ERFYDPQAGDVLidginlkefq 454
Cdd:cd03223 1 IELENLSL---ATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMPEGEDLL---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 455 lkwirskigLVSQEPVLFTASIKDNIAYGKEDAtteeikaaaelanaskfvdklpqgldtmvgehgtqLSGGQKQRIAVA 534
Cdd:cd03223 68 ---------FLPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFA 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 535 RAILKDPRILLLDEATSALDAESE----RVVQEALdrimvnrTTVV-VAHR 580
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEdrlyQLLKELG-------ITVIsVGHR 147
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
384-608 |
8.95e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.30 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKWIRSKIG 463
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPVL---FTasIKDNIA-----YGKEDATTEE-IKAAAELAnaskfvdKLPQGLDTMVGEhgtqLSGGQKQRIAVA 534
Cdd:PRK13537 84 VVPQFDNLdpdFT--VRENLLvfgryFGLSAAAARAlVPPLLEFA-------KLENKADAKVGE----LSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARgKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
369-602 |
1.12e-13 |
|
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: 71.41 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 369 SYSTNGKVLDDIKGDIELKDVyftyPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGi 448
Cdd:cd03220 9 SYPTYKGGSSSLKKLGILGRK----GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 449 nlkefQLKWIrskIGL-VSQEPVLftaSIKDNIAY--------GKE-DATTEEIKAAAELANAskfvdklpqgLDTMVGE 518
Cdd:cd03220 84 -----RVSSL---LGLgGGFNPEL---TGRENIYLngrllglsRKEiDEKIDEIIEFSELGDF----------IDLPVKT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 519 hgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAE-SERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQG 596
Cdd:cd03220 143 ----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKG 218
|
....*.
gi 1063707070 597 KIVEKG 602
Cdd:cd03220 219 KIRFDG 224
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
128-278 |
1.20e-13 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 72.76 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 128 MISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLiqdaMGEKVGKAIQ-LLATFVGGF-VIAFVRG-- 203
Cdd:cd18590 61 MCTLSRLNLRLRHQLFSSLVQQDIGFFE-KTKTGDLTSRLSTDTTL----MSRSVALNANvLLRSLVKTLgMLGFMLSls 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 204 WLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYK 278
Cdd:cd18590 136 WQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYN 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
392-563 |
1.61e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 74.59 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 392 TYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerfydpqAGdvlIDginlKEFQLKWIRS---KIGLVSQE 468
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KDFNGEARPQpgiKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 469 PVL-FTASIKDNI-------------------AYGKEDA----------TTEEIKAAAELANASKFVD------KLPQGl 512
Cdd:TIGR03719 77 PQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDAdfdklaaeqaELQEIIDAADAWDLDSQLEiamdalRCPPW- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 513 DTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES----ERVVQE 563
Cdd:TIGR03719 156 DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
404-597 |
1.96e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQA---GDVLIDGinlKEFQLKWIR----SKIGLVSQEPVLFTA-S 475
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEG---EELQASNIRdterAGIAIIHQELALVKElS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGKEDATTEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALdA 555
Cdd:PRK13549 99 VLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL-T 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063707070 556 ESERVVQEALDRIMVNR--TTVVVAHRLSTVRN-ADMIAVIHQGK 597
Cdd:PRK13549 176 ESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
403-602 |
2.60e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 70.44 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRsKIGLV--SQEPVLFTASIKDNI 480
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 481 AYGKEdatTEEIKAAAELANASKFVDKLPQG--LDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:cd03267 117 YLLAA---IYDLPPARFKKRLDELSELLDLEelLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063707070 559 RVVQEALDRIMVNRTTVVV--AHRLSTV-RNADMIAVIHQGKIVEKG 602
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
406-628 |
5.05e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKS----TVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSKIG----LVSQEPVlftASIk 477
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPM---TSL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 478 dNIAYGKEDATTEEIKA---AAELANASKFVDKLpqgldTMVG-----------EHgtQLSGGQKQRIAVARAILKDPRI 543
Cdd:PRK11022 103 -NPCYTVGFQIMEAIKVhqgGNKKTRRQRAIDLL-----NQVGipdpasrldvyPH--QLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMV--NRTTVVVAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQ-LI 619
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQaLL 254
|
....*....
gi 1063707070 620 RLQEEKKSD 628
Cdd:PRK11022 255 RALPEFAQD 263
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
60-272 |
5.52e-13 |
|
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: 70.90 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTNTT----DKVSKVALKFVWLGIGTFAAAFLQlsGWMIS--GER 133
Cdd:cd18547 5 IILAIISTLLSV-------LGPYLLGKAIDLIIEGLGGGGgvdfSGLLRILLLLLGLYLLSALFSYLQ--NRLMArvSQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 134 QAARIRS-LYLKtILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLS 212
Cdd:cd18547 76 TVYDLRKdLFEK-LQRLPLSYFD-THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 213 SIPLLVmagaLLAIVIAKTASRG----QTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKH 272
Cdd:cd18547 154 TVPLSL----LVTKFIAKRSQKYfrkqQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEI 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-579 |
7.65e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.36 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGT-----TVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKeFQLKWIRSKiglvsqepvlFTASIKD 478
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD----------YEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 479 nIAYGKEDATTEEIKAAAELANaskfvdklPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:cd03237 81 -LLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180
....*....|....*....|...
gi 1063707070 559 RVVQEALDRIMVN--RTTVVVAH 579
Cdd:cd03237 152 LMASKVIRRFAENneKTAFVVEH 174
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
405-617 |
1.00e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.52 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 405 FSLfiSSGTTVALVGQSGSGKS-TVVSLIERFydpqAGDVLIDG---------INLKEFQLKWIRS-KIGLVSQEPVlfT 473
Cdd:PRK09473 37 FSL--RAGETLGIVGESGSGKSqTAFALMGLL----AANGRIGGsatfngreiLNLPEKELNKLRAeQISMIFQDPM--T 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 474 A-----SIKDNIA--------YGKEDATTEEIKA--AAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAIL 538
Cdd:PRK09473 109 SlnpymRVGEQLMevlmlhkgMSKAEAFEESVRMldAVKMPEARKRMKMYPH-----------EFSGGMRQRVMIAMALL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKreFNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPY 257
|
..
gi 1063707070 616 SQ 617
Cdd:PRK09473 258 SI 259
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
395-609 |
1.97e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVV-SLIERFYDPQA-------GDVLIDGINLKEF---QLKWIRSKIG 463
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLkALAGDLTGGGAprgarvtGDVTLNGEPLAAIdapRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQEPvlFTASIKDNIAYGK----------EDATTEEIKAAAELANAskfvdklpqglDTMVGEHGTQLSGGQKQRIAV 533
Cdd:PRK13547 90 QAAQPA--FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 534 ARAILK---------DPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA--HRLS-TVRNADMIAVIHQGKIVEK 601
Cdd:PRK13547 157 ARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNlAARHADRIAMLADGAIVAH 236
|
....*...
gi 1063707070 602 GSHTELLK 609
Cdd:PRK13547 237 GAPADVLT 244
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
761-921 |
2.29e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 69.08 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 761 FWAIIFMVLGFA---SIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVG 837
Cdd:cd18564 53 LLLAAAALVGIAllrGLASY-AGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDR--RRTGDLLSRLTGDVGAIQDLLV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 838 DSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASF 917
Cdd:cd18564 130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAF 209
|
....
gi 1063707070 918 CAED 921
Cdd:cd18564 210 GREE 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
405-620 |
2.41e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 69.16 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 405 FSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQ----AGDVLIDGINL-----KEfQLKWIRSKIGLVSQEPVLF--- 472
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLlklspRE-RRKIIGREIAMIFQEPSSCldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 473 TASIKDNIaygKEDATTEEIK------------AAAEL------ANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVA 534
Cdd:COG4170 105 SAKIGDQL---IEAIPSWTFKgkwwqrfkwrkkRAIELlhrvgiKDHKDIMNSYPH-----------ELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 535 RAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV--VAHRLSTV-RNADMIAVIHQGKIVEKGSHTELLKDP 611
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIllISHDLESIsQWADTITVLYCGQTVESGPTEQILKSP 250
|
250
....*....|
gi 1063707070 612 EGAYSQ-LIR 620
Cdd:COG4170 251 HHPYTKaLLR 260
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
64-340 |
3.70e-12 |
|
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: 68.21 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 64 ILGTLGSIGNGLGFPLMTLLFGDLIDAFgENQTNTTDKVSKVALKFVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYL 143
Cdd:cd18541 2 LLGILFLILVDLLQLLIPRIIGRAIDAL-TAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 144 KTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVgkaIQLL-ATFVGGFVIA--FVRGWLLTLVMLSSIPLLVMA 220
Cdd:cd18541 81 AHLLTLSPSFYQ-KNRTGDLMARATNDLNAVRMALGPGI---LYLVdALFLGVLVLVmmFTISPKLTLIALLPLPLLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 221 GALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGLGLGTLFLVVFC 300
Cdd:cd18541 157 VYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1063707070 301 SYALAVWYGGKLILDKGYTGGQV--LNIIIAVLTGSM-SLGQT 340
Cdd:cd18541 237 SFLIVLWYGGRLVIRGTITLGDLvaFNSYLGMLIWPMmALGWV 279
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
763-921 |
4.33e-12 |
|
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: 68.36 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 763 AIIFMVLGFASIIAYPAQTFFFAIAGcKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQ 842
Cdd:cd18565 58 GLTVAAFLLESLFQYLSGVLWRRFAQ-RVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANS 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 843 TVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18565 135 IIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAED 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
404-594 |
5.19e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.84 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLF----ISSGTTVALVGQSGSGKSTVVSL---------------------IERFydpqAGDVLIDGI-NLKEFQLKW 457
Cdd:PRK13409 87 GFKLYglpiPKEGKVTGILGPNGIGKTTAVKIlsgelipnlgdyeeepswdevLKRF----RGTELQNYFkKLYNGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 458 IRsKIGLVSQEPVLFTASIKdniaygkedattEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAI 537
Cdd:PRK13409 163 VH-KPQYVDLIPKVFKGKVR------------ELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAAL 227
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 538 LKDPRILLLDEATSALDAEsERV-VQEALDRIMVNRTTVVVAHRLSTVrnaDMIA-VIH 594
Cdd:PRK13409 228 LRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDLAVL---DYLAdNVH 282
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
116-323 |
5.62e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 67.50 E-value: 5.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 116 TFAAAFLQLSG---WMISGERQAARIRSLYLKTILRQDIAFFDIDtNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATF 192
Cdd:cd18589 46 TIASAVSEFVCdliYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN-QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 193 VGGFVIAFVRGWLLTLVMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKH 272
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 273 LVTAYKagvIEGGSTGLGLGTLFLVVFCSYALAV---WYGGKLIldkgyTGGQV 323
Cdd:cd18589 205 LQKTYR---LNKKEAAAYAVSMWTSSFSGLALKVgilYYGGQLV-----TAGTV 250
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
384-607 |
7.00e-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: 69.06 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERF--YDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IG---------LVSQEPVLF------TASIKDNIA---------YGKEDATTEEIKAAAELA-NASKFVDKLPQGLDTMV 516
Cdd:TIGR03269 78 VGepcpvcggtLEPEEVDFWnlsdklRRRIRKRIAimlqrtfalYGDDTVLDNVLEALEEIGyEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 517 GEH-----GTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVRN-AD 588
Cdd:TIGR03269 158 LSHrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSD 237
|
250
....*....|....*....
gi 1063707070 589 MIAVIHQGKIVEKGSHTEL 607
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEV 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
400-608 |
7.37e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerFYDPQA--GDVLIDGINLKEFQLKWI-RSKIGLVSQEPVLFT-AS 475
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWQTAKImREAVAIVPEGRRVFSrMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGKEDATTEEIKAAAElanasKFVDKLPQGLDTMVGEHGTqLSGGQKQRIAVARAILKDPRILLLDEATSALda 555
Cdd:PRK11614 97 VEENLAMGGFFAERDQFQERIK-----WVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL-- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 556 eSERVVQEALDRIMVNR----TTVVVAHRLS-TVRNADMIAVIHQGKIVEKGSHTELL 608
Cdd:PRK11614 169 -APIIIQQIFDTIEQLReqgmTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
716-978 |
1.14e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 66.72 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 716 EIPVLILGSISAAANGVILPIF-GILISSVIkaffqPPKKLKEDTsFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQR 794
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLiKIAIDEYI-----PNGDLSGLL-IIALLFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 795 IRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPL 874
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFDS--RPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 875 IALNGFLYMKFM-KGFSADAKKMYGEASQVANDAVGsIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIgfgFSF 953
Cdd:cd18545 153 LVLVVFLLRRRArKAWQRVRKKISNLNAYLHESISG-IRVIQSFAREDENEEIFDELNRENRKANMRAVRLNAL---FWP 228
|
250 260
....*....|....*....|....*...
gi 1063707070 954 FVLFSS---YAASFYVGARLVDDGKTTF 978
Cdd:cd18545 229 LVELISalgTALVYWYGGKLVLGGAITV 256
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
384-548 |
1.20e-11 |
|
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: 68.29 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPDEQIFR-G-FSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIRSK 461
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTlGpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTAsikdniAYGKEDATTEEiKAAA-----ELANASKFVDklpQGLDTmvgehgTQLSGGQKQRIAVARA 536
Cdd:COG4615 408 FSAVFSDFHLFDR------LLGLDGEADPA-RAREllerlELDHKVSVED---GRFST------TDLSQGQRKRLALLVA 471
|
170
....*....|..
gi 1063707070 537 ILKDPRILLLDE 548
Cdd:COG4615 472 LLEDRPILVFDE 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
401-600 |
1.44e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 1.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFY--DPQAGDVLIDGINLkefqlkwirskiglvSQEpvlftASIKD 478
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 479 NIAygkedaTTEEIKAAAELANASKFVDklPQGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:COG2401 105 AIG------RKGDFKDAVELLNAVGLSD--AVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063707070 559 RVVQEALDRIM--VNRTTVVVAHRlSTVRNA---DMIAVIHQGKIVE 600
Cdd:COG2401 173 KRVARNLQKLArrAGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
384-600 |
1.47e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeqifrGFS-----LFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWI 458
Cdd:PRK10522 323 LELRNVTFAYQDN-------GFSvgpinLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 459 RSKIGLVSQEPVLFTASIKDniaygkeDATTEEIKAAAELANASKFVDKLpqgldTMVGEH--GTQLSGGQKQRIAVARA 536
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLLGP-------EGKPANPALVEKWLERLKMAHKL-----ELEDGRisNLKLSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVV-QEALD--RIMvNRTTVVVAHRLSTVRNADMIAVIHQGKIVE 600
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFyQVLLPllQEM-GKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
392-557 |
1.65e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 392 TYParPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIerfydpqAGdvlIDginlKEFQLKWIRS---KIGLVSQE 468
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AG---VD----KEFEGEARPApgiKVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 469 PVL-FTASIKDNI-------------------AYGKEDATT----------EEIKAAAELANASKFVD------KLPQGl 512
Cdd:PRK11819 79 PQLdPEKTVRENVeegvaevkaaldrfneiyaAYAEPDADFdalaaeqgelQEIIDAADAWDLDSQLEiamdalRCPPW- 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1063707070 513 DTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAES 557
Cdd:PRK11819 158 DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
404-594 |
4.78e-11 |
|
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: 64.31 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLF----ISSGTTVALVGQSGSGKSTVVSLIE--------RFYDPQAGDVLID---GINLKEF-------QLKWIRsK 461
Cdd:cd03236 14 SFKLHrlpvPREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYftkllegDVKVIV-K 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 462 IGLVSQEPVLFTASIKDNIaygkedatteeiKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDP 541
Cdd:cd03236 93 PQYVDLIPKAVKGKVGELL------------KKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 542 RILLLDEATSALDAESE----RVVQEaldRIMVNRTTVVVAHRLSTVrnaDMIA-VIH 594
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLAVL---DYLSdYIH 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
390-599 |
7.86e-11 |
|
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: 62.67 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 390 YFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKST----VVSLIERFYDPQaGDVLIDGINLKEFQLKWiRSKIGLV 465
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKY-PGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 466 SQE----PVLftasikdniaygkedaTTEE-IKAAAELaNASKFVDKLpqgldtmvgehgtqlSGGQKQRIAVARAILKD 540
Cdd:cd03233 89 SEEdvhfPTL----------------TVREtLDFALRC-KGNEFVRGI---------------SGGERKRVSIAEALVSR 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 541 PRILLLDEATSALDAEServvqeALDRIMVNRTtvvVAHRLSTVRNA-------------DMIAVIHQGKIV 599
Cdd:cd03233 137 ASVLCWDNSTRGLDSST------ALEILKCIRT---MADVLKTTTFVslyqasdeiydlfDKVLVLYEGRQI 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
404-594 |
8.61e-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: 65.96 E-value: 8.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLF----ISSGTTVALVGQSGSGKSTVVS-----LIERFYDPQAgDVLIDGInLKEFQ-------LKWIRS------- 460
Cdd:COG1245 87 GFRLYglpvPKKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDE-EPSWDEV-LKRFRgtelqdyFKKLANgeikvah 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 461 KIGLVSQEPVLFTASIKdniaygkedattEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKD 540
Cdd:COG1245 165 KPQYVDLIPKVFKGTVR------------ELLEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 541 PRILLLDEATSALD----AESERVVQEALDRimvNRTTVVVAHRLSTVrnaDMIA-VIH 594
Cdd:COG1245 231 ADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAIL---DYLAdYVH 283
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
398-653 |
9.61e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 65.58 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDV-LIDGINLKEF---QLKWIRSkiglvSQEPVLFT 473
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFaqhQLEFLRA-----DESPLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 474 ASIkdniaygkedatteeikaaAELANASKFVDKLP----QGldTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:PRK10636 399 ARL-------------------APQELEQKLRDYLGgfgfQG--DKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 550 TSALDAESERVVQEALdrIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKiVEkgSHTELLKDpegaYSQ-LIRLQEEKKS 627
Cdd:PRK10636 458 TNHLDLDMRQALTEAL--IDFEGALVVVSHDRHLLRStTDDLYLVHDGK-VE--PFDGDLED----YQQwLSDVQKQENQ 528
|
250 260
....*....|....*....|....*.
gi 1063707070 628 DENAAEEQKMSSIESFKQSSLRKSSL 653
Cdd:PRK10636 529 TDEAPKENNANSAQARKDQKRREAEL 554
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
404-599 |
1.09e-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: 65.23 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYdPQA---GDVLIDGINLKEFQLKWIRSK-IGLVSQEPVLF-TASIKD 478
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpELSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 479 NIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL-DAES 557
Cdd:TIGR02633 98 NIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLtEKET 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1063707070 558 ERVVQEALDRIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIV 599
Cdd:TIGR02633 178 EILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
395-563 |
1.14e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.20 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 395 ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIRSKIGLVSQ----EPV 470
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHrnamKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 LftaSIKDNIA-----YGKEDATTEEIKAAAELANaskfVDKLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILL 545
Cdd:PRK13539 88 L---TVAENLEfwaafLGGEELDIAAALEAVGLAP----LAHLPFG----------YLSAGQKRRVALARLLVSNRPIWI 150
|
170
....*....|....*...
gi 1063707070 546 LDEATSALDAESERVVQE 563
Cdd:PRK13539 151 LDEPTAALDAAAVALFAE 168
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
761-977 |
1.40e-10 |
|
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: 63.58 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 761 FWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSL 840
Cdd:cd18541 41 RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRMALGPGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 841 AQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAE 920
Cdd:cd18541 119 LYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 921 DKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18541 199 EAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTIT 255
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
404-612 |
1.57e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 62.70 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKWIrSKIGLVS--QEPVLF---TA---- 474
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFremTVienl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 ------SIKDNIAYGKEdATTEEIKAAAE-LANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:PRK11300 102 lvaqhqQLKTGLFSGLL-KTPAFRRAESEaLDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 548 EATSALDAESERVVQEALD--RIMVNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPE 612
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
416-600 |
1.61e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.81 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 416 ALVGQSGSGKST---VVSLIERF--YDpqaGDVLIDGinlKEFQLKWIRS--KIGLV--SQE----PVLftaSIKDNIAY 482
Cdd:NF040905 31 ALCGENGAGKSTlmkVLSGVYPHgsYE---GEILFDG---EVCRFKDIRDseALGIViiHQElaliPYL---SIAENIFL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 483 GKEDATTEEIKAAAELANASKFVDKLpqGL----DTMVGEHGTqlsgGQKQRIAVARAILKDPRILLLDEATSAL-DAES 557
Cdd:NF040905 102 GNERAKRGVIDWNETNRRARELLAKV--GLdespDTLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAALnEEDS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063707070 558 ERVvqeaLDRIMVNR----TTVVVAHRLSTVRN-ADMIAVIHQGKIVE 600
Cdd:NF040905 176 AAL----LDLLLELKaqgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
763-977 |
1.66e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 63.28 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 763 AIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQ 842
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHER--ETSGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 843 TVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALngflymkFMKGFSADAKKMYGEA-SQVAN------DAVGSIRTVA 915
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-------ATRWFRRRSSRAYRRArERIAAvnadlqETLAGIRVVQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 916 SFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18546 193 AFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLT 254
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
396-567 |
2.68e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 396 RPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK----EF--QLKWIRSKIG----LV 465
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdEYhqDLLYLGHQPGikteLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 466 SQEPVLFTASIKDniaygkeDATTEEIKAAAELANASKFVDkLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILL 545
Cdd:PRK13538 91 ALENLRFYQRLHG-------PGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWI 152
|
170 180
....*....|....*....|..
gi 1063707070 546 LDEATSALDAESERVVQEALDR 567
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
719-977 |
4.01e-10 |
|
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: 62.11 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 719 VLILGSISAAAnGVILPIfgiLISSVI-KAFFQPpkklkeDTS--FWAIIFMV-LGFASIIAYPAQTFFFAIAGCKLVQR 794
Cdd:cd18550 4 VLLLILLSALL-GLLPPL---LLREIIdDALPQG------DLGllVLLALGMVaVAVASALLGVVQTYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 795 IRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPL 874
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTR--TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 875 IALNGFLYMKFMKGFSADAKKMYGEASQVAND--AVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVsGIGFGFS 952
Cdd:cd18550 152 FVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALA-GRWFFAA 230
|
250 260
....*....|....*....|....*.
gi 1063707070 953 FFVLFSSYAASFY-VGARLVDDGKTT 977
Cdd:cd18550 231 LGLFTAIGPALVYwVGGLLVIGGGLT 256
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
398-622 |
9.16e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLI--ERFYDPQAGDVLIDGINLKEFQLKWIRSK-IGLVSQEPV---- 470
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEgIFMAFQYPVeipg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 ----LFTASIKDNIAYGKEDATTEEIKAAAELANASKFVdKLPQGLDTMVGEHGtqLSGGQKQRIAVARAILKDPRILLL 546
Cdd:PRK09580 93 vsnqFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALL-KMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCIL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 547 DEATSALDAESERVVQEALDRIM-VNRTTVVVAH--RLSTVRNADMIAVIHQGKIVEKGSHTELLKDPEGAYSQLIRLQ 622
Cdd:PRK09580 170 DESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGYGWLTEQQ 248
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
398-572 |
1.27e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 398 DEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLK------EFQLKWIRSKIGLvsqEPVL 471
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKkdlctyQKQLCFVGHRSGI---NPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 ftaSIKDNIAYGKEDATTE-EIKAAAELANASKFVDkLPQGLdtmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEAT 550
Cdd:PRK13540 90 ---TLRENCLYDIHFSPGAvGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180
....*....|....*....|..
gi 1063707070 551 SALDaesERVVQEALDRIMVNR 572
Cdd:PRK13540 156 VALD---ELSLLTIITKIQEHR 174
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
719-977 |
1.97e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 59.83 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 719 VLILGSISAAANGVILPIFGILISSVIKAffqppkkLKEDTSFWAIIFMVLGFASI-----IAYPAQTFFFAIAGCKLVQ 793
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDDVLIQ-------LGPGGNTSLLLLLVLGLAGAyvlsaLLGILRGRLLARLGERITA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 794 RIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLP 873
Cdd:cd18563 77 DLRRDLYEHLQRLSLSFFDK--RQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 874 LIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSF 953
Cdd:cd18563 155 LVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLT 234
|
250 260
....*....|....*....|....
gi 1063707070 954 FVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18563 235 FLTSLGTLIVWYFGGRQVLSGTMT 258
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
411-591 |
2.38e-09 |
|
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: 57.00 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 411 SGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVL-IDGINLKEFQLKWIRskiglvsqepvlftasikdniaygkedatt 489
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 490 eeikaaaelanaskfvdklpqglDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALD--- 566
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180
....*....|....*....|....*....
gi 1063707070 567 ----RIMVNRTTVVVAHRLSTVRNADMIA 591
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
714-977 |
2.43e-09 |
|
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: 59.77 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 714 KPEIPVLILGSISAAANGVILPIF-GILISSVIkaffqpPKKLKEDTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLV 792
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFfQILIDDII------PSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 793 QRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSaDAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAML 872
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFET--RKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLII 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 873 PLIALNGFLYMKFMKgfSADAKKMYGEASQVAN--DAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFG 950
Cdd:cd18570 152 PLYILIILLFNKPFK--KKNREVMESNAELNSYliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSS 229
|
250 260
....*....|....*....|....*..
gi 1063707070 951 FSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18570 230 IKGLISLIGSLLILWIGSYLVIKGQLS 256
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
714-978 |
2.53e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 59.80 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 714 KPEIPVLILGSISAAANGVILPIFgilISSVIKAFFQPpkklKEDTSFWAIIFMVLGFASIIAypAQTFFFAIAGCKL-- 791
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLL---TKYAIDHFITP----GTLDGLTGFILLYLGLILIQA--LSVFLFIRLAGKIem 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 792 -VQR-IRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVL 869
Cdd:cd18540 72 gVSYdLRKKAFEHLQTLSFSYFDK--TPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 870 AMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDKVMNMYSKKCEgPMKN-GIRQGIVSGIg 948
Cdd:cd18540 150 AVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTE-EMRRaSVRAARLSAL- 227
|
250 260 270
....*....|....*....|....*....|...
gi 1063707070 949 fgFSFFVLFSSYAAS---FYVGARLVDDGKTTF 978
Cdd:cd18540 228 --FLPIVLFLGSIATalvLWYGGILVLAGAITI 258
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
403-609 |
3.35e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 59.72 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGIN----LKEFqlkwiRSKIGLV----SQ----EPV 470
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrRKEF-----ARRIGVVfgqrSQlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 LFTASIKDNIaYGKEDATTEE-IKAAAELANASKFvdklpqgLDTMVgehgTQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:COG4586 114 IDSFRLLKAI-YRIPDAEYKKrLDELVELLDLGEL-------LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEP 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 550 TSALDAESERVVQEALDRImvNR---TTVVVA-HRLSTVRN-ADMIAVIHQGKIVEKGSHTELLK 609
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEY--NRergTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
404-601 |
4.51e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIRSK----IGLVSQE----PVLftaS 475
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQElnliPQL---T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 476 IKDNIAYGKEDATT-EEIKAAAELANASKFVDKL--PQGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK10762 96 IAENIFLGREFVNRfGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 553 L-DAESE---RVVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGK-IVEK 601
Cdd:PRK10762 172 LtDTETEslfRVIRELKSQ---GRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
406-600 |
4.68e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.92 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLKWIR----SKIGLVSQE----PVLftaSIK 477
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTaalaAGVAIIYQElhlvPEM---TVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 478 DNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLD--TMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDA 555
Cdd:PRK11288 98 ENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063707070 556 -ESE---RVVQEALDRimvNRTTVVVAHRLSTV-RNADMIAVIHQGKIVE 600
Cdd:PRK11288 174 rEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
404-591 |
5.05e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 404 GFSLFISSGT-----TVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDginLK-EFQLKWIRSKI-GLVSQepvlFTASI 476
Cdd:PRK13409 352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKPDYdGTVED----LLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 477 KDNIAygkedatTEEIKAaaELANaskfvdklPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAE 556
Cdd:PRK13409 425 TDDLG-------SSYYKS--EIIK--------PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063707070 557 SERVVQEALDRIMVNR--TTVVVAHRLSTVrnaDMIA 591
Cdd:PRK13409 488 QRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
384-562 |
8.19e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.49 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVL--------------IDGIN 449
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 450 LkefqlkwirskiglvSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELAnaskfvdklpqgLDTMVgehgtQLSGGQKQ 529
Cdd:PLN03073 587 L---------------SSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLA------------LQPMY-----TLSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALDAES-ERVVQ 562
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
720-921 |
9.24e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 57.88 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVilpiFGILISSVIKAFFQPPKKLKEDTSFWAIIFMVLGFASIIAypAQTF---FFAIAGCKLVQ-RI 795
Cdd:cd18543 1 LILALLAALLATL----AGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEA--VLSFlrrYLAGRLSLGVEhDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 796 RSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGdSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLI 875
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDR--WQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1063707070 876 ALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18543 152 VLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRER 197
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
63-262 |
1.02e-08 |
|
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: 57.96 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 63 MILGTLGSIGNGLgFPLM-TLLFGDLIDAFGENQTNTTDKVSK------VALKFVWLGIGTFAAAFLQ-----LSGWMIS 130
Cdd:cd18565 1 LVLGLLASILNRL-FDLApPLLIGVAIDAVFNGEASFLPLVPAslgpadPRGQLWLLGGLTVAAFLLEslfqyLSGVLWR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 131 GERQAAR--IRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTL 208
Cdd:cd18565 80 RFAQRVQhdLRTDTYDHVQRLDMAFFE-DRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 209 VMLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGE 262
Cdd:cd18565 159 VALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAE 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
406-602 |
1.32e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQLKW-IRSKIGLVSQE-PVLFTASIKDNIAYG 483
Cdd:PRK09700 25 NLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLaAQLGIGIIYQElSVIDELTVLENLYIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 484 KE-----------DATTEEIKAAAELANASKFVDklpqgLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLDEATSA 552
Cdd:PRK09700 105 RHltkkvcgvniiDWREMRVRAAMMLLRVGLKVD-----LDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1063707070 553 L-DAESERVVQeALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKIVEKG 602
Cdd:PRK09700 176 LtNKEVDYLFL-IMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
720-921 |
1.40e-08 |
|
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: 57.16 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 720 LILGSISAAANGVILPIFGILISSVIKAFFQPPKKLkedTSFWAIIFMVLGfasiiAYPAQTFFFAI-------AGCKLV 792
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL---GLLLGLALLLLG-----AYLLRALLNFLriylnhvAEQKVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 793 QRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAML 872
Cdd:cd18778 73 ADLRSDLYDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1063707070 873 PLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18778 151 PFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREE 199
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
52-321 |
1.42e-08 |
|
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: 57.40 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 52 FAFAdsfdFLLMILGTLGSIgnglgfpLMTLLFGDLIDAFGENQTNTTDKVSKVALKFVWLGIGTFAAAFLQ--LSGWMi 129
Cdd:cd18544 1 FILA----LLLLLLATALEL-------LGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQtyLLQKL- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 130 sGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLV 209
Cdd:cd18544 69 -GQRIIYDLRRDLFSHIQRLPLSFFD-RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 210 MLSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTGL 289
Cdd:cd18544 147 SLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFAL 226
|
250 260 270
....*....|....*....|....*....|..
gi 1063707070 290 GLGTLFLVVFCSYALAVWYGGKLILDKGYTGG 321
Cdd:cd18544 227 FRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
387-596 |
1.54e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.71 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 387 KDVYFTYP-ARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTV---------VSLIErfydpqaGDVLIDGINLKE-FQl 455
Cdd:cd03232 7 KNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLldvlagrktAGVIT-------GEILINGRPLDKnFQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 456 kwiRSkIGLVSQEPVLFtasikdniaygkEDATTEEikaaaelanASKFVDKLpQGldtmvgehgtqLSGGQKQRIAVAR 535
Cdd:cd03232 79 ---RS-TGYVEQQDVHS------------PNLTVRE---------ALRFSALL-RG-----------LSVEQRKRLTIGV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 536 AILKDPRILLLDEATSALDAESERVVQEALDRI-MVNRTTVVVAHRLSTV--RNADMIAVIHQG 596
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
384-620 |
1.66e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.81 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYpaRPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfQLKwiRSKIG 463
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-ALQ--KNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQE-------PVLftasIKDNIAYGKEDATTEEIKAAAElanASKFVDKLPQGLDTMVGEHGT--QLSGGQKQRIAVA 534
Cdd:PRK15056 82 YVPQSeevdwsfPVL----VEDVVMMGRYGHMGWLRRAKKR---DRQIVTAALARVDMVEFRHRQigELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 535 RAILKDPRILLLDEATSALDAESE-RVVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKG--SHTELLKDP 611
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGptETTFTAENL 234
|
....*....
gi 1063707070 612 EGAYSQLIR 620
Cdd:PRK15056 235 ELAFSGVLR 243
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
406-620 |
1.72e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.50 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLI--------------ERFYDpqagdvlIDGINLKEFQL-KWIRSKIGLVSQEP- 469
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdnwrvtadrMRFDD-------IDLLRLSPRERrKLVGHNVSMIFQEPq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 470 --VLFTASIKDNIAYGKEDATTE---------EIKAAAELANASKFVDKlpqglDTMVGEHGTQLSGGQKQRIAVARAIL 538
Cdd:PRK15093 100 scLDPSERVGRQLMQNIPGWTYKgrwwqrfgwRKRRAIELLHRVGIKDH-----KDAMRSFPYELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV--VAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDPEGAY 615
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQTVETAPSKELVTTPHHPY 254
|
....*.
gi 1063707070 616 SQ-LIR 620
Cdd:PRK15093 255 TQaLIR 260
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
403-599 |
1.87e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.11 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLI--ERfyDPQAGDVLIDGINLKEFQ-LKWIRSKIGLVSQEP-----VLfTA 474
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSpRERRRLGVAYIPEDRlgrglVP-DM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 SIKDNIA----YGKEDATTEEIKAAAELANASKFVDKL---PQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:COG3845 352 SVAENLIlgryRRPPFSRGGFLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 548 EATSALDAES-----ERVVQEA------------LDRIMvnrttvvvahRLStvrnaDMIAVIHQGKIV 599
Cdd:COG3845 428 QPTRGLDVGAiefihQRLLELRdagaavllisedLDEIL----------ALS-----DRIAVMYEGRIV 481
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
384-584 |
1.98e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 56.28 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARpdeQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginLKEFQLkwirsKIG 463
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKL-----RIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 LVSQ----EPVL-FTASIKDNIAYGKEDAtteEIKAAAELANASKFVDKLPQgldtmvgehgtQLSGGQKQRIAVARAIL 538
Cdd:PRK09544 71 YVPQklylDTTLpLTVNRFLRLRPGTKKE---DILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALL 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063707070 539 KDPRILLLDEATSALDAESERVVQEALDRIM--VNRTTVVVAHRLSTV 584
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRreLDCAVLMVSHDLHLV 184
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
401-597 |
2.56e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.97 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 401 IFRGFSLFISSGTTVALVGQSGSGKSTVVSLIE-RFYDPQ-AGDVLIDGINLKefqlKWIRSKIGLVSQEPVL------- 471
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPT----KQILKRTGFVTQDDILyphltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 ----FTASIKDNIAYGKEDATTEEIKAAAELAnaskfvdkLPQGLDTMVGEHGTQ-LSGGQKQRIAVARAILKDPRILLL 546
Cdd:PLN03211 159 etlvFCSLLRLPKSLTKQEKILVAESVISELG--------LTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 547 DEATSALDAESE-RVVQEALDRIMVNRTTVVVAHRLST--VRNADMIAVIHQGK 597
Cdd:PLN03211 231 DEPTSGLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
762-978 |
2.58e-08 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 56.64 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 762 WAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLA 841
Cdd:cd18548 41 TGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDK--FGTSSLITRLTNDVTQVQNFVMMLLR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 842 QTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18548 119 MLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNRED 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063707070 922 KVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTF 978
Cdd:cd18548 199 YEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQV 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
388-591 |
4.25e-08 |
|
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: 57.10 E-value: 4.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 388 DVYFTYPARpdEQIFRGFSLFISSGT-----TVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginlkEFQLKwirski 462
Cdd:COG1245 339 ETLVEYPDL--TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 glvsqepvlftasikdnIAY------GKEDATTEEI--KAAAELANASKF---------VDKLpqgLDTMVGEhgtqLSG 525
Cdd:COG1245 403 -----------------ISYkpqyisPDYDGTVEEFlrSANTDDFGSSYYkteiikplgLEKL---LDKNVKD----LSG 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 526 GQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNR--TTVVVAHRLSTVrnaDMIA 591
Cdd:COG1245 459 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
61-323 |
5.10e-08 |
|
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: 55.57 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 61 LLMILGTLGsIGNGLGfPLMTLLFGDLID-AFGENQTNTtdkvskvalkFVWLGIGTFAAAFLQ---------LSGWMis 130
Cdd:cd18550 1 LALVLLLIL-LSALLG-LLPPLLLREIIDdALPQGDLGL----------LVLLALGMVAVAVASallgvvqtyLSARI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 131 GERQAARIRSLYLKTILRQDIAFFdIDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVM 210
Cdd:cd18550 67 GQGVMYDLRVQLYAHLQRMSLAFF-TRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 211 LSSIPLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQT--IGSIRTVASFTGEKQAISNYNKHLVTAYKAGVIEGGSTG 288
Cdd:cd18550 146 LVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGR 225
|
250 260 270
....*....|....*....|....*....|....*
gi 1063707070 289 LGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQV 323
Cdd:cd18550 226 WFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTL 260
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
368-557 |
5.65e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 368 DSYSTNGKVLDD--IKGDI-ELKDVYFTYPARPDE-QIFRGFSLFISSGTTVALVGQSGSGKSTVVS-LIERFYDP--QA 440
Cdd:TIGR00956 741 ESDDVNDEKDMEkeSGEDIfHWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVTTGviTG 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 441 GDVLIDGINLKE-FQlkwiRSkIGLVSQEPV-LFTASIKDNIAYgkedatTEEIKAAAELANASK--FVDKLPQGL---- 512
Cdd:TIGR00956 821 GDRLVNGRPLDSsFQ----RS-IGYVQQQDLhLPTSTVRESLRF------SAYLRQPKSVSKSEKmeYVEEVIKLLemes 889
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1063707070 513 --DTMVGEHGTQLSGGQKQRIAVARAILKDPRILL-LDEATSALDAES 557
Cdd:TIGR00956 890 yaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
137-336 |
6.91e-08 |
|
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: 55.14 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 137 RIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSgDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18570 76 RLILGYFKHLLKLPLSFFE-TRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 217 LvmagALLAIVIAKTASRGQTAYAKAATVVE----QTIGSIRTVASFTGEKQAI----SNYNKHLVTAYKAGVIEGGSTG 288
Cdd:cd18570 154 Y----ILIILLFNKPFKKKNREVMESNAELNsyliESLKGIETIKSLNAEEQFLkkieKKFSKLLKKSFKLGKLSNLQSS 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1063707070 289 LGLgtlfLVVFCSYALAVWYGGKLILDKGYTGGQVL--NIIIAVLTGSMS 336
Cdd:cd18570 230 IKG----LISLIGSLLILWIGSYLVIKGQLSLGQLIafNALLGYFLGPIE 275
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
763-932 |
1.00e-07 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 54.78 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 763 AIIFMVL-GFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLA 841
Cdd:cd18589 38 AITVMSLlTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDS--NQTGDIVSRVTTDTEDMSESLSENLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 842 QTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18589 116 LLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEE 195
|
170
....*....|.
gi 1063707070 922 KVMNMYSKKCE 932
Cdd:cd18589 196 GEAQRYRQRLQ 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
384-579 |
1.17e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYPARPdeqIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVlidginlkefqlKWirskig 463
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KW------ 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 464 lvsqepvlftaSIKDNIAYGKEDAtteeikaAAELANASKFVD-----KLPQGLDTMV-GEHG-------------TQLS 524
Cdd:PRK15064 379 -----------SENANIGYYAQDH-------AYDFENDLTLFDwmsqwRQEGDDEQAVrGTLGrllfsqddikksvKVLS 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 525 GGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDriMVNRTTVVVAH 579
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE--KYEGTLIFVSH 493
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
405-598 |
1.36e-07 |
|
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: 55.22 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 405 FSLfiSSGTTVALVGQSGSGKSTVVSLIERFYDPQ-AGDVLIDG--INLKEFQlKWIRSKIGLVSQE-------PVL--- 471
Cdd:TIGR02633 281 FSL--RRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPA-QAIRAGIAMVPEDrkrhgivPILgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 --FTASIKDNIAY-GKEDATTEE--IKAAAELANASKFVDKLPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRILLL 546
Cdd:TIGR02633 358 knITLSVLKSFCFkMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 547 DEATSALD----AESERVV-QEALDRIMVnrttVVVAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:TIGR02633 428 DEPTRGVDvgakYEIYKLInQLAQEGVAI----IVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
412-590 |
2.68e-07 |
|
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: 53.00 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 412 GTTVALVGQSGSGKSTVV------SLIERFY----DPQAGDVlIDGINLKEfqlkwirsKIGLVSQEPV----------- 470
Cdd:cd03271 21 GVLTCVTGVSGSGKSSLIndtlypALARRLHlkkeQPGNHDR-IEGLEHID--------KVIVIDQSPIgrtprsnpaty 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 471 --LFTaSIKD----------------NIAY-GKE-----DATTEEikaAAEL-ANASKFVDKLPQ----GLDTM-VGEHG 520
Cdd:cd03271 92 tgVFD-EIRElfcevckgkrynretlEVRYkGKSiadvlDMTVEE---ALEFfENIPKIARKLQTlcdvGLGYIkLGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 521 TQLSGGQKQRIAVARAILKDPR---ILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRNADMI 590
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIeHNLDVIKCADWI 241
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
759-978 |
3.05e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 53.37 E-value: 3.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 759 TSFWAIIFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSaDAATIRG-LVG 837
Cdd:cd18782 42 YVIGVVMLVAALLEAVLTA-LRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDK--RPVGELSTRIS-ELDTIRGfLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 838 DSLAQTVQNLSSILAgLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASF 917
Cdd:cd18782 118 TALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQ 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 918 CAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTTF 978
Cdd:cd18782 197 NAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTL 257
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
60-315 |
3.54e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 52.92 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIGNGLGFPLMTllfGDLIDAFGENQtNTTDKVSKVALkfvwLGIGTFAA-AFLQ-LSGWM--ISGERQA 135
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLI---RELVDLVTIGS-KSLGLLLGLAL----LLLGAYLLrALLNfLRIYLnhVAEQKVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 136 ARIRS-LYLKtILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSI 214
Cdd:cd18778 73 ADLRSdLYDK-LQRLSLRYFD-DRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 215 PLLVMAGALLAIVIAKTASRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNYNKhLVTAYKAGVIEGGSTGLGLGTl 294
Cdd:cd18778 151 PFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA-LSRRYRKAQLRAMKLWAIFHP- 228
|
250 260
....*....|....*....|....
gi 1063707070 295 fLVVF---CSYALAVWYGGKLILD 315
Cdd:cd18778 229 -LMEFltsLGTVLVLGFGGRLVLA 251
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
765-977 |
5.40e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 52.59 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 765 IFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLsADAATIRGLVGDSLAQTV 844
Cdd:cd18566 48 VVIAILLESLLRL-LRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFER--EPSGAHLERL-NSLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 845 QNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMK-----GFSADAKKMygeasQVANDAVGSIRTVASFCA 919
Cdd:cd18566 124 LDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRralkeRSRADERRQ-----NFLIETLTGIHTIKAMAM 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 920 E----DKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAasfyVGARLVDDGKTT 977
Cdd:cd18566 199 EpqmlRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVA----FGALLVINGDLT 256
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
115-279 |
7.58e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 52.11 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 115 GTFAAAFLQLSGWMisGER--QAARIRSLylKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATF 192
Cdd:cd18546 53 WVAQRAQTRLTGRT--GERllYDLRLRVF--AHLQRLSLDFHE-RETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 193 VGGFVIAFVRGWLLTLVMLSSIPLLvmagALLAIVIAKTASRgqtAYAKA--------ATVVEqTIGSIRTVASFTGEKQ 264
Cdd:cd18546 128 VGIAVVLLVLDPRLALVALAALPPL----ALATRWFRRRSSR---AYRRAreriaavnADLQE-TLAGIRVVQAFRRERR 199
|
170
....*....|....*
gi 1063707070 265 AISNYnKHLVTAYKA 279
Cdd:cd18546 200 NAERF-AELSDDYRD 213
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
60-335 |
8.52e-07 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 52.02 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSigngLGFPLMTllfGDLIDAFgeNQTNTTDKVSKVALKFVWLGIGTFAAAFLqlSGWMIS--GERQAAR 137
Cdd:cd18548 5 PLFKLLEVLLE----LLLPTLM---ADIIDEG--IANGDLSYILRTGLLMLLLALLGLIAGIL--AGYFAAkaSQGFGRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 138 IRS-LYLKTilrQDIAFFDIDT-NTGEVVGRMSGDTVLIQDAmgekVGKAIQLLA----TFVGGFVIAFVRGWLLTLVML 211
Cdd:cd18548 74 LRKdLFEKI---QSFSFAEIDKfGTSSLITRLTNDVTQVQNF----VMMLLRMLVrapiMLIGAIIMAFRINPKLALILL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 212 SSIPLLVmagALLAIVIAKTA---SRGQTAYAKAATVVEQTIGSIRTVASFTGEKQAISNY---NKHLV-TAYKAGVIeg 284
Cdd:cd18548 147 VAIPILA---LVVFLIMKKAIplfKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFdkaNDDLTdTSLKAGRL-- 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 285 gsTGLGLGTLFLVVFCSYALAVWYGGKLILDKGYTGGQV-------LNIIIAVLTGSM 335
Cdd:cd18548 222 --MALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
385-566 |
8.54e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIdGINLKefqlkwirskIGL 464
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE----------VAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQ-----EPvlfTASIKDNIAYGKEDATTEEIKAAAelanASKFVDKL--PQGLDTMVgehgTQLSGGQKQRIAVARAI 537
Cdd:PRK11147 387 FDQhraelDP---EKTVMDNLAEGKQEVMVNGRPRHV----LGYLQDFLfhPKRAMTPV----KALSGGERNRLLLARLF 455
|
170 180
....*....|....*....|....*....
gi 1063707070 538 LKDPRILLLDEATSALDAESERVVQEALD 566
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
409-582 |
1.12e-06 |
|
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: 52.44 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 409 ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefqlkwiRSKIGLVSQEPVLFTASIKDNIAY------ 482
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIYpdssed 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 483 ----GKEDATTEEIKAAAELANaskfVDKLPQGLDTmVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESE 558
Cdd:TIGR00954 544 mkrrGLSDKDLEQILDNVQLTH----ILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
170 180
....*....|....*....|....
gi 1063707070 559 RVVQEALDRimVNRTTVVVAHRLS 582
Cdd:TIGR00954 619 GYMYRLCRE--FGITLFSVSHRKS 640
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
422-598 |
1.26e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 422 GSGKSTVVSLIERFYDPQ-AGDVLIDGINLK-EFQLKWIRSKIGLVSQE-------PVLftaSIKDNIAYGKED--ATTE 490
Cdd:PRK13549 298 GAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAALDrfTGGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 491 EIKAAAELANASKFVDKL---PQGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD--AESE------R 559
Cdd:PRK13549 375 RIDDAAELKTILESIQRLkvkTASPELAIA----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyklinQ 450
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1063707070 560 VVQEALDRIMvnrttvvVAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:PRK13549 451 LVQQGVAIIV-------ISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
757-887 |
1.66e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 50.97 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 757 EDTSFWAIIFMVLGF-ASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGL 835
Cdd:cd18580 35 SSSGYYLGVYAALLVlASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFDT--TPSGRILNRFSKDIGLIDEE 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 836 VGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVlamLPLIALNGFLYMKFMK 887
Cdd:cd18580 113 LPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL---PPLLVVYYLLQRYYLR 161
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
60-321 |
1.87e-06 |
|
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: 50.93 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 60 FLLMILGTLGSIGNGLGFPLmtlLFGDLIDAFGENQtNTTDkVSKVALKFVWLGIGTFAAAFLQ--LSGWMisGERQAAR 137
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPY---LIKIAIDEYIPNG-DLSG-LLIIALLFLALNLVNWVASRLRiyLMAKV--GQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 138 IRS-LYLKtILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLLATFVGGFVIAFVRGWLLTLVMLSSIPL 216
Cdd:cd18545 75 LRQdLFSH-LQKLSFSFFD-SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 217 LVmagaLLAIVIAKTASRG-QTAYAKAATV---VEQTIGSIRTVASFTGEKQAISNYNKHLVTAYKAGViegGSTGLGLG 292
Cdd:cd18545 153 LV----LVVFLLRRRARKAwQRVRKKISNLnayLHESISGIRVIQSFAREDENEEIFDELNRENRKANM---RAVRLNAL 225
|
250 260 270
....*....|....*....|....*....|..
gi 1063707070 293 TLFLVVFCS---YALAVWYGGKLILDKGYTGG 321
Cdd:cd18545 226 FWPLVELISalgTALVYWYGGKLVLGGAITVG 257
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
400-582 |
3.61e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.39 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKSTVVSL---------IErfydpqaGDVLIDGINLKEFQLKWIRskiGLVSQ--- 467
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVlagrktggyIE-------GDIRISGFPKKQETFARIS---GYCEQndi 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 468 --------EPVLFTASIKDNIAYGKEDAT--TEEIKAAAELANASkfvdklpqglDTMVGEHG-TQLSGGQKQRIAVARA 536
Cdd:PLN03140 964 hspqvtvrESLIYSAFLRLPKEVSKEEKMmfVDEVMELVELDNLK----------DAIVGLPGvTGLSTEQRKRLTIAVE 1033
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEAL-DRIMVNRTTVVVAHRLS 582
Cdd:PLN03140 1034 LVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
486-651 |
4.30e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 486 DATTEEIKAAAELANASKFVDklpqgldtMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEAL 565
Cdd:PLN03073 316 DAYTAEARAASILAGLSFTPE--------MQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 566 drIMVNRTTVVVAHRLSTVrNADMIAVIHQgkivekgsHTELLKDPEGAYSQLIRLQEEKKSDENAA---EEQKMSSIES 642
Cdd:PLN03073 388 --LKWPKTFIVVSHAREFL-NTVVTDILHL--------HGQKLVTYKGDYDTFERTREEQLKNQQKAfesNERSRSHMQA 456
|
170
....*....|....*..
gi 1063707070 643 F--------KQSSLRKS 651
Cdd:PLN03073 457 FidkfrynaKRASLVQS 473
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
407-557 |
5.70e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 407 LFISSGTTVALVGQSGSGKSTVVSLIerfydpqAGDVLID-GINLKEFQLKWIRskigLVSQEPVLFTASIKDNIAYG-K 484
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDLIVAR----LQQDPPRNVEGTVYDFVAEGiE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 485 EDA-----------------------TTEEIKAAAELANASKFVDKLPQGL-------DTMVGEhgtqLSGGQKQRIAVA 534
Cdd:PRK11147 93 EQAeylkryhdishlvetdpseknlnELAKLQEQLDHHNLWQLENRINEVLaqlgldpDAALSS----LSGGWLRKAALG 168
|
170 180
....*....|....*....|...
gi 1063707070 535 RAILKDPRILLLDEATSALDAES 557
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIET 191
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
758-884 |
5.74e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 49.39 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 758 DTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVG 837
Cdd:cd18604 41 SVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDT--TPVGRILNRFSKDIETIDSELA 118
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063707070 838 DSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMK 884
Cdd:cd18604 119 DSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLR 165
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
831-977 |
9.46e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 48.71 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 831 TIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKG-----FSADAKKMygeaSQVAn 905
Cdd:cd18568 110 KIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRnsreiFQANAEQQ----SFLV- 184
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063707070 906 DAVGSIRTVASFCAEDKV----MNMYSKKCEGPMKnGIRQGIVSGIGFGFSFFVlfsSYAASFYVGARLVDDGKTT 977
Cdd:cd18568 185 EALTGIATIKALAAERPIrwrwENKFAKALNTRFR-GQKLSIVLQLISSLINHL---GTIAVLWYGAYLVISGQLT 256
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
486-607 |
1.11e-05 |
|
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: 49.63 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 486 DATTEEikaaaelanASKFVDKLP---QGLDTMV---------GEHGTQLSGGQKQRIAVARAILKD---PRILLLDEAT 550
Cdd:TIGR00630 790 DMTVEE---------AYEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT 860
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 551 SALDAESERVVQEALDRIMVNRTTVVV-AHRLSTVRNADMIAVI------HQGKIVEKGSHTEL 607
Cdd:TIGR00630 861 TGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
405-606 |
1.58e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 405 FSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlKEFQLK----WIRSKIGLV----SQEPVLFTASI 476
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRsprdAIRAGIMLCpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 477 KDNI---AYGKEDATTEEIKAAAELANASKFVDKL----PQGlDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEA 549
Cdd:PRK11288 349 ADNInisARRHHLRAGCLINNRWEAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 550 TSALD--AESE--RVVQEALDRimvNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTE 606
Cdd:PRK11288 424 TRGIDvgAKHEiyNVIYELAAQ---GVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
385-672 |
2.14e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 385 ELKDVYFTYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefQLKWIRSKIGL 464
Cdd:PRK13545 23 KLKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 465 VSQEPVLFTASIKDNIAYGKEDATTEEIKAAAELANASKFVDklpQGLDTMvgehgtqlSGGQKQRIAVARAILKDPRIL 544
Cdd:PRK13545 97 NGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIY---QPVKTY--------SSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 545 LLDEATSALDAESERVVQEALDRIMVN-RTTVVVAHRLSTVRNADMIAV-IHQGKIVEKGSHTELLKDpegaYSQLIRL- 621
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDH----YDEFLKKy 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1063707070 622 -QEEKKSDENAAEEQkmssIESFKQSSLRKSSLGRSLSKggsSRGNSSRHSF 672
Cdd:PRK13545 242 nQMSVEERKDFREEQ----ISQFQHGLLQEDQTGRERKR---KKGKKTSRKF 286
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
409-581 |
3.48e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 409 ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGInlkefqlkwirskiglvsqepvlfTASIKdniaygkedat 488
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------------------TPVYK----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 489 teeikaaaelanaskfvdklPQGLDtmvgehgtqLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRI 568
Cdd:cd03222 67 --------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170
....*....|....*
gi 1063707070 569 MVN--RTTVVVAHRL 581
Cdd:cd03222 118 SEEgkKTALVVEHDL 132
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
407-553 |
3.64e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 407 LFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDG--INLKEFQlKWIRSKIGLVSQE-PVLFTASIKDNIAYG 483
Cdd:PRK10982 19 LKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSK-EALENGISMVHQElNLVLQRSVMDNMWLG 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 484 KEDATTEEIKAAAELANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSAL 553
Cdd:PRK10982 98 RYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
402-598 |
3.79e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.35 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGFSLFISSGTTVALVGQSGSGKStvvSLIERFY---DPQAGDVLIDGINLKEFQLKwIRSKIGLV-----SQEPVLF- 472
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 473 TASIKDNIAY------------GKEDATTEEIKAAAELanasKFvdklpqgldtmvgEHGTQ----LSGGQKQRIAVARA 536
Cdd:PRK15439 355 DAPLAWNVCAlthnrrgfwikpARENAVLERYRRALNI----KF-------------NHAEQaartLSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 537 ILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVV-VAHRLSTVRN-ADMIAVIHQGKI 598
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
400-554 |
4.41e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLF-------ISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkEFQLKWirskiglVSQE-PVL 471
Cdd:PRK10636 8 QIRRGVRVLldnatatINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQLAW-------VNQEtPAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 FTASIKDNIAYGKEDATTEEIKAAAELANASKFVDKLPQGLDTM---------------VGEHGTQL-------SGGQKQ 529
Cdd:PRK10636 77 PQPALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIdawtirsraasllhgLGFSNEQLerpvsdfSGGWRM 156
|
170 180
....*....|....*....|....*
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALD 554
Cdd:PRK10636 157 RLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
400-609 |
5.70e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 400 QIFRGFSLFISSGTTVALVGQSGSGKST----VVSLIERFYDPQAGDVLIDGINLKEFQlKWIRSKIGLVSQE----PVL 471
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIK-KHYRGDVVYNAETdvhfPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 472 FTASIKDNIAYGKEDATteEIKAAAELANASKFVD------KLPQGLDTMVGEHGTQ-LSGGQKQRIAVARAILKDPRIL 544
Cdd:TIGR00956 154 TVGETLDFAARCKTPQN--RPDGVSREEYAKHIADvymatyGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 545 LLDEATSALDAEServvqeALDRIMVNRTTVVVAHRLSTV------RNA----DMIAVIHQGKIVEKGSHTELLK 609
Cdd:TIGR00956 232 CWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
419-587 |
6.11e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.25 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 419 GQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEFQ---LKWIRSKIGLVSQEPVLftasikDNIAYgkedatTEEIKAA 495
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLEMTVF------ENLKF------WSEIYNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 496 AELANASKFVDKLPQGLDtmvgEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEaLDRIMVNRTTV 575
Cdd:PRK13541 101 AETLYAAIHYFKLHDLLD----EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNN-LIVMKANSGGI 175
|
170
....*....|....
gi 1063707070 576 VV--AHRLSTVRNA 587
Cdd:PRK13541 176 VLlsSHLESSIKSA 189
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
406-639 |
7.29e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 406 SLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGinlkefQLKWIRSKIGLVSQEPVLftasikDNIAYGK- 484
Cdd:PRK13546 44 SLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQLTGI------ENIEFKMl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 485 -EDATTEEIKA-AAELANASKFVDKLPQGLdtmvgehgTQLSGGQKQRIAVARAILKDPRILLLDEATSALDaesERVVQ 562
Cdd:PRK13546 112 cMGFKRKEIKAmTPKIIEFSELGEFIYQPV--------KKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QTFAQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 563 EALDRIM----VNRTTVVVAHRLSTVRN-ADMIAVIHQGKIVEKGSHTELLKDpegaYSQLIRLQEEKKSDENAAEEQKM 637
Cdd:PRK13546 181 KCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLNDFKKKSKAEQKEFRNKL 256
|
..
gi 1063707070 638 SS 639
Cdd:PRK13546 257 DE 258
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-598 |
8.18e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 475 SIKDNI---AYGKEDATTEEIKAAAELANASKFVD----KLPqGLDTMVGEhgtqLSGGQKQRIAVARAILKDPRILLLD 547
Cdd:PRK10762 346 SVKENMsltALRYFSRAGGSLKHADEQQAVSDFIRlfniKTP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 548 EATSALD--AESE------RVVQEALDRIMVNRTTVVVahrlstVRNADMIAVIHQGKI 598
Cdd:PRK10762 421 EPTRGVDvgAKKEiyqlinQFKAEGLSIILVSSEMPEV------LGMSDRILVMHEGRI 473
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
788-921 |
1.20e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 45.13 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 788 GCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSADAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFV 867
Cdd:cd18549 70 GARIETDMRRDLFEHLQKLSFSFFDN--NKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLI 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1063707070 868 VLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAED 921
Cdd:cd18549 148 VFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEE 201
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
403-631 |
1.62e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 403 RGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLIDGINLKEfqlKWIRSKI---------GLVSQepvLF- 472
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVcpriaympqGLGKN---LYp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 473 TASIKDNIAY--------GKE-DATTEEIKAAAELAnasKFVDKlPQGldtmvgehgtQLSGGQKQRIAVARAILKDPRI 543
Cdd:NF033858 92 TLSVFENLDFfgrlfgqdAAErRRRIDELLRATGLA---PFADR-PAG----------KLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 544 LLLDEATSALDAESERVVQEALDRIMVNRT--TVVVAhrlstvrNADM--------IAVIHQGKIVEKGSHTELL----- 608
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAERPgmSVLVA-------TAYMeeaerfdwLVAMDAGRVLATGTPAELLartga 230
|
250 260
....*....|....*....|...
gi 1063707070 609 KDPEGAYSQLirLQEEKKSDENA 631
Cdd:NF033858 231 DTLEAAFIAL--LPEEKRRGHQP 251
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
411-590 |
2.29e-04 |
|
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: 43.36 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 411 SGTTVaLVGQSGSGKSTvvslierfydpqagdvLIDGINLKEFQLKwIRSKIGLVSQEPVLFTASIKDNIAYGKEDATTE 490
Cdd:cd03240 22 SPLTL-IVGQNGAGKTT----------------IIEALKYALTGEL-PPNSKGGAHDPKLIREGEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 491 EIKAAAELA--NASKFVdklPQG-LDTMVGEHGTQLSGGQKQ------RIAVARAILKDPRILLLDEATSALDAEServV 561
Cdd:cd03240 84 KYTITRSLAilENVIFC---HQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---I 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1063707070 562 QEALDRIM------VNRTTVVVAHRLSTVRNADMI 590
Cdd:cd03240 158 EESLAEIIeerksqKNFQLIVITHDEELVDAADHI 192
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
146-271 |
2.37e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 44.36 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 146 ILRQDIAFFDiDTNTGEVVGRMSGDTVLIqdamGEKVGKAIQLL----ATFVGGFVIAFVRGWLLTLVMLSSIPLLvmag 221
Cdd:cd18549 85 LQKLSFSFFD-NNKTGQLMSRITNDLFDI----SELAHHGPEDLfisiITIIGSFIILLTINVPLTLIVFALLPLM---- 155
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063707070 222 ALLAIVIAK------TASRGQTA--YAKaatvVEQTIGSIRTVASFTGEKQAISNYNK 271
Cdd:cd18549 156 IIFTIYFNKkmkkafRRVREKIGeiNAQ----LEDSLSGIRVVKAFANEEYEIEKFDE 209
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
522-604 |
4.88e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 522 QLSGGQKQRIAVARAI---LKDPRIL-LLDEATSALDAESERVVQEALDRIMVNRTTVVVA-HRLSTVRNADmiAVIHQG 596
Cdd:cd03227 77 QLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVItHLPELAELAD--KLIHIK 154
|
....*...
gi 1063707070 597 KIVEKGSH 604
Cdd:cd03227 155 KVITGVYK 162
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
499-607 |
6.67e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 499 ANASKFVDKLpqGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERVVQEALDRIMVNRTTVVVA 578
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
90 100 110
....*....|....*....|....*....|.
gi 1063707070 579 HRL--STVRNADMIAVIHQGKIVEKGSHTEL 607
Cdd:NF000106 201 TQYmeEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
523-602 |
6.68e-04 |
|
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: 41.54 E-value: 6.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 523 LSGGQKQRIAVARAILKDPR--ILLLDEATSALDAESERVVQEALDRIMVNRTTV-VVAHRLSTVRNADMI------AVI 593
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTViLIEHNLDVLSSADWIidfgpgSGK 167
|
....*....
gi 1063707070 594 HQGKIVEKG 602
Cdd:cd03238 168 SGGKVVFSG 176
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
384-566 |
7.48e-04 |
|
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: 43.39 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 384 IELKDVYFTYParpDEQIFRGFSLFISSGTTVALVGQSGSGKSTVVSLIERFYDPQAGDVLI-DGInlkefqlkwirsKI 462
Cdd:TIGR03719 323 IEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETV------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 463 GLVSQEpvlftasiKDNIAYGKedATTEEIKAAAEL-----------ANASKFVDKlpqGLDT--MVGehgtQLSGGQKQ 529
Cdd:TIGR03719 388 AYVDQS--------RDALDPNK--TVWEEISGGLDIiklgkreipsrAYVGRFNFK---GSDQqkKVG----QLSGGERN 450
|
170 180 190
....*....|....*....|....*....|....*..
gi 1063707070 530 RIAVARAILKDPRILLLDEATSALDAESERVVQEALD 566
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
759-878 |
8.44e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 42.46 E-value: 8.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 759 TSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDepENSSGTIGARLSADAATIRGLVGD 838
Cdd:cd18606 34 QGFYIGIYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD--TTPLGRILNRFSKDTDVLDNELPD 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1063707070 839 SLAQTVQNLSSILA--GLIIAFLACWQLAFVVLAMLPLIALN 878
Cdd:cd18606 112 SLRMFLYTLSSIIGtfILIIIYLPWFAIALPPLLVLYYFIAN 153
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
765-977 |
8.77e-04 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 42.42 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 765 IFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMevgwfdepenssgtigaRLSADAATirglVGdSLAQTV 844
Cdd:cd18587 48 VLIALLFDFILKL-LRAYFIDVAGKRADVILSSRLFERVLGL-----------------RLEARPAS----VG-SFANNL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 845 QNL--------SSILAGLI-----------IAFLAcWQLAFVVLAMLPLIALNGFLYMKFMKGFSadaKKMYGEASQ--- 902
Cdd:cd18587 105 REFesvrdfftSATLTALIdlpfvllflavIALIG-GPLALVPLVAIPLVLLYGLLLQKPLRRLV---EESMRESAQkna 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 903 VANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18587 181 LLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELT 255
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
362-554 |
1.19e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 362 ERRPNIdsystnGKVLddikgdIELKD--VYftYPARPDEQIFRGFSLFISSGTTVALVGQSGSGKS-TVVSLIERFYDP 438
Cdd:NF040905 248 ERTPKI------GEVV------FEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGR 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 439 Q-AGDVLIDGinlKEFQLKWIRskiglvsqepvlftASIKDNIAYGKEDATT------EEIKAAAELAN----------- 500
Cdd:NF040905 314 NiSGTVFKDG---KEVDVSTVS--------------DAIDAGLAYVTEDRKGyglnliDDIKRNITLANlgkvsrrgvid 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 501 -------ASKFVDKL----PqGLDTMVGehgtQLSGGQKQRIAVARAILKDPRILLLDEATSALD 554
Cdd:NF040905 377 eneeikvAEEYRKKMniktP-SVFQKVG----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
758-888 |
2.30e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 41.39 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 758 DTSFWAIIFMVLGFASIIAYPAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDepENSSGTIGARLSADAATIRGLVG 837
Cdd:cd18599 56 DLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFD--TTPTGRILNRFSKDLDEVDVRLP 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1063707070 838 DSLAQTVQNLSSILAGLIIaflACWQLAFVVLAMLPLIALNGFLYMKFMKG 888
Cdd:cd18599 134 FTLENFLQNVLLVVFSLII---IAIVFPWFLIALIPLAIIFVFLSKIFRRA 181
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|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
763-977 |
2.52e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 40.96 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 763 AIIFMVLGFASIIAYpAQTFFFAIAGCKLVQRIRSMCFEKVVHMEVGWFDEpeNSSGTIGARLSAdAATIRGLVGDSLAQ 842
Cdd:cd18783 46 IGVVIALLFEGILGY-LRRYLLLVATTRIDARLALRTFDRLLSLPIDFFER--TPAGVLTKHMQQ-IERIRQFLTGQLFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 843 TVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFSADAKKMYGEASQVANDAVGSIRTVASFCAEDK 922
Cdd:cd18783 122 TLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPR 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1063707070 923 VMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDGKTT 977
Cdd:cd18783 202 QRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLT 256
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
511-602 |
2.58e-03 |
|
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: 40.70 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 511 GLD--TMVGEHGTqLSGGQKQRIAVARAI---LKDPrILLLDEATSALDAESERVVQEALDRIM-VNRTTVVVAHRLSTV 584
Cdd:cd03270 125 GLGylTLSRSAPT-LSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTI 202
|
90 100
....*....|....*....|....
gi 1063707070 585 RNADMI------AVIHQGKIVEKG 602
Cdd:cd03270 203 RAADHVidigpgAGVHGGEIVAQG 226
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|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
523-615 |
2.68e-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: 41.92 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 523 LSGGQKQRIAVARAI---LKDPrILLLDEATSALDAESERVVQEALDRIM-VNRTTVVVAHRLSTVRNADMI------AV 592
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsgLTGV-LYVLDEPSIGLHQRDNRRLINTLKRLRdLGNTLIVVEHDEDTIRAADYVidigpgAG 567
|
90 100
....*....|....*....|....*.
gi 1063707070 593 IHQGKIVEKGSHTELLKDPE---GAY 615
Cdd:TIGR00630 568 EHGGEVVASGTPEEILANPDsltGQY 593
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|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
816-977 |
2.73e-03 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 40.95 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 816 NSSGTIGARLSAdAATIRGLVGDSLAQTVQNLSSILAGLIIAFLACWQLAFVVLAMLPLIALNGFLYMKFMKGFsADAKK 895
Cdd:cd18588 96 RQVGDTVARVRE-LESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRR-LEEKF 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 896 MYGEASQ-VANDAVGSIRTVASFCAEDKVMNMYSKKCEGPMKNGIRQGIVSGIGFGFSFFVLFSSYAASFYVGARLVDDG 974
Cdd:cd18588 174 QRGAENQsFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDG 253
|
...
gi 1063707070 975 KTT 977
Cdd:cd18588 254 ELT 256
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
522-567 |
5.67e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.21 E-value: 5.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1063707070 522 QLSGGQKQRIA-------------VARAILKDPRILLLDEATSALDAESERVVQEALDR 567
Cdd:pfam13558 32 GLSGGEKQLLAylplaaalaaqygSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
402-554 |
7.89e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 402 FRGF---SLFISSGTTVaLVGQSGSGKSTVVSLIERFYDPQAGDVL--IDGINLKEFQLKWIRskIGLVsqepvlFTASI 476
Cdd:COG3593 11 FRSIkdlSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRKFdeEDFYLGDDPDLPEIE--IELT------FGSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 477 KDNIAYGKEDATTEEIKAAAELANASkfVDKLPQGLDTMVGEHGTQLSGGQKQRIAVA----RAILKDPRILLLDEATSA 552
Cdd:COG3593 82 SRLLRLLLKEEDKEELEEALEELNEE--LKEALKALNELLSEYLKELLDGLDLELELSldelEDLLKSLSLRIEDGKELP 159
|
..
gi 1063707070 553 LD 554
Cdd:COG3593 160 LD 161
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|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
109-226 |
8.94e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 39.41 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063707070 109 FVWLGIGTFAAAFLQLSGWMISGERQAARIRSLYLKTILRQDIAFFDiDTNTGEVVGRMSGDTVLIQDAMGEKVGKAIQL 188
Cdd:cd18580 45 AALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD-TTPSGRILNRFSKDIGLIDEELPLALLDFLQS 123
|
90 100 110
....*....|....*....|....*....|....*....
gi 1063707070 189 LATFVGGF-VIAFVRGWLLtlvmlssIPLLVMAGALLAI 226
Cdd:cd18580 124 LFSVLGSLiVIAIVSPYFL-------IVLPPLLVVYYLL 155
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