|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-568 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 534.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 1 MFREMLKLLtKTGKRDLIISSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKH 80
Cdd:COG1132 8 LLRRLLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 81 SAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAII 160
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 161 MAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAK 240
Cdd:COG1132 167 VLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSAL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 241 QLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYERLSRIL-YADVIPD 319
Cdd:COG1132 247 FFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLdEPPEIPD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 320 KVNGI--VPKDNDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRD 397
Cdd:COG1132 327 PPGAVplPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 398 IPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRIS 477
Cdd:COG1132 407 LTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 478 IARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNG 557
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGG 566
|
570
....*....|.
gi 446410310 558 YYTKLWKAQYE 568
Cdd:COG1132 567 LYARLYRLQFG 577
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-557 |
2.34e-122 |
|
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: 371.78 E-value: 2.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 6 LKLLTKTGKRDLIISsVFFALygLSSIAMIVIVFSI--LFQ--IFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHS 81
Cdd:COG4988 8 LKRLARGARRWLALA-VLLGL--LSGLLIIAQAWLLasLLAglIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 82 AGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIM 161
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 162 AVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFsnnksldnelmNKTKKFGET-SKAASRFKA- 239
Cdd:COG4988 165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLF-----------GRAKAEAERiAEASEDFRKr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 240 --KQLSI-F--GFLLD-IGYL-VLLIAGAILV--IKGNLDVLNFIIFAVISKEFYKPFASMEQHY---MYYVSAVdsyER 307
Cdd:COG4988 234 tmKVLRVaFlsSAVLEfFASLsIALVAVYIGFrlLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYharANGIAAA---EK 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 308 LSRILYADViPDKVNGIVP----KDNDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDV 383
Cdd:COG4988 311 IFALLDAPE-PAAPAGTAPlpaaGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 384 HKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGE 463
Cdd:COG4988 390 YSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 464 NGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNL 543
Cdd:COG4988 470 GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRI 549
|
570
....*....|....
gi 446410310 544 LEKGKHGELLAKNG 557
Cdd:COG4988 550 VEQGTHEELLAKNG 563
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-566 |
3.11e-116 |
|
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: 360.69 E-value: 3.11e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 2 FREMLKLLTKTGK--RDLIISSVFFALYGLSSiamivivfSILFQ-IFD----GTSLASLYKYFIAIGLLVVFKGICNMV 74
Cdd:COG2274 144 LRWFLRLLRRYRRllLQVLLASLLINLLALAT--------PLFTQvVIDrvlpNQDLSTLWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 75 admkkHSAGFDIVQQ-----IRERMIIKLKKFSLGFYTNERLGEINTILHkDVDNM-----SLVVGhmwsrMFGDFLIGA 144
Cdd:COG2274 216 -----RSYLLLRLGQridlrLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIrefltGSLLT-----ALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 145 VVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKT 224
Cdd:COG2274 285 IFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 225 KKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDS 304
Cdd:COG2274 365 AKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 305 YERLSRILYA--DVIPDKVNGIVPK-DNDIAFENIDFSYEKDEFKM-EKLSFSIAEKTMTALVGESGSGKTTITNLLLRF 380
Cdd:COG2274 445 LERLDDILDLppEREEGRSKLSLPRlKGDIELENVSFRYPGDSPPVlDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 381 YDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETD 460
Cdd:COG2274 525 YEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 461 IGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQK 540
Cdd:COG2274 605 VGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDK 684
|
570 580
....*....|....*....|....*.
gi 446410310 541 GNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:COG2274 685 GRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
331-563 |
9.79e-107 |
|
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: 319.95 E-value: 9.79e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:cd03251 1 VEFKNVTFRYPGDGPPvLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLW 563
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
331-566 |
1.95e-100 |
|
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: 303.69 E-value: 1.95e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY-EKDEFKMEK-LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRIS 408
Cdd:cd03249 1 IEFKNVSFRYpSRPDVPILKgLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPI 488
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 489 LILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
331-566 |
2.08e-100 |
|
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: 303.77 E-value: 2.08e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILI 490
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 491 LDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
80-564 |
3.89e-100 |
|
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: 314.40 E-value: 3.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 80 HSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAI 159
Cdd:COG4987 80 HDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALAL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 160 IMAVS-VPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFK 238
Cdd:COG4987 160 VLALGlLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLS 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 239 AKQLSIFGFLLDIGYLVLLIAGAILVIKGNLD-----VLNFIIFAVIskEfykPFASMEQHYMYYVSAVDSYERLSRIL- 312
Cdd:COG4987 240 ALAQALLQLAAGLAVVAVLWLAAPLVAAGALSgpllaLLVLAALALF--E---ALAPLPAAAQHLGRVRAAARRLNELLd 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 313 -YADVIPDKVNGIVPKDNDIAFENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITL 390
Cdd:COG4987 315 aPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPvLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 391 GGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSG 470
Cdd:COG4987 395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSG 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 471 GQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHG 550
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHE 554
|
490
....*....|....
gi 446410310 551 ELLAKNGYYTKLWK 564
Cdd:COG4987 555 ELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
331-568 |
6.45e-98 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 309.83 E-value: 6.45e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILI 490
Cdd:COG5265 438 PQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILI 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 491 LDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQYE 568
Cdd:COG5265 518 FDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQE 595
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-567 |
1.57e-95 |
|
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: 302.79 E-value: 1.57e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMII 96
Cdd:TIGR02203 16 LVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 97 KLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVP-IALIFLYLT 175
Cdd:TIGR02203 96 KLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPvLSILMRRVS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 176 IK---QSEKIENQNNsallDMVSLFVEYVRGIPVLKSFSNNKSldnelmnKTKKFGETSKAASRFKAKQLS-------IF 245
Cdd:TIGR02203 176 KRlrrISKEIQNSMG----QVTTVAEETLQGYRVVKLFGGQAY-------ETRRFDAVSNRNRRLAMKMTSagsisspIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 246 GFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYERLSRILyaDVIPDKVNGIV 325
Cdd:TIGR02203 245 QLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL--DSPPEKDTGTR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 326 PKDN---DIAFENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYD 401
Cdd:TIGR02203 323 AIERargDVEFRNVTFRYPGRDRPaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 402 ELLDRISIVMQNVQLFDNTIEENIRVGK-KGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIAR 480
Cdd:TIGR02203 403 SLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIAR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 481 AFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYT 560
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYA 562
|
....*..
gi 446410310 561 KLWKAQY 567
Cdd:TIGR02203 563 QLHNMQF 569
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
330-557 |
1.46e-94 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 288.35 E-value: 1.46e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNG 557
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
46-567 |
3.47e-92 |
|
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: 294.30 E-value: 3.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 46 FDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNM 125
Cdd:TIGR02204 49 FSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 126 SLVVGHMWSRMFGDFL--IGAVVFVGLASidFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRG 203
Cdd:TIGR02204 129 QSVIGSSLSMALRNALmcIGGLIMMFITS--PKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 204 IPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNL---DVLNFIIFAVI 280
Cdd:TIGR02204 207 IRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMsagTLGQFVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 281 SKefyKPFASMEQHYMYYVSAVDSYERLSRILYA--DVIPDKVNGIVPKD--NDIAFENIDFSY--EKDEFKMEKLSFSI 354
Cdd:TIGR02204 287 VA---GSIGTLSEVWGELQRAAGAAERLIELLQAepDIKAPAHPKTLPVPlrGEIEFEQVNFAYpaRPDQPALDGLNLTV 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 355 AEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATK 434
Cdd:TIGR02204 364 RPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATD 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 435 EEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELA 514
Cdd:TIGR02204 444 EEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLM 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446410310 515 KNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQY 567
Cdd:TIGR02204 524 KGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQF 576
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
330-567 |
6.18e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 285.76 E-value: 6.18e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYE-KDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRIS 408
Cdd:PRK11176 341 DIEFRNVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDNTIEENIRVGKKGA-TKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAP 487
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQY 567
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQF 580
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
251-566 |
7.24e-86 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 278.00 E-value: 7.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 251 IGYLVLLIAGAILVIKGNL---DVLNFIIFA--VISKefykpfasMEQHYMYYVSAVDSYERLSRIL-YADVIP---DKV 321
Cdd:PRK13657 252 ITMLAILVLGAALVQKGQLrvgEVVAFVGFAtlLIGR--------LDQVVAFINQVFMAAPKLEEFFeVEDAVPdvrDPP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 322 NGIVPKD--NDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIP 399
Cdd:PRK13657 324 GAIDLGRvkGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 400 YDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIA 479
Cdd:PRK13657 404 RASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYY 559
Cdd:PRK13657 484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRF 563
|
....*..
gi 446410310 560 TKLWKAQ 566
Cdd:PRK13657 564 AALLRAQ 570
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-537 |
6.21e-85 |
|
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: 273.78 E-value: 6.21e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 14 KRDLIISSVFFALYGLSSIAMI-VIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRE 92
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAwLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 93 RMIIKLKKFSLGFYTNERLGEINTILHKDVDNM----SLVVGHMWSRMFGDFLIGAVVFVglasIDFKLAIIMAVSVPIA 168
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALdgyfARYLPQLVLAVIVPLAILAAVFP----QDWISGLILLLTAPLI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 169 LIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFsnnksldnelmNKTKKFGETSKAAS-RFKAKQLSIfgf 247
Cdd:TIGR02857 158 PIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLF-----------GRAKAQAAAIRRSSeEYRERTMRV--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 248 lLDIGYL---VLLIAGAILV-----------IKGNLDvLNFIIFAVI-SKEFYKPFASMEQHYMYYVSAVDSYERLSRIL 312
Cdd:TIGR02857 224 -LRIAFLssaVLELFATLSValvavyigfrlLAGDLD-LATGLFVLLlAPEFYLPLRQLGAQYHARADGVAAAEALFAVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 313 YADVIPDKVNGIVPKDND--IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITL 390
Cdd:TIGR02857 302 DAAPRPLAGKAPVTAAPAssLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 391 GGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSG 470
Cdd:TIGR02857 382 NGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSG 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 471 GQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILV 537
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVV 528
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-562 |
1.86e-73 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 248.10 E-value: 1.86e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 1 MFReMLKLLtKTGKRDLIISSVFFALYGLSSIAM---IVIVFSILFQIFDGTSLAS----LYKYFIAIGLLVVFKGICNM 73
Cdd:TIGR00958 149 LFR-LLGLS-GRDWPWLISAFVFLTLSSLGEMFIpfyTGRVIDTLGGDKGPPALASaiffMCLLSIASSVSAGLRGGSFN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 74 VADMKkhsagfdIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGH-----MWSrmfGDFLIGAVVFv 148
Cdd:TIGR00958 227 YTMAR-------INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLnvnvlLRN---LVMLLGLLGF- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 149 gLASIDFKLAIIMAVSVPIaLIFL---YLTIKQSEKIENQNNSALLDMVSLfvEYVRGIPVLKSFSN-NKSLD--NELMN 222
Cdd:TIGR00958 296 -MLWLSPRLTMVTLINLPL-VFLAekvFGKRYQLLSEELQEAVAKANQVAE--EALSGMRTVRSFAAeEGEASrfKEALE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 223 KTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLliaGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAV 302
Cdd:TIGR00958 372 ETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYY---GGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAV 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 303 DSYERLSRilYADVIPD-KVNGIVPKDND---IAFENIDFSY--EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNL 376
Cdd:TIGR00958 449 GASEKVFE--YLDRKPNiPLTGTLAPLNLeglIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAAL 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 377 LLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKG 456
Cdd:TIGR00958 527 LQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNG 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 457 YETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITelAKNRTVLVVAHHLKTIQKADQIL 536
Cdd:TIGR00958 607 YDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQIL 684
|
570 580
....*....|....*....|....*.
gi 446410310 537 VFQKGNLLEKGKHGELLAKNGYYTKL 562
Cdd:TIGR00958 685 VLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
331-566 |
2.08e-73 |
|
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: 233.92 E-value: 2.08e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDE-FKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:cd03252 1 ITFEHVRFRYKPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
331-541 |
4.53e-71 |
|
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: 225.34 E-value: 4.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY-EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDNTIEENIrvgkkgatkeeiikaakkarihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKG 541
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
195-566 |
2.16e-70 |
|
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: 239.64 E-value: 2.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 195 SLFVEYVRGIPVLKSfsnnKSLDNELMNKTKKFGETSKAASrFKAKQLS-----IFGFLLDIGYLVLLIAGAILVIKGNL 269
Cdd:TIGR01846 318 SFLVESVTGIETIKA----TATEPQFQNRWDRQLAAYVAAS-FRVTNLGniagqAIELIQKLTFAILLWFGAHLVIGGAL 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 270 DVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYERLSRILYADVIPDKVNGI-VPK-DNDIAFENIDFSYEKDEFK- 346
Cdd:TIGR01846 393 SPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAaLPElRGAITFENIRFRYAPDSPEv 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIR 426
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:TIGR01846 553 LCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALI 632
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 507 QDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:TIGR01846 633 MRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
318-543 |
6.17e-67 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 216.95 E-value: 6.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 318 PDKVNGIVpkdndiAFENIDFSYEK--DEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI 395
Cdd:cd03248 5 PDHLKGIV------KFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 396 RDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQR 475
Cdd:cd03248 79 SQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 476 ISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNL 543
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
251-565 |
5.16e-65 |
|
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: 222.46 E-value: 5.16e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 251 IGYLVLLIAGAILVIKGNL---DVLNFIIFAVISkefykpFASMEQHYMYYVSAVDSYERLSRIL-YADVIPDKVNgivP 326
Cdd:TIGR01192 252 ISMMCILVIGTVLVIKGELsvgEVIAFIGFANLL------IGRLDQMSGFITQIFEARAKLEDFFdLEDSVFQREE---P 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 327 KD--------NDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDI 398
Cdd:TIGR01192 323 ADapelpnvkGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTV 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 399 PYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISI 478
Cdd:TIGR01192 403 TRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAI 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGY 558
Cdd:TIGR01192 483 ARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGR 562
|
....*..
gi 446410310 559 YTKLWKA 565
Cdd:TIGR01192 563 FYKLLRR 569
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-562 |
1.40e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 210.86 E-value: 1.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 6 LKLLTKTGKRDLIISSVFFALYGLSSIAMIVIVFSILFQ-IFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGF 84
Cdd:PRK11174 13 LKQQSKPAKRWLNLSILLGFLSGLLLIAQAWLLATILQAlIIENIPREALLPPFILLILLFVLRALLAWLRERVGFKAGQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 85 DIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDN-----------MSLVVghmwsrmFGDFLIGAVVFvglaSI 153
Cdd:PRK11174 93 HIRQQIRQQVLDKLQQLGPAWIQGKPAGSWATLVLEQVEDmhdfyarylpqMALAV-------LVPLLILIAVF----PI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 154 DFKLAIIMAVSVPIALIFLYLT-IKQSEkiENQNN-SALLDMVSLFVEYVRGIPVLKSFsnnksldnelmNKTKKFGETS 231
Cdd:PRK11174 162 NWAAGLILLGTAPLIPLFMALVgMGAAD--ANRRNfLALARLSGHFLDRLRGLETLRLF-----------NRGEAETESI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 232 KAASR----------------------FKAkqLSI------FGFL----LDIGYL---VLLIAGailvikgnLDVLnfiI 276
Cdd:PRK11174 229 RSASEdfrqrtmevlrmaflssavlefFAS--ISIalvavyFGFSylgeLNFGHYgtgVTLFAG--------FFVL---I 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 277 FAvisKEFYKPFASMEQHYMYYVSAVDSYERLSRILYADVIPDKVNGIVPKDND-IAFENIDFSYEKDEFK--MEKLSFS 353
Cdd:PRK11174 296 LA---PEFYQPLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDpVTIEAEDLEILSPDGKtlAGPLNFT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 354 IAEKTMTALVGESGSGKTTITNLLLRF--YdvhKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKG 431
Cdd:PRK11174 373 LPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 432 ATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAIT 511
Cdd:PRK11174 450 ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 446410310 512 ELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKL 562
Cdd:PRK11174 530 AASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
59-562 |
6.22e-60 |
|
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: 211.52 E-value: 6.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 59 IAIGLLV--VFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTilhkDVDNMSLVVGHMWSRM 136
Cdd:TIGR01193 198 ISIGLIIayIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVS----RFTDASSIIDALASTI 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 137 FGDFL-IGAVVFVG--LASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNN 213
Cdd:TIGR01193 274 LSLFLdMWILVIVGlfLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 214 KSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQ 293
Cdd:TIGR01193 354 AERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIIN 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 294 HYMYYVSAVDSYERLSRILYADVIPDKVNGIVPKDN---DIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGK 370
Cdd:TIGR01193 434 LQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNlngDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 371 TTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVG-KKGATKEEIIKAAKKARIHDF 449
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 450 IMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELaKNRTVLVVAHHLKTI 529
Cdd:TIGR01193 594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVA 672
|
490 500 510
....*....|....*....|....*....|...
gi 446410310 530 QKADQILVFQKGNLLEKGKHGELLAKNGYYTKL 562
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
80-563 |
6.32e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.53 E-value: 6.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 80 HSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSlvvgHMWSR----MFGDFLIGAVVFVGLASIDF 155
Cdd:PRK11160 85 HDATFRVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLD----HLYLRlispLVAALVVILVLTIGLSFFDL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 156 KLA-----IIMAVSVPIALIFLYLTIKQSEKIeNQNNSALLdmvSLFVEYVRGIPVLKSFSNNKSLDNElMNKTkkfgET 230
Cdd:PRK11160 161 TLAltlggILLLLLLLLPLLFYRLGKKPGQDL-THLRAQYR---VQLTEWLQGQAELTLFGAEDRYRQQ-LEQT----EQ 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 231 SKAASRFKAKQLSIFG---FLLDIGYLVLLI----AGAI--LVIKGNLDVLnFIIFAVISKEFYKPFASMEQHymyyVSA 301
Cdd:PRK11160 232 QWLAAQRRQANLTGLSqalMILANGLTVVLMlwlaAGGVggNAQPGALIAL-FVFAALAAFEALMPVAGAFQH----LGQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 302 V-DSYERLSRILYA--DVIPDKVNGIVPKDNDIAFENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLL 377
Cdd:PRK11160 307 ViASARRINEITEQkpEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 378 LRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSlPKGY 457
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGL 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 458 ETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILV 537
Cdd:PRK11160 466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
|
490 500
....*....|....*....|....*.
gi 446410310 538 FQKGNLLEKGKHGELLAKNGYYTKLW 563
Cdd:PRK11160 546 MDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-526 |
7.43e-60 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 207.60 E-value: 7.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 3 REMLKLLtKTGKRDLIISSVFFALYGLSSIAMIVIVFSILfqifdgtSLASLYKYFIAIGLLVV---FKGICNMVAD--- 76
Cdd:TIGR02868 2 LRILPLL-KPRRRRLALAVLLGALALGSAVALLGVSAWLI-------SRAAEMPPVLYLSVAAVavrAFGIGRAVFRyle 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 77 -MKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNmslvVGHMWSR----MFGDFLIGAVVFVGLA 151
Cdd:TIGR02868 74 rLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDA----LQDLYVRvivpAGVALVVGAAAVAAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 152 SIDFKLAIIMAVSVPIALIFL----YLTIKQSEKIENQNNSALLDMVslfVEYVRGIPVLKSFSNNKSLDNELMNKTKKF 227
Cdd:TIGR02868 150 VLSVPAALILAAGLLLAGFVAplvsLRAARAAEQALARLRGELAAQL---TDALDGAAELVASGALPAALAQVEEADREL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 228 GETSKAASRFKAkqLSIFGFLLDIGYLVL--LIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSY 305
Cdd:TIGR02868 227 TRAERRAAAATA--LGAALTLLAAGLAVLgaLWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 306 ERLSRILYADVIPDKVNG-----IVPKDNDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRF 380
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSApaagaVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 381 YDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETD 460
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 461 IGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHL 526
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
330-547 |
3.28e-58 |
|
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: 193.48 E-value: 3.28e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYEKDE-FKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRIS 408
Cdd:cd03244 2 DIEFKNVSLRYRPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDNTIEENIRVGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPI 488
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 489 LILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKG 547
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
338-566 |
7.93e-57 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 200.32 E-value: 7.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 338 FSY-EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQL 416
Cdd:PRK10789 321 FTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 FDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 497 NVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
330-547 |
2.51e-56 |
|
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: 188.57 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRIS 408
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPI 488
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 489 LILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKG 547
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
298-555 |
1.06e-54 |
|
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: 194.20 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 298 YVSAVDSYERLSRILyaDVIPDKVNGI---VPKdNDIAFENIDFSY---EKDEFKMekLSFSIAEKTMTALVGESGSGKT 371
Cdd:COG4618 298 FVSARQAYRRLNELL--AAVPAEPERMplpRPK-GRLSVENLTVVPpgsKRPILRG--VSFSLEPGEVLGVIGPSGSGKS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 372 TITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENI-RVGKkgATKEEIIKAAKKARIHDFI 450
Cdd:COG4618 373 TLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFGD--ADPEKVVAAAKLAGVHEMI 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 451 MSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTI 529
Cdd:COG4618 451 LRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLL 530
|
250 260
....*....|....*....|....*.
gi 446410310 530 QKADQILVFQKGNLLEKGKHGELLAK 555
Cdd:COG4618 531 AAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
247-562 |
2.56e-54 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 195.93 E-value: 2.56e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 247 FLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMeqhyMYYVSAVDSYE----RLSRILYADVIPDKVN 322
Cdd:TIGR03796 385 LLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNL----VGFGGTLQELEgdlnRLDDVLRNPVDPLLEE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 323 GIVPKDND---------IAFENIDFSYEK-DEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGG 392
Cdd:TIGR03796 461 PEGSAATSepprrlsgyVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDG 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 393 TDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQ 472
Cdd:TIGR03796 541 IPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQ 620
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 473 RQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITElaKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGEL 552
Cdd:TIGR03796 621 RQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEEL 698
|
330
....*....|
gi 446410310 553 LAKNGYYTKL 562
Cdd:TIGR03796 699 WAVGGAYARL 708
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
141-566 |
5.94e-51 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 184.54 E-value: 5.94e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 141 LIGAVVfVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFsnnksldnel 220
Cdd:PRK10790 152 LIGAML-VAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF---------- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 221 mNKTKKFGETSKAASR--FKA--KQLSIFGFLLDiGYLVLLIAgaiLVIKGNLDVLNF---------IIFAVIS--KEFY 285
Cdd:PRK10790 221 -RQQARFGERMGEASRshYMArmQTLRLDGFLLR-PLLSLFSA---LILCGLLMLFGFsasgtievgVLYAFISylGRLN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 286 KPF------ASMEQHymyyvsAVDSYERLSRIL------YADVIPDKVNGivpkdnDIAFENIDFSYEKDEFKMEKLSFS 353
Cdd:PRK10790 296 EPLielttqQSMLQQ------AVVAGERVFELMdgprqqYGNDDRPLQSG------RIDIDNVSFAYRDDNLVLQNINLS 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 354 IAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKgAT 433
Cdd:PRK10790 364 VPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-IS 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 434 KEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL 513
Cdd:PRK10790 443 EEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV 522
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 446410310 514 AKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:PRK10790 523 REHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
256-555 |
6.27e-51 |
|
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: 183.32 E-value: 6.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 256 LLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYERLSRILYADVIPDKVNGIVPKDNDIAFEN 335
Cdd:TIGR01842 242 VLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPEPEGHLSVEN 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 336 IDFSY-EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNV 414
Cdd:TIGR01842 322 VTIVPpGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDV 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 415 QLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEM 494
Cdd:TIGR01842 402 ELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 495 TSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAK 555
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
154-566 |
1.13e-48 |
|
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: 179.77 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 154 DFKLAII-MAVSVPIALIFLYLTI----KQSEKIENQNNsalldMVSLFVEYVRGIPVLK-SFSNNKSLdnelMNKTKKF 227
Cdd:TIGR03797 274 SWKLALVaVALALVAIAVTLVLGLlqvrKERRLLELSGK-----ISGLTVQLINGISKLRvAGAENRAF----ARWAKLF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 228 GETSK--AASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKG-NLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDS 304
Cdd:TIGR03797 345 SRQRKleLSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGaGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 305 YERLSRILYAD-------VIPDKVNGivpkdnDIAFENIDFSYEKD-EFKMEKLSFSIAEKTMTALVGESGSGKTTITNL 376
Cdd:TIGR03797 425 WERAKPILEALpevdeakTDPGKLSG------AIEVDRVTFRYRPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 377 LLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIrVGKKGATKEEIIKAAKKARIHDFIMSLPKG 456
Cdd:TIGR03797 499 LLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMG 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 457 YETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDpvNESliQDAITE-LAK-NRTVLVVAHHLKTIQKADQ 534
Cdd:TIGR03797 578 MHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD--NRT--QAIVSEsLERlKVTRIVIAHRLSTIRNADR 653
|
410 420 430
....*....|....*....|....*....|..
gi 446410310 535 ILVFQKGNLLEKGKHGELLAKNGYYTKLWKAQ 566
Cdd:TIGR03797 654 IYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
350-564 |
6.05e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 168.28 E-value: 6.05e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDV---------------------------------------------- 383
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 384 --------HKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPK 455
Cdd:PTZ00265 1267 gedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPN 1346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 456 GYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQKAD 533
Cdd:PTZ00265 1347 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSD 1426
|
250 260 270
....*....|....*....|....*....|....*..
gi 446410310 534 QILVF----QKGNLLE-KGKHGELL-AKNGYYTKLWK 564
Cdd:PTZ00265 1427 KIVVFnnpdRTGSFVQaHGTHEELLsVQDGVYKKYVK 1463
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
331-543 |
5.56e-41 |
|
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: 145.82 E-value: 5.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY-EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDNTIEENIrvgkkgatkeeiikaakkarihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQKADQILVFQKGNL 543
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
331-547 |
1.37e-39 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 142.45 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY-EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPyDELLDRISI 409
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDNTIEENIrvgkkgatkeeiikaakkarihdfimslpkgyetdigenGGILSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKG 547
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
326-547 |
3.45e-39 |
|
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: 142.17 E-value: 3.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 326 PKDNDIAFENIDFSYEKDEFKMEK-LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELL 404
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKnVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 405 DRISIVMQNVQLFDNTIEENIRVGKKgATKEEIIKAAKkarihdfimslpkgyetdIGENGGILSGGQRQRISIARAFLK 484
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLDPFDE-YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 485 DAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKG 547
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
331-548 |
4.41e-39 |
|
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: 142.70 E-value: 4.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHK-----GKITLGGTDIRDIPYD--EL 403
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDvlEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 404 LDRISIVMQNVQLFDNTIEENIRVG-------KKGATKEEIIKAAKKARIHDFIMSLPKGYEtdigenggiLSGGQRQRI 476
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGK 548
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGP 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
103-557 |
8.80e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 149.74 E-value: 8.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 103 LGFYTNERlGEINTILHKDV--------DNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAvsvpiALIFLYL 174
Cdd:PLN03232 999 LFFHTNPT-GRVINRFSKDIgdidrnvaNLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYA-----AYLYYQS 1072
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 175 TIKQSEKIENQNNSALLdmvSLFVEYVRGIPVLKSFS--------NNKSLDNELmnktkKFGETSKAASRFKAKQLSIFG 246
Cdd:PLN03232 1073 TSREVRRLDSVTRSPIY---AQFGEALNGLSSIRAYKaydrmakiNGKSMDNNI-----RFTLANTSSNRWLTIRLETLG 1144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 247 flldiGYLVLLIAGAILVIKGNLDvlNFIIFAVISK---EFYKPFASMEQHYMYYVS----AVDSYERLSRilYADvIPD 319
Cdd:PLN03232 1145 -----GVMIWLTATFAVLRNGNAE--NQAGFASTMGlllSYTLNITTLLSGVLRQASkaenSLNSVERVGN--YID-LPS 1214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 320 KVNGIV---------PKDNDIAFENIDFSYEKD-EFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKIT 389
Cdd:PLN03232 1215 EATAIIennrpvsgwPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIM 1294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 390 LGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIRVGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILS 469
Cdd:PLN03232 1295 IDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSE-HNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFS 1373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 470 GGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKH 549
Cdd:PLN03232 1374 VGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSP 1453
|
....*...
gi 446410310 550 GELLAKNG 557
Cdd:PLN03232 1454 QELLSRDT 1461
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
62-564 |
1.38e-37 |
|
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: 148.94 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 62 GLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFL 141
Cdd:TIGR00957 1012 GALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLF 1091
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 142 --IGAVVFVGLASIDFKLAIImavsvPIALIFLYL------TIKQSEKIENQNNSALLdmvSLFVEYVRGIPVLKSFsnN 213
Cdd:TIGR00957 1092 nvIGALIVILLATPIAAVIIP-----PLGLLYFFVqrfyvaSSRQLKRLESVSRSPVY---SHFNETLLGVSVIRAF--E 1161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 214 KSLDNELMNKTKkFGETSKAasrfkakqlsifgflldigYLVLLIAGAILVIK----GNLDVLNFIIFAVISKEFYKP-F 288
Cdd:TIGR00957 1162 EQERFIHQSDLK-VDENQKA-------------------YYPSIVANRWLAVRlecvGNCIVLFAALFAVISRHSLSAgL 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 289 ASMEQHYMYYVSAVDSYE-RLSRILYADVI---------------PDKVNGIVPKDN-----DIAFENIDFSYEKD-EFK 346
Cdd:TIGR00957 1222 VGLSVSYSLQVTFYLNWLvRMSSEMETNIVaverlkeysetekeaPWQIQETAPPSGwpprgRVEFRNYCLRYREDlDLV 1301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIR 426
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD 1381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:TIGR00957 1382 PFSQ-YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 507 QDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKLWK 564
Cdd:TIGR00957 1461 QSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
331-541 |
2.57e-36 |
|
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: 134.13 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDE----FKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGtdirdipydelldR 406
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 ISIVMQNVQLFDNTIEENIRVGKKGATK--EEIIKAAkkARIHDFIMsLPKGYETDIGENGGILSGGQRQRISIARAFLK 484
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKAC--ALEPDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 485 DAPILILDEMTSNVDP-VNESLIQDAIT-ELAKNRTVLVVAHHLKTIQKADQILVFQKG 541
Cdd:cd03250 145 DADIYLLDDPLSAVDAhVGRHIFENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
331-543 |
4.31e-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: 134.15 E-value: 4.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKL---SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDEL---- 403
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALkgvSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 404 LDRISIVMQNVQLFDN-TIEENIRVGKKGATKEeiiKAAKKARIHDFI--MSLPKGYETDIGEnggiLSGGQRQRISIAR 480
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVP---KKERRERAEELLerVGLGDRLNHYPSE----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 481 AFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQKADQILVFQKGNL 543
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-496 |
6.42e-36 |
|
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: 131.23 E-value: 6.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDN-TIEENIRVg 428
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENLRL- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 429 kkGATKEEIIKAAKKARIHDFI--MSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:pfam00005 83 --GLLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
295-556 |
1.39e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 142.86 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 295 YMYYVSAVDS-YERLSRilyADVIPDKVNGIVPKD-NDIAFENIDFSYE--KDEFKMEKLSFSIAEKTMTALVGESGSGK 370
Cdd:PTZ00265 348 YMKSLEATNSlYEIINR---KPLVENNDDGKKLKDiKKIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 371 TTITNLLLRFYDVHKGKITLGGT-DIRDIPYDELLDRISIVMQNVQLFDNTIEENIR----------------------- 426
Cdd:PTZ00265 425 STILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlealsnyynedgnds 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 --------------------------------VGKKGATKE--EIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQ 472
Cdd:PTZ00265 505 qenknkrnscrakcagdlndmsnttdsnelieMRKNYQTIKdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQ 584
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 473 RQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELA--KNRTVLVVAHHLKTIQKADQILVF---QKGNLLEKG 547
Cdd:PTZ00265 585 KQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrERGSTVDVD 664
|
....*....
gi 446410310 548 KHGELLAKN 556
Cdd:PTZ00265 665 IIGEDPTKD 673
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
323-565 |
1.85e-35 |
|
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: 133.88 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 323 GIVPKDNDIAFENIDFSYE---KDEFKMEKLSFSIAEKTmtALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIP 399
Cdd:cd03288 12 GLVGLGGEIKIHDLCVRYEnnlKPVLKHVKAYIKPGQKV--GICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 400 YDELLDRISIVMQNVQLFDNTIEENIRVGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIA 479
Cdd:cd03288 90 LHTLRSRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLA-KNGY 558
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGV 248
|
....*..
gi 446410310 559 YTKLWKA 565
Cdd:cd03288 249 FASLVRT 255
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
331-547 |
5.20e-35 |
|
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: 131.47 E-value: 5.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKL---SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR- 406
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 --ISIVMQNVQLFDN---TIEENI----RVGKKGATKEEIIKAAKKARIH-----DFIMSLPkgYEtdigenggiLSGGQ 472
Cdd:cd03257 82 keIQMVFQDPMSSLNprmTIGEQIaeplRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYP--HE---------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 473 RQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
331-554 |
5.30e-35 |
|
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: 138.11 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYE---KDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD- 405
Cdd:COG1123 261 LEVRNLSKRYPvrgKGGVRaVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 --RISIVMQN--VQLF-DNTIEENIRVG---KKGATKEEIikaakKARIHDFI--MSLPKGY-ETDIGEnggiLSGGQRQ 474
Cdd:COG1123 341 rrRVQMVFQDpySSLNpRMTVGDIIAEPlrlHGLLSRAER-----RERVAELLerVGLPPDLaDRYPHE----LSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 475 RISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGE 551
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491
|
...
gi 446410310 552 LLA 554
Cdd:COG1123 492 VFA 494
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
350-543 |
6.93e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 6.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENI---- 425
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLpfpf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RVGKKGATKEEIIKAAKKARIHDFIMslpkgyETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESL 505
Cdd:COG4619 99 QLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446410310 506 IQDAITELA--KNRTVLVVAHHLKTIQK-ADQILVFQKGNL 543
Cdd:COG4619 169 VEELLREYLaeEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
350-555 |
1.16e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 130.95 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPyDELLDRISIVMQNVQLFDN-TIEENIR-V 427
Cdd:COG1131 19 VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVPQEPALYPDlTVRENLRfF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GK-KGATKEEIikaakKARIHDFI--MSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNES 504
Cdd:COG1131 98 ARlYGLPRKEA-----RERIDELLelFGLTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446410310 505 LIQDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAK 555
Cdd:COG1131 169 ELWELLRELAAeGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
331-556 |
6.93e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 128.33 E-value: 6.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEkdEFKMEkLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDElldR-ISI 409
Cdd:COG3840 2 LRLDDLTYRYG--DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE---RpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDN-TIEENIRVG-----KKGAT-KEEIIKAAKKARIHDFIMSLPkgyetdigengGILSGGQRQRISIARAF 482
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlrpglKLTAEqRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 483 LKDAPILILDEMTSNVDPV--NESLiqDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAKN 556
Cdd:COG3840 145 VRKRPILLLDEPFSALDPAlrQEML--DLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
331-555 |
8.19e-34 |
|
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: 128.22 E-value: 8.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQN--VQLFDNTIEENIRVGKK--GATKEEIIKAAKKA------------RIHDfimslpkgyetdigenggiLSGGQRQ 474
Cdd:COG1122 81 FQNpdDQLFAPTVEEDVAFGPEnlGLPREEIRERVEEAlelvglehladrPPHE-------------------LSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 475 RISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGEL 552
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREV 221
|
...
gi 446410310 553 LAK 555
Cdd:COG1122 222 FSD 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
333-541 |
8.32e-34 |
|
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: 125.82 E-value: 8.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 333 FENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQ 412
Cdd:cd00267 2 IENLSFRYGGRTA-LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 413 nvqlfdntieenirvgkkgatkeeiikaakkarihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILILD 492
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446410310 493 EMTSNVDPVNESLIQDAITELA-KNRTVLVVAHHLKTIQKA-DQILVFQKG 541
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
331-545 |
1.20e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 127.85 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKL---SFSIAEKTMTALVGESGSGKTTITNLL--LRFYDvhKGKITLGGTDIRDIPYDEL-- 403
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALrgvSLSIEAGEFVAIVGPSGSGKSTLLNILggLDRPT--SGEVLIDGQDISSLSERELar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 404 --LDRISIVMQNVQLFDN-TIEENIRVG------KKGATKEEIIKAAKKARIHDFIMSLPkgyetdiGEnggiLSGGQRQ 474
Cdd:COG1136 83 lrRRHIGFVFQFFNLLPElTALENVALPlllagvSRKERRERARELLERVGLGDRLDHRP-------SQ----LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 475 RISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQKADQILVFQKGNLLE 545
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
331-554 |
3.68e-33 |
|
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: 127.03 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQLFDN-TIEENIRVGKK--GATKEEIIKAAKKarihdfIMSL----PKGYetdIGENGGILSGGQRQRISIARAFL 483
Cdd:cd03295 81 IQQIGLFPHmTVEENIALVPKllKWPKEKIRERADE------LLALvgldPAEF---ADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 484 KDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHL-KTIQKADQILVFQKGNLLEKGKHGELLA 554
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
331-554 |
6.95e-33 |
|
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: 131.95 E-value: 6.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVH---KGKITLGGTDIRDIPYDELLDR 406
Cdd:COG1123 5 LEVRDLSVRYPGGDVPaVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 ISIVMQN--VQLFDNTIEENIRVG------KKGATKEEIIKAAKKARIHDFIMSLPkgyetdigengGILSGGQRQRISI 478
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTI-QKADQILVFQKGNLLEKGKHGELLA 554
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
331-557 |
6.95e-33 |
|
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: 126.13 E-value: 6.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYdELLDRISIV 410
Cdd:COG4555 2 IEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQLFDN-TIEENIRVGkkgATKEEIIKAAKKARIHDFI--MSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAP 487
Cdd:COG4555 80 PDERGLYDRlTVRENIRYF---AELYGLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAKNG 557
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
333-541 |
7.92e-33 |
|
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: 124.89 E-value: 7.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 333 FENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVM 411
Cdd:cd03225 2 LKNLSFSYPDGARPaLDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 QN--VQLFDNTIEENIRVGKK--GATKEEIIKAAKKArIHDFIMSLPKgyETDIGEnggiLSGGQRQRISIARAFLKDAP 487
Cdd:cd03225 82 QNpdDQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEA-LELVGLEGLR--DRSPFT----LSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTI-QKADQILVFQKG 541
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
331-541 |
3.61e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.05 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYE-----KDefkmekLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRdipydELLD 405
Cdd:COG1121 7 IELENLTVSYGgrpvlED------VSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 RISIVMQNVQlFDN----TIEENI---RVGKKGATKeeIIKAAKKARIHDFI----MSlpkGYETD-IGEnggiLSGGQR 473
Cdd:COG1121 76 RIGYVPQRAE-VDWdfpiTVRDVVlmgRYGRRGLFR--RPSRADREAVDEALervgLE---DLADRpIGE----LSGGQQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 474 QRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:COG1121 146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLNRG 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
351-554 |
5.57e-32 |
|
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: 123.76 E-value: 5.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQN-------VQLFDNTIEE 423
Cdd:COG1124 25 SLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyaslhpRHTVDRILAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 424 NIRVGKKGATKEEIIKAAKKA---------RIHDfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILILDEM 494
Cdd:COG1124 105 PLRIHGLPDREERIAELLEQVglppsfldrYPHQ-------------------LSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 495 TSNVDPVNESLIQDAITEL--AKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:COG1124 166 TSALDVSVQAEILNLLKDLreERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
331-553 |
7.20e-32 |
|
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: 123.62 E-value: 7.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:COG1120 2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQL-FDNTIEENIRVGKK---------GATKEEIIKAA-KKARIHDFImslpkgyETDIGEnggiLSGGQRQRISIA 479
Cdd:COG1120 81 PQEPPApFGLTVRELVALGRYphlglfgrpSAEDREAVEEAlERTGLEHLA-------DRPVDE----LSGGERQRVLIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLK-TIQKADQILVFQKGNLLEKGKHGELL 553
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
334-536 |
1.13e-31 |
|
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: 121.60 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGtdiRDIPYDELLDRISIVMQN 413
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 414 V--QLFDNTIEENIRVGKK--GATKEEIIKAAKKARIHDFIMSLPKgyetdigenggILSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKelDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHLKTIQK-ADQIL 536
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVL 197
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-547 |
8.56e-31 |
|
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: 118.31 E-value: 8.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQN 413
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 414 VQLFDntieenirvgkkgatkeeiikaakkarIHDFIMslpKGYETdigenggiLSGGQRQRISIARAFLKDAPILILDE 493
Cdd:cd03214 82 LELLG---------------------------LAHLAD---RPFNE--------LSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 494 MTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLK-TIQKADQILVFQKGNLLEKG 547
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
326-557 |
1.22e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 127.93 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 326 PKDNDIAFENIDFSYEKD-EFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELL 404
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 405 DRISIVMQNVQLFDNTIEENIRVGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLK 484
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNLDPFNE-HNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 485 DAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNG 557
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
331-551 |
3.63e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.85 E-value: 3.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD---RI 407
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFDN-TIEENI----RV-GKKGAT-KEEIIKAAKKARIHDFIMSLPkgyetdigengGILSGGQRQRISIAR 480
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENValplRVtGKSRKEiRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 481 AFLKDAPILILDEMTSNVDPVNESLIQDAITELakNR---TVLVVAHHLKTIQKADQ-ILVFQKGNLLEKGKHGE 551
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEI--NRrgtTVLIATHDLELVDRMPKrVLELEDGRLVRDEARGV 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
331-553 |
8.17e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDE-FKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:PRK13632 8 IKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNV--QLFDNTIEENIRVG------KKGATKEEIIKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARA 481
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 482 FLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
350-543 |
1.07e-28 |
|
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: 112.11 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPyDELLDRISIVMQNVQLFDN-TIEENIRvg 428
Cdd:cd03230 19 ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLPEEPSLYENlTVRENLK-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 429 kkgatkeeiikaakkarihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQD 508
Cdd:cd03230 96 ---------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWE 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 446410310 509 AITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNL 543
Cdd:cd03230 137 LLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
350-547 |
1.23e-28 |
|
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: 113.38 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDEllDRISIVMQNVQLFDN-TIEENI--- 425
Cdd:cd03259 19 LSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER--RNIGMVFQDYALFPHlTVAENIafg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 ---RVGKKGATKEEIIKAAKKARIHDFIMSLPkgYEtdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVN 502
Cdd:cd03259 97 lklRGVPKAEIRARVRELLELVGLEGLLNRYP--HE---------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446410310 503 ESLIQDAITELAKNR--TVLVVAHHL-KTIQKADQILVFQKGNLLEKG 547
Cdd:cd03259 166 REELREELKELQRELgiTTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
326-555 |
6.36e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 113.36 E-value: 6.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 326 PKDNDIAFENIDFSYeKDEFK--MEKLSFSIAEKTMTALVGESGSGKTTITNL---LLRFYDVHKGKITLGGTDIRDIPY 400
Cdd:PRK13640 1 MKDNIVEFKHVSFTY-PDSKKpaLNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 401 DELLDRISIVMQNV--QLFDNTIEENIRVG--KKGATKEEIIKAAKKA----RIHDFIMSLPKGyetdigenggiLSGGQ 472
Cdd:PRK13640 80 WDIREKVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVladvGMLDYIDSEPAN-----------LSGGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 473 RQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHG 550
Cdd:PRK13640 149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPV 228
|
....*
gi 446410310 551 ELLAK 555
Cdd:PRK13640 229 EIFSK 233
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
350-554 |
8.74e-28 |
|
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: 110.99 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNVQLFDN-TIEENIRV 427
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPElTVEENLLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GKKGATKEEIikaakKARIhDFIMSL-PKGYETdIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:cd03224 99 GAYARRRAKR-----KARL-ERVYELfPRLKER-RKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446410310 507 QDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:cd03224 172 FEAIRELRDeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
331-548 |
1.26e-27 |
|
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: 110.28 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKmekLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPydeLLDR-ISI 409
Cdd:cd03298 1 VRLDKIRFSYGEQPMH---FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP---PADRpVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDN-TIEENIRVGKKGATK------EEIIKAAKKARIHDFIMSLPkgyetdigengGILSGGQRQRISIARAF 482
Cdd:cd03298 75 LFQENNLFAHlTVEQNVGLGLSPGLKltaedrQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 483 LKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQKADQILVFqkgnlLEKGK 548
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRLAQRVVF-----LDNGR 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-559 |
1.75e-27 |
|
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: 118.12 E-value: 1.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 5 MLKLLTKTGKRDLIISSVFFALYGLSSIAMIVIVfSILFQIFDGTSLASLYKYFIAiGLLVV-----------FKGICnM 73
Cdd:TIGR00957 307 LFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQIL-SLLIRFVNDPMAPDWQGYFYT-GLLFVcaclqtlilhqYFHIC-F 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 74 VADMKKHSAGFDIVqqIRERMII--KLKKFSlgfytneRLGEINTILHKDVD---NMSLVVGHMWSRMFGDFL------- 141
Cdd:TIGR00957 384 VSGMRIKTAVMGAV--YRKALVItnSARKSS-------TVGEIVNLMSVDAQrfmDLATYINMIWSAPLQVILalyflwl 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 142 -IGAVVFVGLAsidfklaiIMAVSVPI-ALIFLYLTIKQSEKIENQNNSalldmVSLFVEYVRGIPVLKSFSNNKSLDNE 219
Cdd:TIGR00957 455 nLGPSVLAGVA--------VMVLMVPLnAVMAMKTKTYQVAHMKSKDNR-----IKLMNEILNGIKVLKLYAWELAFLDK 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 220 LMNKTKKFGETSKAASRFKAkqLSIFGFLLDiGYLVLLIAGAILVIKGNLDVLN----FIIFAVISKEFYkPFASMEQHY 295
Cdd:TIGR00957 522 VEGIRQEELKVLKKSAYLHA--VGTFTWVCT-PFLVALITFAVYVTVDENNILDaekaFVSLALFNILRF-PLNILPMVI 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 296 MYYVSAVDSYERLSRIL-YADVIPDKVNGIVPKD---NDIAFENIDFSYEKDEF-KMEKLSFSIAEKTMTALVGESGSGK 370
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFLsHEELEPDSIERRTIKPgegNSITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGK 677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 371 TTITNLLLRFYDVHKGKITLGGTdirdipydelldrISIVMQNVQLFDNTIEENIRVGKKGATK--EEIIKAAkkARIHD 448
Cdd:TIGR00957 678 SSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEKyyQQVLEAC--ALLPD 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 449 FIMsLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDP-VNESLIQDAITE--LAKNRTVLVVAHH 525
Cdd:TIGR00957 743 LEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGKHIFEHVIGPegVLKNKTRILVTHG 821
|
570 580 590
....*....|....*....|....*....|....
gi 446410310 526 LKTIQKADQILVFQKGNLLEKGKHGELLAKNGYY 559
Cdd:TIGR00957 822 ISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
333-541 |
3.73e-27 |
|
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: 109.16 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 333 FENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGtdirdIPYDELLDRISIVMQ 412
Cdd:cd03235 2 VEDLTVSYGGHPV-LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 413 NVQL---FDNTIEENI---RVGKKG-------ATKEEIIKAAKKARIHDFImslpkgyETDIGEnggiLSGGQRQRISIA 479
Cdd:cd03235 76 RRSIdrdFPISVRDVVlmgLYGHKGlfrrlskADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
331-548 |
6.41e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 108.41 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKmekLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTD-IRDIPYDElldRISI 409
Cdd:TIGR01277 1 LALDKVRYEYEHLPME---FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShTGLAPYQR---PVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDN-TIEENIRVGKKGATK------EEIIKAAKKARIHDFIMSLPkgyetdigengGILSGGQRQRISIARAF 482
Cdd:TIGR01277 75 LFQENNLFAHlTVRQNIGLGLHPGLKlnaeqqEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 483 LKDAPILILDEMTSNVDPVNESLIQDAITELA--KNRTVLVVAHHLK-TIQKADQILVFQKGNLLEKGK 548
Cdd:TIGR01277 144 VRPNPILLLDEPFSALDPLLREEMLALVKQLCseRQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVSD 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
344-555 |
6.41e-27 |
|
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: 108.96 E-value: 6.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 344 EFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDEllDRISIVMQNVQLFDN-TIE 422
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 423 ENIRVGKKgatKEEIIKAAKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDP-V 501
Cdd:cd03299 90 KNIAYGLK---KRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 502 NESLIQDaITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAK 555
Cdd:cd03299 165 KEKLREE-LKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
17-308 |
2.56e-26 |
|
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: 108.79 E-value: 2.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMII 96
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 97 KLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTI 176
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 177 KQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVL 256
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446410310 257 LIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYERL 308
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-547 |
6.00e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.92 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 322 NGIVPKDNDIAFENIDFsyekdefkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVH-----KGKITLGGTDIR 396
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEV--------LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 397 DIPYDELLDRISIVMQ------NVQLFDNT---IEENIRVGKKGATKEEIIKAAKKARIHDFImslpkgyETDIGENGGI 467
Cdd:PRK14247 74 KMDVIELRRRVQMVFQipnpipNLSIFENValgLKLNRLVKSKKELQERVRWALEKAQLWDEV-------KDRLDAPAGK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 468 LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEK 546
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEW 226
|
.
gi 446410310 547 G 547
Cdd:PRK14247 227 G 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
350-541 |
1.18e-25 |
|
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: 103.81 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYD--ELLDRISIVMQNVQLFDN-TIEENIR 426
Cdd:cd03229 19 VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFPHlTVLENIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGkkgatkeeiikaakkarihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:cd03229 99 LG---------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 446410310 507 QDAITELAKN--RTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:cd03229 140 RALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
331-548 |
3.00e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.73 E-value: 3.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYekDEFK-MEKLSFSIAEKTMTALVGESGSGKTTitnlLLR-------FYDVHK--GKITLGGTDIRDIPY 400
Cdd:COG1117 12 IEVRNLNVYY--GDKQaLKDINLDIPENKVTALIGPSGCGKST----LLRclnrmndLIPGARveGEILLDGEDIYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 401 D--ELLDRISIVMQNVQLFDNTIEENIRVG------KKGATKEEIIKAA-KKA--------RIHDfimslpkgyetdige 463
Cdd:COG1117 86 DvvELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKAalwdevkdRLKK--------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 464 NGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLktiQKA----DQILVFQ 539
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNM---QQAarvsDYTAFFY 227
|
....*....
gi 446410310 540 KGNLLEKGK 548
Cdd:COG1117 228 LGELVEFGP 236
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
331-538 |
3.72e-25 |
|
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: 103.71 E-value: 3.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFK---MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDelldrI 407
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFD-NTIEENIRVG------KKGATKEEIIKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIAR 480
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 481 AFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHL-KTIQKADQILVF 538
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIdEAVFLADRVVVL 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
331-554 |
4.51e-25 |
|
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: 103.74 E-value: 4.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEkDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD---RI 407
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFDN-TIEENIRVG--KKGATKEEII--KAAKKAR---IHDFIMSLPkgyetdiGEnggiLSGGQRQRISIA 479
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPlrEHTRLSEEEIreIVLEKLEavgLRGAEDLYP-------AE----LSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITEL--AKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
330-547 |
6.26e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 106.34 E-value: 6.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTitnlLLR----FYDVHKGKITLGGTDIRDI-PYDell 404
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGLpPEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 405 DRISIVMQNVQLFDN-TIEENIRVG--KKGATKEEIikaakKARIHDFI--MSLPkGYET-DIGEnggiLSGGQRQRISI 478
Cdd:COG3842 77 RNVGMVFQDYALFPHlTVAENVAFGlrMRGVPKAEI-----RARVAELLelVGLE-GLADrYPHQ----LSGGQQQRVAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPvneSLIQDAITELAK-----NRTVLVVAHHLK---TIqkADQILVFQKGNLLEKG 547
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDA---KLREEMREELRRlqrelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
331-557 |
7.43e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 104.33 E-value: 7.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY-EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNV--QLFDNTIEENIRVG--KKGATKEEIIK----AAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARA 481
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGleNIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 482 FLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQKADQILVFQKGNLLEKG------KHGELL 553
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGtpeeifKSGHML 234
|
....
gi 446410310 554 AKNG 557
Cdd:PRK13635 235 QEIG 238
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
350-544 |
2.09e-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: 101.43 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPyDELLDRISIVMQNVQLFDN-TIEENIRV- 427
Cdd:cd03263 21 LSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR-KAARQSLGYCPQFDALFDElTVREHLRFy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 -GKKGATKEEIIKAAKKARIHdfiMSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:cd03263 100 aRLKGLPKSEIKEEVELLLRV---LGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 446410310 507 QDAITELAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLL 544
Cdd:cd03263 173 WDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
328-554 |
2.11e-24 |
|
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: 101.98 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 328 DNDIAFENIDFSYekDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD- 405
Cdd:COG1127 3 EPMIEVRNLTKSF--GDRVvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 --RISIVMQNVQLFDN-TIEENIRVG---KKGATKEEIIKAAKKA----RIHDFIMSLPkgyetdiGEnggiLSGGQRQR 475
Cdd:COG1127 81 rrRIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 476 ISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGEL 552
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 446410310 553 LA 554
Cdd:COG1127 230 LA 231
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
331-556 |
2.88e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.58 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYekDEFKMeKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDElldR-ISI 409
Cdd:PRK10771 2 LKLTDITWLY--HHLPM-RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR---RpVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDN-TIEENIRVGK------KGATKEEIIKAAKKARIHDFIMSLPkgyetdigengGILSGGQRQRISIARAF 482
Cdd:PRK10771 76 LFQENNLFSHlTVAQNIGLGLnpglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 483 LKDAPILILDEMTSNVDPV--NE--SLIQDAITElaKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAKN 556
Cdd:PRK10771 145 VREQPILLLDEPFSALDPAlrQEmlTLVSQVCQE--RQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
350-554 |
3.37e-24 |
|
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: 103.21 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYD---VHKGKITLGGTDIRDIPYDELLD----RISIVMQN-------VQ 415
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtslnpVM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 416 LFDNTIEENIRV---GKKGATKEEIIKAAKKARIHD---FIMSLPkgYEtdigenggiLSGGQRQRISIARAFLKDAPIL 489
Cdd:COG0444 104 TVGDQIAEPLRIhggLSKAEARERAIELLERVGLPDperRLDRYP--HE---------LSGGMRQRVMIARALALEPKLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:COG0444 173 IADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFE 240
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
350-547 |
1.74e-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: 99.43 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNVQLFDN-TIEENIRV 427
Cdd:cd03219 19 VSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLENVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GKKGATKEEII---KAAKKARIHDFIMSLPK--GYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVN 502
Cdd:cd03219 99 AAQARTGSGLLlarARREEREARERAEELLErvGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446410310 503 ESLIQDAITELA-KNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03219 179 TEELAELIRELReRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
350-552 |
2.44e-23 |
|
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: 98.75 E-value: 2.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNVQLFDN-TIEENIRV 427
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFPRlTVEENLLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GKKGAtkeeiikAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPvneSLIQ 507
Cdd:TIGR03410 99 GLAAL-------PRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP---SIIK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446410310 508 D---AITELAKNR--TVLVVAHHLK-TIQKADQILVFQKGNLLEKGKHGEL 552
Cdd:TIGR03410 169 DigrVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-552 |
2.48e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 105.25 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 333 FENIDFSY-EKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVM 411
Cdd:PTZ00243 1311 FEGVQMRYrEGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 QNVQLFDNTIEENIRVGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILIL 491
Cdd:PTZ00243 1391 QDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIL 1469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 492 -DEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGEL 552
Cdd:PTZ00243 1470 mDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
351-547 |
3.90e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 98.14 E-value: 3.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTI---TNLLLRFydvHKGKITLGGTDI----RDIpyDELLDRISIVMQNVQLFDN-TIE 422
Cdd:COG1126 21 SLDVEKGEVVVIIGPSGSGKSTLlrcINLLEEP---DSGTITVDGEDLtdskKDI--NKLRRKVGMVFQQFNLFPHlTVL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 423 ENI-----RVgkKGATKEEIIKAA----KKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARAFLKDAPILILDE 493
Cdd:COG1126 96 ENVtlapiKV--KKMSKAEAEERAmellERVGLADKADAYPAQ-----------LSGGQQQRVAIARALAMEPKVMLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 494 MTSNVDP--VNESLiqDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:COG1126 163 PTSALDPelVGEVL--DVMRDLAKEgMTMVVVTHEMGFAREvADRVVFMDGGRIVEEG 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
330-547 |
6.27e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 100.15 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTitnlLLR----FYDVHKGKITLGGTDIRDIPYDellD 405
Cdd:COG3839 3 SLELENVSKSYGGVEA-LKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTSGEILIGGRDVTDLPPK---D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 R-ISIVMQNVQLFDN-TIEENIRVGKK--GATKEEIIK----AAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRIS 477
Cdd:COG3839 75 RnIAMVFQSYALYPHmTVYENIAFPLKlrKVPKAEIDRrvreAAELLGLEDLLDRKPKQ-----------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 478 IARAFLKDAPILILDEMTSNVDPvneSLIQDAITELAK-----NRTVLVVAHH------LktiqkADQILVFQKGNLLEK 546
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDA---KLRVEMRAEIKRlhrrlGTTTIYVTHDqveamtL-----ADRIAVMNDGRIQQV 215
|
.
gi 446410310 547 G 547
Cdd:COG3839 216 G 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
348-535 |
6.99e-23 |
|
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: 96.78 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKTTitnlLLR----FYDVHKGKITLGGTDIRDIPyDELLDRISIVMQNVQLFDN-TIE 422
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 423 ENI----RVGKKGATKEEIIKAAKKARIHDFiMSLPKGYetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNV 498
Cdd:COG4133 94 ENLrfwaALYGLRADREAIDEALEAVGLAGL-ADLPVRQ----------LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 446410310 499 DPVNESLIQDAITE-LAKNRTVLVVAHHLKTIQKADQI 535
Cdd:COG4133 163 DAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
331-541 |
9.88e-23 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.85 E-value: 9.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY--EKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRdipydELLDRI 407
Cdd:COG1116 8 LELRGVSKRFptGGGGVTaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFD-NTIEENIRVG--KKGATKEEIIKAAKK--ARIH--DFIMSLPkgYEtdigenggiLSGGQRQRISIAR 480
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGleLRGVPKAERRERAREllELVGlaGFEDAYP--HQ---------LSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 481 AFLKDAPILILDEMTSNVDPVNESLIQDAITEL--AKNRTVLVVAH------HLktiqkADQILVFQKG 541
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
331-547 |
1.82e-22 |
|
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: 95.31 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEK-----LSFSIAEKTMTALVGESGSGKTTITNLL--LRFYDVHKGKITLGGTDIRDipyDEL 403
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqllknVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 404 LDRISIVMQNVQLFDN-TIEENIRVgkkgatkeeiikAAKKarihdfimslpKGyetdigenggiLSGGQRQRISIARAF 482
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF------------AAKL-----------RG-----------LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 483 LKDAPILILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHLKT--IQKADQILVFQKGNLLEKG 547
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
331-541 |
2.15e-22 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 96.28 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD---RI 407
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFDN-TIEENI---RVGKKGA--------TKEEIIKA---------AKKA--RIHDfimslpkgyetdigen 464
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVlagRLGRTSTwrsllglfPPEDRERAlealervglADKAyqRADQ---------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 465 ggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:COG3638 147 ---LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDG 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
347-541 |
3.45e-22 |
|
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: 94.90 E-value: 3.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI--RDIPYDELLDRISIVMQNVQLFDN-TIEE 423
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 424 NIRVGK---KGATKEEIIKAA----KKARIHDFIMSLPkgyetdigengGILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:cd03262 96 NITLAPikvKGMSKAEAEERAlellEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446410310 497 NVDP--VNESLiqDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:cd03262 165 ALDPelVGEVL--DVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
327-548 |
6.50e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 95.59 E-value: 6.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 327 KDNDIAFENIDFSYEKDE-FKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD 405
Cdd:PRK13648 4 KNSIIVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 RISIVMQNV--QLFDNTIEENIRVGKKGAT------KEEIIKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRIS 477
Cdd:PRK13648 84 HIGIVFQNPdnQFVGSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 478 IARAFLKDAPILILDEMTSNVDPVNESLIQDAITELA--KNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGK 548
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
351-555 |
6.59e-22 |
|
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: 95.40 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD----RISIVMQNVQLFDN-TIEENI 425
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RVGK--KGATKEEIIKAAKKA----RIHDFIMSLPkgyetdigengGILSGGQRQRISIARAFLKDAPILILDEMTSNVD 499
Cdd:cd03294 124 AFGLevQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 500 PVNESLIQDAITELAKN--RTVLVVAHHL-KTIQKADQILVFQKGNLLEKGKHGELLAK 555
Cdd:cd03294 193 PLIRREMQDELLRLQAElqKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
348-555 |
6.61e-22 |
|
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: 94.57 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKTTITNL--LLRFYDvhKGKITLGGTDIRDIPYDELLD---RISIVMQNVQLFDN-TI 421
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCinGLERPT--SGSVLVDGTDLTLLSGKELRKarrRIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 422 EENIRVGKKGATKEeiiKAAKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPV 501
Cdd:cd03258 100 FENVALPLEIAGVP---KAEIEERVLELLELV--GLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 502 NESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAK 555
Cdd:cd03258 175 TTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
335-547 |
8.33e-22 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 93.90 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 335 NIDFSYEKDEFKMeKLSFSIAEKTmTALVGESGSGKTTITNLLLRFYDVHKGKITLGGT---DIR---DIPYDEllDRIS 408
Cdd:cd03297 3 CVDIEKRLPDFTL-KIDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkkiNLPPQQ--RKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDN-TIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLPKGYEtdigengGILSGGQRQRISIARAFLKDAP 487
Cdd:cd03297 79 LVFQQYALFPHlNVRENLAFGLKRKRNREDRISVDELLDLLGLDHLLNRYP-------AQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
331-536 |
8.78e-22 |
|
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: 94.56 E-value: 8.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD---RI 407
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFDN-TIEENIRVGKKGA-----------TKEEIIKAAKkarihdfimSLPK-GYETDIGENGGILSGGQRQ 474
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALA---------ALERvGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 475 RISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELA--KNRTVLVVAHHLKTIQK-ADQIL 536
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAREyADRIV 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
330-562 |
9.56e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYEKD---EFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGG----TDIRDIPYD 401
Cdd:PRK13645 6 DIILDNVSYTYAKKtpfEFKaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 402 ELLDR-ISIVMQ--NVQLFDNTIEENIRVG--KKGATKEEIIKaaKKARIHDFImSLPKGYetdIGENGGILSGGQRQRI 476
Cdd:PRK13645 86 KRLRKeIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLKLV-QLPEDY---VKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN--RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFEIF 239
|
....*....
gi 446410310 554 AKNGYYTKL 562
Cdd:PRK13645 240 SNQELLTKI 248
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-554 |
2.11e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 94.39 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYEK--DEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVM 411
Cdd:PRK13642 8 ENLVFKYEKesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 QNV--QLFDNTIEENIRVG--KKGATKEEIIKAAKKA----RIHDFIMSLPkgyetdigengGILSGGQRQRISIARAFL 483
Cdd:PRK13642 88 QNPdnQFVGATVEDDVAFGmeNQGIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 484 KDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
334-547 |
4.47e-21 |
|
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: 91.55 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYEKDEfKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDellDR-ISIVMQ 412
Cdd:cd03301 4 ENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRdIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 413 NVQLFDN-TIEENIRVGKK--GATKEEIIK----AAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARAFLKD 485
Cdd:cd03301 80 NYALYPHmTVYDNIAFGLKlrKVPKDEIDErvreVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 486 APILILDEMTSNVDPvneSLIQDAITELAK-----NRTVLVVAH-HLKTIQKADQILVFQKGNLLEKG 547
Cdd:cd03301 149 PKVFLMDEPLSNLDA---KLRVQMRAELKRlqqrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
331-541 |
7.88e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 7.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY-EKDEFKMEKL---SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRD--IPYDELL 404
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALdnvNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 405 DRISIVMQ--NVQLFDNTIEENIRVGKK--GATKEEIIKAAKKArihdfiMSLPK-GYETDIGENGGILSGGQRQRISIA 479
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPInlGLSEEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKG 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
331-529 |
1.19e-20 |
|
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: 90.54 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI-----RDIPYdeLLD 405
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrgRAIPY--LRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 RISIVMQNVQLF-DNTIEENIR-----VGKKGATKEEIIKAAK-----KARIHDFIMSLpkgyetdigenggilSGGQRQ 474
Cdd:cd03292 79 KIGVVFQDFRLLpDRNVYENVAfalevTGVPPREIRKRVPAALelvglSHKHRALPAEL---------------SGGEQQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 475 RISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTI 529
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKEL 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
331-561 |
1.39e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKdEFKMEK-----LSFSIAEKTMTALVGESGSGKTTIT---NLLLRfydVHKGKITLGGTDIR----DI 398
Cdd:PRK13641 3 IKFENVDYIYSP-GTPMEKkgldnISFELEEGSFVALVGHTGSGKSTLMqhfNALLK---PSSGTITIAGYHITpetgNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 399 PYDELLDRISIVMQ--NVQLFDNTIEENIRVGKK--GATKEEIIKAAKKArihdfimsLPK-GYETDIGENGGI-LSGGQ 472
Cdd:PRK13641 79 NLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfGFSEDEAKEKALKW--------LKKvGLSEDLISKSPFeLSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 473 RQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHG 550
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPK 230
|
250
....*....|.
gi 446410310 551 ELLAKNGYYTK 561
Cdd:PRK13641 231 EIFSDKEWLKK 241
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
331-547 |
2.00e-20 |
|
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: 90.37 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEkDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDEllDRISIV 410
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQLFDN-TIEENIRVG--KKGATKEEIikaakKARIHDFI-MSLPKGYET-DIGEnggiLSGGQRQRISIARAFLKD 485
Cdd:cd03300 78 FQNYALFPHlTVFENIAFGlrLKKLPKAEI-----KERVAEALdLVQLEGYANrKPSQ----LSGGQQQRVAIARALVNE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 486 APILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAH-HLKTIQKADQILVFQKGNLLEKG 547
Cdd:cd03300 149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
340-553 |
2.78e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 90.61 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 340 YEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDV-----HKGKITLGGTDIRDIPYD--ELLDRISIVMQ 412
Cdd:PRK14243 19 YYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 413 NVQLFDNTIEENI----RV-GKKGATKEEIIKAAKKARIHDFImslpkgyETDIGENGGILSGGQRQRISIARAFLKDAP 487
Cdd:PRK14243 99 KPNPFPKSIYDNIaygaRInGYKGDMDELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKG-KHGELL 553
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGgRYGYLV 238
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
347-543 |
3.35e-20 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 90.68 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVhKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIR 426
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:cd03289 99 PYGK-WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 446410310 507 QDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNL 543
Cdd:cd03289 178 RKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
330-557 |
3.65e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 90.85 E-value: 3.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYE-KDEFKMEKL---SFSIAEKTMTALVGESGSGKTTIT---NLLLRfydVHKGKITLGGTDI----RDI 398
Cdd:PRK13634 2 DITFQKVEHRYQyKTPFERRALydvNVSIPSGSYVAIIGHTGSGKSTLLqhlNGLLQ---PTSGTVTIGERVItagkKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 399 PYDELLDRISIVMQ--NVQLFDNTIEENIRVGKK--GATKEEIIKAAKKarihdfiMSLPKGYETDIGENGGI-LSGGQR 473
Cdd:PRK13634 79 KLKPLRKKVGIVFQfpEHQLFEETVEKDICFGPMnfGVSEEDAKQKARE-------MIELVGLPEELLARSPFeLSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 474 QRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL--AKNRTVLVVAHHLKTI-QKADQILVFQKGNLLEKG--- 547
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGtpr 231
|
250
....*....|...
gi 446410310 548 ---KHGELLAKNG 557
Cdd:PRK13634 232 eifADPDELEAIG 244
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
350-554 |
4.10e-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: 90.10 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNVQLFDN-TIEENIRV 427
Cdd:COG0411 23 VSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLENVLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GKKGATKEEIIKA--------AKKARIHDFIMSLPK--GYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSN 497
Cdd:COG0411 103 AAHARLGRGLLAAllrlprarREEREARERAEELLErvGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAG 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 498 VDPVnESL-IQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQkgnllekgkHGELLA 554
Cdd:COG0411 183 LNPE-ETEeLAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLD---------FGRVIA 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
338-541 |
4.48e-20 |
|
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: 88.93 E-value: 4.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 338 FSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR----ISIVMQN 413
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 414 VQLFDNTIEENIRVGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDE 493
Cdd:cd03290 88 PWLLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446410310 494 MTSNVD-PVNESLIQDAITELAKN--RTVLVVAHHLKTIQKADQILVFQKG 541
Cdd:cd03290 167 PFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
331-542 |
8.82e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.33 E-value: 8.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVH-----KGKITLGGTDI--RDIPYDEL 403
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 404 LDRISIVMQNVQLFDNTIEENIRVGKKgatkeeIIKAAKKARIHDFIMSLPKGYE------TDIGENGGILSGGQRQRIS 477
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVK------IVGWRPKLEIDDIVESALKDADlwdeikHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 478 IARAFLKDAPILILDEMTSNVDPVN----ESLIQDaiTELAKNRTVLVVAHHLKTIQKADQILVFQKGN 542
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQS--LRLRSELTMVIVSHNLHQVSRLSDFTAFFKGN 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
328-547 |
8.87e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 328 DNDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTitnLLLRF---YDVHKGKITLGGTDIRDIPYDELL 404
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHLngiYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 405 DRISIVMQNV--QLFDNTIEENIRVG--KKGATKEEIIK----AAKKARIHDFIMSLPkgYEtdigenggiLSGGQRQRI 476
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERrveeALKAVRMWDFRDKPP--YH---------LSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHLK-TIQKADQILVFQKGNLLEKG 547
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
359-547 |
9.29e-20 |
|
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: 88.02 E-value: 9.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 359 MTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPyDELLDRISIVMQNVQLFDN-TIEENI-------RVGKK 430
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQEFGVYPNfTVREFLdyiawlkGIPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 431 GAtKEEIIKAAKKARIHDFimslpkgYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAI 510
Cdd:cd03264 106 EV-KARVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 446410310 511 TELAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03264 174 SELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
20-304 |
1.20e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 89.26 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 20 SSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLK 99
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 100 KFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQS 179
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 180 EKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIA 259
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446410310 260 GAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHY---MYYVSAVDS 304
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWhagYQGISAADS 288
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
347-547 |
1.31e-19 |
|
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: 87.81 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYdELLDRISIVMQNVQLFDN-TIEENI 425
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA-EARRRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RV-----GKKGAtkeeiikaAKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDP 500
Cdd:cd03266 100 EYfaglyGLKGD--------ELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446410310 501 VNESLIQDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03266 170 MATRALREFIRQLrALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
334-548 |
1.58e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.29 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYEKDEfKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVH-----KGKITLGGTDIRDIPYD--ELLDR 406
Cdd:PRK14239 9 SDLSVYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDtvDLRKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 ISIVMQNVQLFDNTIEENIRVGK--KGATKEEIIKAA-----KKARIHDFIMSlpKGYETDIGenggiLSGGQRQRISIA 479
Cdd:PRK14239 88 IGMVFQQPNPFPMSIYENVVYGLrlKGIKDKQVLDEAvekslKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGK 548
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
350-554 |
2.09e-19 |
|
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: 87.21 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDElldR----ISIVMQNVQLFDN-TIEEN 424
Cdd:cd03218 19 VSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK---RarlgIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 425 IRVGKKGATKEEIIKAAK-KARIHDF-IMSLPKgyetdigENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVN 502
Cdd:cd03218 96 ILAVLEIRGLSKKEREEKlEELLEEFhITHLRK-------SKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446410310 503 ESLIQDAITEL-AKNRTVLVVAHHLK-TIQKADQILVFQKGNLLEKGKHGELLA 554
Cdd:cd03218 169 VQDIQKIIKILkDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
350-554 |
3.37e-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: 86.96 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNVQLFDN-TIEENIRV 427
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFPSlTVEENLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GKKGATKeeiiKAAKKARIhDFIMSL-PKGYETdIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDP--VNEs 504
Cdd:COG0410 102 GAYARRD----RAEVRADL-ERVYELfPRLKER-RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPliVEE- 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446410310 505 lIQDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:COG0410 175 -IFEIIRRLNReGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
347-555 |
3.60e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.90 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGtdirdipydelldRISIVMQNVQLFDNTIEENIR 426
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGkkgATKEE-----IIKAAKkarIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPV 501
Cdd:TIGR01271 509 FG---LSYDEyrytsVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 502 NESLI-QDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAK 555
Cdd:TIGR01271 583 TEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
347-552 |
3.67e-19 |
|
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: 87.99 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGtdirdipydelldRISIVMQNVQLFDNTIEENIR 426
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKkgATKEEIIKAAKKA-RIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESL 505
Cdd:cd03291 120 FGV--SYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446410310 506 IQDA-ITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGEL 552
Cdd:cd03291 198 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
331-562 |
4.37e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.91 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKD---EFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELL-- 404
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 405 --DRISIVMQ--NVQLFDNTIEENIRVGKK--GATKEEIikaakKARIHDFIMSLpkGYETDIGENGGI-LSGGQRQRIS 477
Cdd:PRK13646 83 vrKRIGMVFQfpESQLFEDTVEREIIFGPKnfKMNLDEV-----KNYAHRLLMDL--GFSRDVMSQSPFqMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 478 IARAFLKDAPILILDEMTSNVDPVNESLIQDAITELA--KNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
....*...
gi 446410310 555 KNGYYTKL 562
Cdd:PRK13646 236 DKKKLADW 243
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
362-554 |
5.66e-19 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 88.32 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 362 LVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDelLDRISIVMQNVQLFDN-TIEENIRVGKK--GATKEEIi 438
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHmTVEENVAFGLKmrKVPRAEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 439 kaakKARIHDfimSLPKGYETDIGENGGI-LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR 517
Cdd:TIGR01187 78 ----KPRVLE---ALRLVQLEEFADRKPHqLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446410310 518 --TVLVVAH-HLKTIQKADQILVFQKGNLLEKGKHGELLA 554
Cdd:TIGR01187 151 giTFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-548 |
7.95e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 86.43 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 327 KDNDIAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVH-----KGKITLGGTDIRDIPYD 401
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 402 --ELLDRISIVMQNVQLFDN-TIEENIRVGKK----GATKEEIIK----AAKKARIHDFIMSLPKGYETDigenggiLSG 470
Cdd:PRK14267 80 piEVRREVGMVFQYPNPFPHlTIYDNVAIGVKlnglVKSKKELDErvewALKKAALWDEVKDRLNDYPSN-------LSG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 471 GQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHH-LKTIQKADQILVFQKGNLLEKGK 548
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGP 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
332-561 |
8.62e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 332 AFENIDFSYEKDefkmeKLSFsiaektmtaLVGESGSGKTTITN----LL------LRFYDVHKG-KITLGGTDIRDIP- 399
Cdd:PRK13631 41 ALNNISYTFEKN-----KIYF---------IIGNSGSGKSTLVThfngLIkskygtIQVGDIYIGdKKNNHELITNPYSk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 400 ----YDELLDRISIVMQ--NVQLFDNTIEENIRVG--KKGATKEEiikAAKKARIHDFIMSLPKGYetdIGENGGILSGG 471
Cdd:PRK13631 107 kiknFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGpvALGVKKSE---AKKLAKFYLNKMGLDDSY---LERSPFGLSGG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 472 QRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHL-KTIQKADQILVFQKGNLLEKGKH 549
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTP 260
|
250
....*....|..
gi 446410310 550 GELLAKNGYYTK 561
Cdd:PRK13631 261 YEIFTDQHIINS 272
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-562 |
1.19e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.42 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 5 MLKLLTKTGKRDLIISSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGF 84
Cdd:PLN03232 291 LLRALNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGRVGF 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 85 DIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLV---VGHMWSRMFGDFLIGAVVF--VGLASIdFKlAI 159
Cdd:PLN03232 371 RLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIaeqLHGLWSAPFRIIVSMVLLYqqLGVASL-FG-SL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 160 IMAVSVPialiFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMnktkkfGETSKAASRF-K 238
Cdd:PLN03232 449 ILFLLIP----LQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQ------GIRNEELSWFrK 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 239 AKQLSIF-GFLLD-IGYLVLLIA-GAILVIKGNLD----VLNFIIFAVISKefykPFASMEQHYMYYVSAVDSYERLSRI 311
Cdd:PLN03232 519 AQLLSAFnSFILNsIPVVVTLVSfGVFVLLGGDLTparaFTSLSLFAVLRS----PLNMLPNLLSQVVNANVSLQRIEEL 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 312 LYADV-IPDKVNGIVPKDNDIAFENIDFSYEKDEFK--MEKLSFSIAEKTMTALVGESGSGKTTITNLLLrfydvhkGKI 388
Cdd:PLN03232 595 LLSEErILAQNPPLQPGAPAISIKNGYFSWDSKTSKptLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GEL 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 389 TLGGTDIRDIPydellDRISIVMQNVQLFDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMsLPKGYETDIGENGGIL 468
Cdd:PLN03232 668 SHAETSSVVIR-----GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDL-LPGRDLTEIGERGVNI 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 469 SGGQRQRISIARAFLKDAPILILDEMTSNVDP-VNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKG 547
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG 821
|
570
....*....|....*
gi 446410310 548 KHGELLAKNGYYTKL 562
Cdd:PLN03232 822 TFAELSKSGSLFKKL 836
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
330-553 |
2.90e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 330 DIAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISI 409
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQnvQLfdnTIEENIRV---------------GKKGATKEEII-KAAKKARIHDFIMSLPkgyeTDigenggiLSGGQR 473
Cdd:PRK11231 81 LPQ--HH---LTPEGITVrelvaygrspwlslwGRLSAEDNARVnQAMEQTRINHLADRRL----TD-------LSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 474 QRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGE 551
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEE 224
|
..
gi 446410310 552 LL 553
Cdd:PRK11231 225 VM 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
347-554 |
3.20e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.15 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDV-----HKGKITLGGTDI---RDIPydELLDRISIVMQNVQLFD 418
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDVL--EFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 419 NTIEENIRVGKKG--ATKEEIIKAAKKARIHDfiMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:PRK14271 115 MSIMDNVLAGVRAhkLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 497 NVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
348-547 |
5.07e-18 |
|
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: 82.65 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIpyDELLDRISIVMQNVQLFDN-TIEENIR 426
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALIEAPGFYPNlTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKKGATKeeiikaaKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:cd03268 95 LLARLLGI-------RKKRIDEVLDVV--GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKEL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446410310 507 QDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03268 166 RELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
331-493 |
6.80e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.20 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYekDEFK-MEKLSFSIAEKTMTALVGESGSGKTTitnlLLR------FYDvhKGKITLGGTDIR-DIPyde 402
Cdd:COG1118 3 IEVRNISKRF--GSFTlLDDVSLEIASGELVALLGPSGSGKTT----LLRiiagleTPD--SGRIVLNGRDLFtNLP--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 403 LLDR-ISIVMQNVQLFDN-TIEENIRVG--KKGATKEEIikaakKARIHDFI--MSLPkgyetdigengGI-------LS 469
Cdd:COG1118 72 PRERrVGFVFQHYALFPHmTVAENIAFGlrVRPPSKAEI-----RARVEELLelVQLE-----------GLadrypsqLS 135
|
170 180
....*....|....*....|....
gi 446410310 470 GGQRQRISIARAFLKDAPILILDE 493
Cdd:COG1118 136 GGQRQRVALARALAVEPEVLLLDE 159
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
347-552 |
8.54e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.16 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI-------RDIpydelldriSIVMQNVQLFDN 419
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthrsiqqRDI---------CMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 420 -TIEENIRVGKK--GATKEEIIKAAKKA-RIHDFImslpkGYETDIGENggiLSGGQRQRISIARAFLKDAPILILDEMT 495
Cdd:PRK11432 93 mSLGENVGYGLKmlGVPKEERKQRVKEAlELVDLA-----GFEDRYVDQ---ISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 496 SNVDPVNESLIQDAITELAK--NRTVLVVAH-HLKTIQKADQILVFQKGNLLEKGKHGEL 552
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
331-552 |
1.12e-17 |
|
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: 82.39 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIdfSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPydeLLDR-IS 408
Cdd:cd03296 3 IEVRNV--SKRFGDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERnVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDN-TIEENIRVG---KKGATKEEiiKAAKKARIHDFIM-----SLPKGYETDigenggiLSGGQRQRISIA 479
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGlrvKPRSERPP--EAEIRAKVHELLKlvqldWLADRYPAQ-------LSGGQRQRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 480 RAFLKDAPILILDEMTSNVDP-VNESL------IQDAItelakNRTVLVVAH-HLKTIQKADQILVFQKGNLLEKGKHGE 551
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAkVRKELrrwlrrLHDEL-----HVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
.
gi 446410310 552 L 552
Cdd:cd03296 224 V 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
331-554 |
1.18e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 1.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIP-YDELLDRISI 409
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQN--VQLFDNTIEENIRVGKKG------ATKEEIIKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARA 481
Cdd:PRK13644 82 VFQNpeTQFVGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSPKT-----------LSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 482 FLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
351-553 |
1.52e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.70 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD----RISIVMQNVQLFDN-TIEENI 425
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RVGKK--GATKEEIIKAAKKARIHDFIMSLPKGYETDigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNE 503
Cdd:PRK10070 128 AFGMElaGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446410310 504 SLIQDAITEL-AKN-RTVLVVAHHL-KTIQKADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK10070 201 TEMQDELVKLqAKHqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-553 |
2.10e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.73 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIrdiPYDELLDR--IS 408
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARLARarIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQnvqlFDN-----TIEENIRV-----GKKGATKEEIIKAakkarIHDFiMSLPKGYETDIGEnggiLSGGQRQRISI 478
Cdd:PRK13536 118 VVPQ----FDNldlefTVRENLLVfgryfGMSTREIEAVIPS-----LLEF-ARLESKADARVSD----LSGGMKRRLTL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPVNESLIQDAITE-LAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALI 260
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
351-499 |
2.25e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 83.24 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAE-KTMtALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD---RISIVMQN----------VQl 416
Cdd:COG4608 38 SFDIRRgETL-GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDpyaslnprmtVG- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 fdNTIEENIRVGKKGAtkeeiiKAAKKARIHDfIMS---LPKGY------EtdigenggiLSGGQRQRISIARAFLKDAP 487
Cdd:COG4608 116 --DIIAEPLRIHGLAS------KAERRERVAE-LLElvgLRPEHadryphE---------FSGGQRQRIGIARALALNPK 177
|
170
....*....|..
gi 446410310 488 ILILDEMTSNVD 499
Cdd:COG4608 178 LIVCDEPVSALD 189
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
331-556 |
2.85e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.83 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKD---EFK-MEKLSFSIAEKTMTALVGESGSGKTTIT---NLLL--------------------RFYDV 383
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKaLDNVSVEINQGEFIAIIGQTGSGKTTFIehlNALLlpdtgtiewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 384 HKGKITLGGTDIRDIPY-DELLDRISIVMQ--NVQLFDNTIEENIRVGKK--GATKEEiikAAKKARIHDFIMSLPKGYe 458
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVsmGVSKEE---AKKRAAKYIELVGLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 459 tdIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHLKTI-QKADQIL 536
Cdd:PRK13651 159 --LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTI 236
|
250 260
....*....|....*....|
gi 446410310 537 VFQKGNLLEKGKHGELLAKN 556
Cdd:PRK13651 237 FFKDGKIIKDGDTYDILSDN 256
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
336-554 |
3.30e-17 |
|
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: 83.24 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 336 IDFSYEKDEFKMeKLSFSIAEKTMTALVGESGSGKTTITNL---LLRFYdvhKGKITLGGTDIRDIPYDELLD----RIS 408
Cdd:TIGR02142 3 ARFSKRLGDFSL-DADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRPD---EGEIVLNGRTLFDSRKGIFLPpekrRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDN-TIEENIRVGKKGATKEEiiKAAKKARIHDFImslpkGYETDIGENGGILSGGQRQRISIARAFLKDAP 487
Cdd:TIGR02142 79 YVFQEARLFPHlSVRGNLRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 488 ILILDEMTSNVD--------PVNESLIQdaitELakNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:TIGR02142 152 LLLMDEPLAALDdprkyeilPYLERLHA----EF--GIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
350-553 |
3.51e-17 |
|
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: 81.78 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDipydelLDRISI--VMQNVQL-FDNTIEE-NI 425
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQ------LDRKQRraFRRDVQLvFQDSPSAvNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RvgkkgATKEEII-----------KAAKKARIHDFI--MSLPkgyETDIGENGGILSGGQRQRISIARAFLKDAPILILD 492
Cdd:TIGR02769 104 R-----MTVRQIIgeplrhltsldESEQKARIAELLdmVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 493 EMTSNVDPVNESLIQDAITEL--AKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELL 553
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKLqqAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
4-545 |
3.56e-17 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 84.85 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 4 EMLKLLTKTGKRDLIISSVFFALYGLSSIAMIVIVFSILfqIFDGTSLASLYKYFIaiGLLVVFkGICNMVADMKKHSAG 83
Cdd:COG4615 2 NLLRLLLRESRWLLLLALLLGLLSGLANAGLIALINQAL--NATGAALARLLLLFA--GLLVLL-LLSRLASQLLLTRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 84 FDIVQQIRERMIIK-----LKKFslgfytnERLG--EINTILHKDVDNMSLVVGhmwsrMFGDFLIGAVVFVG----LAS 152
Cdd:COG4615 77 QHAVARLRLRLSRRilaapLERL-------ERIGaaRLLAALTEDVRTISQAFV-----RLPELLQSVALVLGclayLAW 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 153 IDFKLAIIMAVSVPIALIFLYLTIKQSEKienqnnsaLLDMVS-----LFVEY---VRGIPVLKsFSNNKS---LDNELm 221
Cdd:COG4615 145 LSPPLFLLTLVLLGLGVAGYRLLVRRARR--------HLRRAReaedrLFKHFralLEGFKELK-LNRRRRrafFDEDL- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 222 nktkkfGETSKAASRFKAKQLSIFGFLLDIGYLVLLIA-GAIL-----VIKGNLDVLNFIIFAVIskeFYK-PFASMEQH 294
Cdd:COG4615 215 ------QPTAERYRDLRIRADTIFALANNWGNLLFFALiGLILfllpaLGWADPAVLSGFVLVLL---FLRgPLSQLVGA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 295 YMYYVSAVDSYERLSRI---LYA---DVIPDKVNGIVPKDNDIAFENIDFSY--EKDE--FKMEKLSFSIAEKTMTALVG 364
Cdd:COG4615 286 LPTLSRANVALRKIEELelaLAAaepAAADAAAPPAPADFQTLELRGVTYRYpgEDGDegFTLGPIDLTIRRGELVFIVG 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 365 ESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIeenirvGKKGATKEEIIKA---- 440
Cdd:COG4615 366 GNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLL------GLDGEADPARAREller 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 441 ---AKKARIhdfimslpkgyetdigENGGI----LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVN-----ESLIQd 508
Cdd:COG4615 440 lelDHKVSV----------------EDGRFsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFrrvfyTELLP- 502
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 446410310 509 aitEL-AKNRTVLVVAH-----HLktiqkADQILVFQKGNLLE 545
Cdd:COG4615 503 ---ELkARGKTVIAISHddryfDL-----ADRVLKMDYGKLVE 537
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
338-553 |
4.32e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 81.25 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 338 FSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHK------GKITLGGTDIRDIPYDELLDRISIVM 411
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 QNVQLFDN-TIEENIRVGKKG---ATKEEIIKAAKKARIHdfiMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAP 487
Cdd:PRK14246 97 QQPNPFPHlSIYDNIAYPLKShgiKEKREIKKIVEECLRK---VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
350-545 |
5.44e-17 |
|
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: 80.56 E-value: 5.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELL----DRISIVMQNVQLFDN-TIEEN 424
Cdd:COG4181 31 ISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARArlraRHVGFVFQSFQLLPTlTALEN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 425 I-----RVGKKGATKeeiiKAAK-------KARIHDFimslPKGyetdigenggiLSGGQRQRISIARAFLKDAPILILD 492
Cdd:COG4181 111 VmlpleLAGRRDARA----RARAllervglGHRLDHY----PAQ-----------LSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 493 EMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQKADQILVFQKGNLLE 545
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
347-563 |
5.71e-17 |
|
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: 85.07 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIrDIPYDELLDRISIVMQNVQLFDN-TIEENI 425
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 --RVGKKGATKEEiikaakkARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNE 503
Cdd:TIGR01257 1025 lfYAQLKGRSWEE-------AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 504 SLIQDAITELAKNRTVLVVAHHLKTIQ-KADQILVFQKGNLLEKGKhgELLAKNGYYTKLW 563
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT--PLFLKNCFGTGFY 1156
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
17-277 |
7.24e-17 |
|
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: 81.31 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMII 96
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 97 KLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTI 176
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 177 KQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVL 256
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260
....*....|....*....|.
gi 446410310 257 LIAGAILVIKGNLDVLNFIIF 277
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISF 261
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
32-287 |
7.27e-17 |
|
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: 81.34 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 32 IAMIVIVF-----SILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFY 106
Cdd:cd18549 14 IAALDLVFplivrYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 107 TNERLGEINTILHKDVDNMSLVVGHMwsrmFGDFLIGAVVFVG----LASIDFKLAIIMAVSVPIALIFLYLTIKQSEKI 182
Cdd:cd18549 94 DNNKTGQLMSRITNDLFDISELAHHG----PEDLFISIITIIGsfiiLLTINVPLTLIVFALLPLMIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 183 ENQNNSALLDMVSLFVEYVRGIPVLKSFSNNkslDNELmnktKKFGETSKA--ASRFKA-KQLSIF----GFLLDIGYLV 255
Cdd:cd18549 170 FRRVREKIGEINAQLEDSLSGIRVVKAFANE---EYEI----EKFDEGNDRflESKKKAyKAMAYFfsgmNFFTNLLNLV 242
|
250 260 270
....*....|....*....|....*....|..
gi 446410310 256 LLIAGAILVIKGNLDVLNFIIFAVISKEFYKP 287
Cdd:cd18549 243 VLVAGGYFIIKGEITLGDLVAFLLYVNVFIKP 274
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
335-554 |
8.04e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 335 NIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTitnLLLRFYDVHK---GKITLGGTDIRdipYD-----ELLDR 406
Cdd:PRK13639 6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKST---LFLHFNGILKptsGEVLIKGEPIK---YDkksllEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 ISIVMQNV--QLFDNTIEENIRVG--KKGATKEEIIKAAKKArIHDFIMSlpkGYETDIGENggiLSGGQRQRISIARAF 482
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEA-LKAVGME---GFENKPPHH---LSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 483 LKDAPILILDEMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
350-500 |
8.36e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVH---KGKITLGGTDIRDIPydELLDRISIVMQNVQLFDN-TIEENI 425
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP--AEQRRIGILFQDDLLFPHlSVGENL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RVG-----KKGATKEEIIKAAKKARIHDFimslpkgYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDP 500
Cdd:COG4136 98 AFAlpptiGRAQRRARVEQALEEAGLAGF-------ADRDPAT----LSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
347-539 |
1.70e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.42 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVhKGKITLGGTDIRDIPYDELLDRISIVMQNVQLFDNTIEENIR 426
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKKgATKEEIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:TIGR01271 1314 PYEQ-WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQII 1392
|
170 180 190
....*....|....*....|....*....|...
gi 446410310 507 QDAITELAKNRTVLVVAHHLKTIQKADQILVFQ 539
Cdd:TIGR01271 1393 RKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
17-281 |
2.23e-16 |
|
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: 79.61 E-value: 2.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLSSIAMIvIVFSILFQIFDGTSLAS---LYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRER 93
Cdd:pfam00664 1 LILAILLAILSGAISPAFP-LVLGRILDVLLPDGDPEtqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 94 MIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLY 173
Cdd:pfam00664 80 LFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 174 LTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGY 253
Cdd:pfam00664 160 VFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSY 239
|
250 260
....*....|....*....|....*...
gi 446410310 254 LVLLIAGAILVIKGNLDVLNFIIFAVIS 281
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
350-524 |
2.51e-16 |
|
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: 78.47 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRfyDVHKGKITLGGTDIRDIPY--DELLDRISIVMQNVQLFDN-TIEENIR 426
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTTSGQILFNGQPRkpDQFQKCVAYVRQDDILLPGlTVRETLT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKKGATKEEIIKAAKKARIHDFIMSLPKgyETDIGEN--GGIlSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNES 504
Cdd:cd03234 104 YTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGGNlvKGI-SGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTAL 180
|
170 180
....*....|....*....|.
gi 446410310 505 LIQDAITELAK-NRTVLVVAH 524
Cdd:cd03234 181 NLVSTLSQLARrNRIVILTIH 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
354-554 |
3.55e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.25 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 354 IAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI-RDIPYD-------ELLDRISIVMQNVQLFDN-TIEEN 424
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSqqkglirQLRQHVGFVFQNFNLFPHrTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 425 IRVGK---KGATKEEIIKAAKKArihdfimsLPK----GYETDIGENggiLSGGQRQRISIARAFLKDAPILILDEMTSN 497
Cdd:PRK11264 106 IIEGPvivKGEPKEEATARAREL--------LAKvglaGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 498 VDP--VNESLiqDAITELAK-NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK11264 175 LDPelVGEVL--NTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
348-547 |
3.61e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 78.66 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKT-------------MTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNV 414
Cdd:PRK13548 6 RNLSVRLGGRTllddvsltlrpgeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 415 QL-FDNTIEENIRVG------KKGATKEEIIKAAKKARIHDFIMSLpkgYETdigenggiLSGGQRQRISIARAFL---- 483
Cdd:PRK13548 86 SLsFPFTVEEVVAMGraphglSRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 484 --KDAPILILDEMTSNVDPVNesliQDAITELAKNRT------VLVVAHHLK-TIQKADQILVFQKGNLLEKG 547
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAH----QHHVLRLARQLAherglaVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
331-547 |
4.78e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTT---ITNLLlrfyDVHK-GKITLGGT--DIRDIPYD--- 401
Cdd:COG4161 3 IQLKNINCFYGSHQA-LFDINLECPSGETLVLLGPSGAGKSSllrVLNLL----ETPDsGQLNIAGHqfDFSQKPSEkai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 402 -ELLDRISIVMQNVQLF------DNTIEENIRVgkKGATKEEIIKAAKKA----RIHDFIMSLPKGyetdigenggiLSG 470
Cdd:COG4161 78 rLLRQKVGMVFQQYNLWphltvmENLIEAPCKV--LGLSKEQAREKAMKLlarlRLTDKADRFPLH-----------LSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 471 GQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR-TVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQG 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-547 |
5.10e-16 |
|
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: 80.88 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDvHKGKITLGGTDIRDIPYDELLD---RISIVMQ----------NVql 416
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRALRPlrrRMQVVFQdpfgslsprmTV-- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 fDNTIEENIRVGKKGATKEEIIKAAKKA------------R-IHDFimslpkgyetdigenggilSGGQRQRISIARAF- 482
Cdd:COG4172 382 -GQIIAEGLRVHGPGLSAAERRARVAEAleevgldpaarhRyPHEF-------------------SGGQRQRIAIARALi 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 483 LKdaP-ILILDEMTSNVDpvneSLIQDAITELAK------NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:COG4172 442 LE--PkLLVLDEPTSALD----VSVQAQILDLLRdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQG 508
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
350-541 |
5.25e-16 |
|
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: 76.94 E-value: 5.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDelldRISIVMQNVQLFDNT--IEENIRV 427
Cdd:cd03269 19 ISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLPEERGLYPKMkvIDQLVYL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GK-KGATKEEIikaakKARIHDFIMSLpkgyetDIGENGGI----LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVN 502
Cdd:cd03269 95 AQlKGLKKEEA-----RRRIDEWLERL------ELSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446410310 503 ESLIQDAITELA-KNRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:cd03269 164 VELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
17-307 |
5.96e-16 |
|
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: 78.60 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMII 96
Cdd:cd18547 7 LAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 97 KLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTI 176
Cdd:cd18547 87 KLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 177 KQSEK--IENQNNSALLDMvslFV-EYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSkaasrFKAKQLS-----IFGFL 248
Cdd:cd18547 167 KRSQKyfRKQQKALGELNG---YIeEMISGQKVVKAFNREEEAIEEFDEINEELYKAS-----FKAQFYSgllmpIMNFI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 249 LDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYER 307
Cdd:cd18547 239 NNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
331-548 |
6.80e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 77.23 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEfKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELL-DRISI 409
Cdd:PRK11614 6 LSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrEAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDN-TIEENIRVGKKGATKEEIIKaaKKARIHDFimsLPKGYETDIgENGGILSGGQRQRISIARAFLKDAPI 488
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 489 LILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAhhlktiQKADQIL-VFQKGNLLEKGK 548
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVE------QNANQALkLADRGYVLENGH 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
331-554 |
1.01e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.31 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI-RDIPYDELldRISI 409
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQ--RVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQnvqlFDN-----TIEENIRV-----GKKGATKEEII-KAAKKARihdfimsLPKGYETDIGEnggiLSGGQRQRISI 478
Cdd:PRK13537 85 VPQ----FDNldpdfTVRENLLVfgryfGLSAAAARALVpPLLEFAK-------LENKADAKVGE----LSGGMKRRLTL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
331-548 |
1.80e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.09 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEK-DEFKMEKL---SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI------RDIpy 400
Cdd:PRK13649 3 INLQNVSYTYQAgTPFEGRALfdvNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 401 DELLDRISIVMQ--NVQLFDNTIEENIRVGKK--GATKEEIIKAAKKArihdfiMSLPKGYETDIGENGGILSGGQRQRI 476
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEETVLKDVAFGPQnfGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHL--KTIQKADQILVFQKGNLLEKGK 548
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLmdDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
331-551 |
2.15e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.68 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI-----RDIPYdeLLD 405
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlknREVPF--LRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 RISIVMQNVQLF-DNTIEENIRVGK--KGATKEEIIKAAKKArihdfimsLPKGYETDIGENGGI-LSGGQRQRISIARA 481
Cdd:PRK10908 80 QIGMIFQDHHLLmDRTVYDNVAIPLiiAGASGDDIRRRVSAA--------LDKVGLLDKAKNFPIqLSGGEQQRVGIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 482 FLKDAPILILDEMTSNVDpvnESLIQDAITELAK-NR---TVLVVAHHLKTIQKAD-QILVFQKGNLLEkGKHGE 551
Cdd:PRK10908 152 VVNKPAVLLADEPTGNLD---DALSEGILRLFEEfNRvgvTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
328-541 |
2.20e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 328 DNDIAFENIDFSYEKD--EFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD 405
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 RISIVMQNV--QLFDNTIEENIRVG--KKGATKEEIIKAAKKAR----IHDFIMSLPKGyetdigenggiLSGGQRQRIS 477
Cdd:PRK13650 82 KIGMVFQNPdnQFVGATVEDDVAFGleNKGIPHEEMKERVNEALelvgMQDFKEREPAR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 478 IARAFLKDAPILILDEMTSNVDPVNE-SLIQdAITELAK--NRTVLVVAHHLKTIQKADQILVFQKG 541
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRlELIK-TIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
331-562 |
2.51e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.78 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFK--MEKLSFSIAEKTMTALVGESGSGKTT-ITNLLLRFYDVHKGKITLGGTdirdipydelldrI 407
Cdd:PLN03130 615 ISIKNGYFSWDSKAERptLSNINLDVPVGSLVAIVGSTGEGKTSlISAMLGELPPRSDASVVIRGT-------------V 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFDNTIEENIRVGKK-GATKEEiiKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDA 486
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPfDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 487 PILILDEMTSNVDP-VNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKGKHGELLAKNGYYTKL 562
Cdd:PLN03130 760 DVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
350-541 |
3.21e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 79.44 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGgtdiRDIPYdelldrisiVMQNVQLFDNTIEENIRVgk 429
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE----RSIAY---------VPQQAWIMNATVRGNILF-- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 430 kgaTKEEiikaaKKARIHDFI---------MSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDP 500
Cdd:PTZ00243 744 ---FDEE-----DAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446410310 501 -VNESLIQDAITELAKNRTVLVVAHHLKTIQKADQILVFQKG 541
Cdd:PTZ00243 816 hVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDG 857
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
350-538 |
4.75e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.81 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDirdipydelldRISIVMQNVQLFDN---TIEENIR 426
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVPDSlplTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VG---KKGATKEeiIKAAKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNE 503
Cdd:NF040873 80 MGrwaRRGLWRR--LTRDDRAAVDDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 446410310 504 SLIQDAITEL-AKNRTVLVVAHHLKTIQKADQILVF 538
Cdd:NF040873 156 ERIIALLAEEhARGATVVVVTHDLELVRRADPCVLL 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-560 |
5.54e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYdelldrisivmqnvqlfdNTI----EE-- 423
Cdd:COG4152 20 VSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR------------------RRIgylpEErg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 424 ---NIRVGK--------KGATKEEIIKAAK----KARIHDfimslpkgYETD-IGEnggiLSGGQRQRISIARAFLKDAP 487
Cdd:COG4152 82 lypKMKVGEqlvylarlKGLSKAEAKRRADewleRLGLGD--------RANKkVEE----LSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAKNGYYT 560
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNT 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
331-552 |
8.91e-15 |
|
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: 73.56 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYekDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPyDELLDRISI 409
Cdd:cd03265 1 IEVENLVKKY--GDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDN-TIEENIRV-----GKKGAT-KEEIIKAAKKARIHDFIMSLPKGYetdigenggilSGGQRQRISIARAF 482
Cdd:cd03265 78 VFQDLSVDDElTGWENLYIharlyGVPGAErRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 483 LKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGEL 552
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
351-541 |
1.10e-14 |
|
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: 71.69 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIR-DIPYDELLDRISIVMQnvqlfdntieenirvgk 429
Cdd:cd03216 20 SLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAGIAMVYQ----------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 430 kgatkeeiikaakkarihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVN-ESLIqD 508
Cdd:cd03216 83 --------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEvERLF-K 123
|
170 180 190
....*....|....*....|....*....|....*
gi 446410310 509 AITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:cd03216 124 VIRRLrAQGVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
335-539 |
1.12e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 335 NIDFSYEKDEFKMeklsfsiaektmtaLVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNV 414
Cdd:PRK10247 25 NISFSLRAGEFKL--------------ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 415 QLFDNTIEEN------IRvgkkGATKEEIIKAAKKARihdfiMSLPkgyETDIGENGGILSGGQRQRISIARAFLKDAPI 488
Cdd:PRK10247 91 TLFGDTVYDNlifpwqIR----NQQPDPAIFLDDLER-----FALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446410310 489 LILDEMTSNVDPVNESLIQDAITELA--KNRTVLVVAHHLKTIQKADQILVFQ 539
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
331-555 |
1.16e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 75.50 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKL---SFSIAEKTMTALVGESGSGKTT----ItNLLLRfYDvhKGKITLGGTDIRDIPYDEL 403
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALddvSLTIEKGEIFGIIGYSGAGKSTlircI-NLLER-PT--SGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 404 LD---RISIVMQNVQLFDN-TIEENI----RVgkKGATKEEIikaakKARIH---DFImslpkgyetdigengGI----- 467
Cdd:COG1135 78 RAarrKIGMIFQHFNLLSSrTVAENValplEI--AGVPKAEI-----RKRVAellELV---------------GLsdkad 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 468 -----LSGGQRQRISIARAfLKDAP-ILILDEMTSNVDPvnesliQ--DAITELAK--NR----TVLVVAHHLKTIQK-A 532
Cdd:COG1135 136 aypsqLSGGQKQRVGIARA-LANNPkVLLCDEATSALDP------EttRSILDLLKdiNRelglTIVLITHEMDVVRRiC 208
|
250 260
....*....|....*....|...
gi 446410310 533 DQILVFQKGNLLEKGKHGELLAK 555
Cdd:COG1135 209 DRVAVLENGRIVEQGPVLDVFAN 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
331-547 |
1.23e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.15 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELldrISIV 410
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQL---FDNTIEENIRVGKKG---------ATKEEIIKAAKkARIhdfimSLPKGYETDIGEnggiLSGGQRQRISI 478
Cdd:PRK15056 84 PQSEEVdwsFPVLVEDVVMMGRYGhmgwlrrakKRDRQIVTAAL-ARV-----DMVEFRHRQIGE----LSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQKADQILVFQKGNLLEKG 547
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
331-553 |
1.35e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 73.59 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRIS-- 408
Cdd:PRK09493 2 IEFKNVSKHFGPTQV-LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFDN-TIEENIRVGK---KGATKEEIIKAAKKArihdfimsLPK-GYETDIGENGGILSGGQRQRISIARAfL 483
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGPlrvRGASKEEAEKQAREL--------LAKvGLAERAHHYPSELSGGQQQRVAIARA-L 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 484 KDAPILIL-DEMTSNVDPV--NESL--IQDAITElakNRTVLVVAHHLKTIQKADQILVF-QKGNLLEKGKHGELL 553
Cdd:PRK09493 152 AVKPKLMLfDEPTSALDPElrHEVLkvMQDLAEE---GMTMVIVTHEIGFAEKVASRLIFiDKGRIAEDGDPQVLI 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
331-553 |
1.71e-14 |
|
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: 73.58 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSY-EKDEFKmeKLSFSIAEKTMTALVGESGSGKTTITNLLLRfyDVHK---------GKiTLGGTDIRDI-P 399
Cdd:COG1119 4 LELRNVTVRRgGKTILD--DISWTVKPGEHWAILGPNGAGKSTLLSLITG--DLPPtygndvrlfGE-RRGGEDVWELrK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 400 ydelldRISIVMQNVQLF---DNTIEENIRVGK-------KGATKEEIIKAakKARIHDFimslpkGYETDIGENGGILS 469
Cdd:COG1119 79 ------RIGLVSPALQLRfprDETVLDVVLSGFfdsiglyREPTDEQRERA--RELLELL------GLAHLADRPFGTLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 470 GGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN--RTVLVVAHHLKTIQKA-DQILVFQKGNLLEK 546
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
....*..
gi 446410310 547 GKHGELL 553
Cdd:COG1119 225 GPKEEVL 231
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
44-291 |
1.86e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 74.11 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 44 QIFDGTSLASLYKYFIAIGLLV-VFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDV 122
Cdd:cd18778 28 LVTIGSKSLGLLLGLALLLLGAyLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 123 DNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVR 202
Cdd:cd18778 108 ANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 203 GIPVLKSFSNNKsldnelmNKTKKFGETSKAASR--FKAKQL-SIF----GFLLDIGYLVLLIAGAILVIKGNLDVLNFI 275
Cdd:cd18778 188 GIREIQAFGREE-------EEAKRFEALSRRYRKaqLRAMKLwAIFhplmEFLTSLGTVLVLGFGGRLVLAGELTIGDLV 260
|
250
....*....|....*.
gi 446410310 276 IFAVISKEFYKPFASM 291
Cdd:cd18778 261 AFLLYLGLFYEPITSL 276
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
344-493 |
1.96e-14 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 75.26 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 344 EFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPydELLDRISIVMQNVQLFDN-TIE 422
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP--PYQRPINMMFQSYALFPHmTVE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 423 ENIRVGKKgatKEEIIKAAKKARIHDfIMSLPKGYETdIGENGGILSGGQRQRISIARAFLKDAPILILDE 493
Cdd:PRK11607 110 QNIAFGLK---QDKLPKAEIASRVNE-MLGLVHMQEF-AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
331-549 |
2.20e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEfKMEKLSFSIAEKTMTALVGESGSGKTTitnlLLRFYDV----HKGKITLGG--------TDIRDI 398
Cdd:PRK11124 3 IQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSS----LLRVLNLlempRSGTLNIAGnhfdfsktPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 399 pyDELLDRISIVMQNVQLF------DNTIEENIRVgkKGATKEEIIKAAKKA----RIHDFIMSLPKGyetdigenggiL 468
Cdd:PRK11124 78 --RELRRNVGMVFQQYNLWphltvqQNLIEAPCRV--LGLSKDQALARAEKLlerlRLKPYADRFPLH-----------L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 469 SGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR-TVLVVAHHLKTIQK-ADQILVFQKGNLLEK 546
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
...
gi 446410310 547 GKH 549
Cdd:PRK11124 223 GDA 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
302-554 |
2.85e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.61 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 302 VDSYERLSR--------------ILYADVIPDKVNGIVPK-DNDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGES 366
Cdd:COG4178 319 VDNYQSLAEwratvdrlagfeeaLEAADALPEAASRIETSeDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 367 GSGKTTitnlLLR-------FYDvhkGKITL-GGTDI-----RdiPY------DELLdrisivmqnvqLFDNTIEEnirv 427
Cdd:COG4178 399 GSGKST----LLRaiaglwpYGS---GRIARpAGARVlflpqR--PYlplgtlREAL-----------LYPATAEA---- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 gkkgATKEEIIKAAKKARIHDFIMSLpkgyetDIGEN-GGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:COG4178 455 ----FSDAELREALEAVGLGHLAERL------DEEADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446410310 507 QDAITELAKNRTVLVVAHHLKTIQKADQILVfqkgnlLEKGKHGELLA 554
Cdd:COG4178 525 YQLLREELPGTTVISVGHRSTLAAFHDRVLE------LTGDGSWQLLP 566
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
80-291 |
2.86e-14 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 73.61 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 80 HSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDV----DNMSLVVGHMWSRMFGDFLIGAVVFVGlasiDF 155
Cdd:cd18554 71 QWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVeqtkDFITTGLMNIWLDMITIIIAICIMLVL----NP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 156 KLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAAS 235
Cdd:cd18554 147 KLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHT 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 236 RFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASM 291
Cdd:cd18554 227 RWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRL 282
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
334-544 |
3.03e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYEKDEFKMEKL---SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDEL--LDR-- 406
Cdd:PRK10535 8 KDIRRSYPSGEEQVEVLkgiSLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqLRReh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 ISIVMQNVQLFDN-TIEENIRVGKKGATKEeiiKAAKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKD 485
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 486 APILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQKADQILVFQKGNLL 544
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
351-538 |
4.36e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNVQLFDN-TIEENIRVG 428
Cdd:COG1129 24 SLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENIFLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 429 ----KKGAT-KEEIIKAAKK--ARIhdfimslpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPV 501
Cdd:COG1129 104 reprRGGLIdWRAMRRRAREllARL---------GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTER 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446410310 502 N-ESLIqDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVF 538
Cdd:COG1129 175 EvERLF-RIIRRLkAQGVAIIYISHRLDEVFEiADRVTVL 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
347-541 |
5.56e-14 |
|
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: 71.31 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITL----GGTDIRDIPYDELL----DRISIVMQnvqlFD 418
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREILalrrRTIGYVSQ----FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 419 NTIEeniRVG----------KKGATKEEiikAAKKAR-------IHDFIMSLPKGyeTdigenggiLSGGQRQRISIARA 481
Cdd:COG4778 103 RVIP---RVSaldvvaepllERGVDREE---ARARARellarlnLPERLWDLPPA--T--------FSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 482 FLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
350-554 |
6.52e-14 |
|
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: 74.34 E-value: 6.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKT----TITNLLLRFYDVHKGKITLGGTDIRDIPYDELL----DRISIVMQ------N-V 414
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQepmtslNpL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 415 QlfdnTIE----ENIRVgKKGATKEEI------------IKAAKKaRIHDFimslPkgYEtdigenggiLSGGQRQRISI 478
Cdd:COG4172 109 H----TIGkqiaEVLRL-HRGLSGAAAraralellervgIPDPER-RLDAY----P--HQ---------LSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPVneslIQDAITELAK------NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGE 551
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDVT----VQAQILDLLKdlqrelGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAE 243
|
...
gi 446410310 552 LLA 554
Cdd:COG4172 244 LFA 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
327-547 |
6.56e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 72.43 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 327 KDNDIAFENIDFSYEKDEFKMEKL-----SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYD 401
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEKLalddvNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 402 -ELLDRISIVMQNV--QLFDNTIEENIRVGKK--GATKEEIIK----AAKKARIHDFIMSLPKgyetdigenggILSGGQ 472
Cdd:PRK13633 81 wDIRNKAGMVFQNPdnQIVATIVEEDVAFGPEnlGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 473 RQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQKADQILVFQKGNLLEKG 547
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-527 |
6.66e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.04 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQL---FDNTIEENI- 425
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEENLa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 ----RVGKKGATKEeiIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDP- 500
Cdd:COG1101 105 layrRGKRRGLRRG--LTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPk 182
|
170 180 190
....*....|....*....|....*....|.
gi 446410310 501 ----VNEsLIQDAITElaKNRTVLVVAHHLK 527
Cdd:COG1101 183 taalVLE-LTEKIVEE--NNLTTLMVTHNME 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
354-552 |
1.10e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.75 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 354 IAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDElldR-ISIVMQNVQLFDN-TIEENIRVGKK- 430
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RgVGMVFQSYALYPHlSVAENMSFGLKl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 431 -GATKEEIIK----AAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESL 505
Cdd:PRK11000 103 aGAKKEEINQrvnqVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446410310 506 IQDAITELAK--NRTVLVVAH-HLKTIQKADQILVFQKGNLLEKGKHGEL 552
Cdd:PRK11000 172 MRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-547 |
1.24e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.59 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDvHKGKITLGGTDIRDIPYDELL---DRISIVMQ----------N 413
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQdpnsslnprlN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 414 VQlfdNTIEENIRVGKKGATKEEiikaaKKARIHDFIMSL---PKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILI 490
Cdd:PRK15134 381 VL---QIIEEGLRVHQPTLSAAQ-----REQQVIAVMEEVgldPETRHRYPAE----FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 491 LDEMTSNVDpvneSLIQDAITELAKNR------TVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:PRK15134 449 LDEPTSSLD----KTVQAQILALLKSLqqkhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
331-553 |
1.39e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.88 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:COG4604 2 IEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQnvqlfDNTIEENIRV-------------GKKGATKEEIIKAAkkarIHDF-IMSLPKGYetdIGEnggiLSGGQRQRI 476
Cdd:COG4604 81 RQ-----ENHINSRLTVrelvafgrfpyskGRLTAEDREIIDEA----IAYLdLEDLADRY---LDE----LSGGQRQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELA--KNRTVLVVAHHLK-TIQKADQILVFQKGNLLEKGKHGELL 553
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTPEEII 224
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
360-526 |
1.60e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.30 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 360 TALVGESGSGKTTITNLLlrfydvhKGKIT--LGGTDiRDIPYDELLDRIS-IVMQNvqLFDNTIEENIRVGKK------ 430
Cdd:PRK13409 102 TGILGPNGIGKTTAVKIL-------SGELIpnLGDYE-EEPSWDEVLKRFRgTELQN--YFKKLYNGEIKVVHKpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 431 ------GATKEEIIKAAKKARIHDFI--MSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDpVN 502
Cdd:PRK13409 172 ipkvfkGKVRELLKKVDERGKLDEVVerLGLENILDRDISE----LSGGELQRVAIAAALLRDADFYFFDEPTSYLD-IR 246
|
170 180
....*....|....*....|....*
gi 446410310 503 ESL-IQDAITELAKNRTVLVVAHHL 526
Cdd:PRK13409 247 QRLnVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
331-556 |
1.66e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQLFDNTIeenirvGKKGATKE--------EIIKAAKKARIHDFIMSLPKgyetdigenggiLSGGQRQRISIARAF 482
Cdd:PRK10522 403 FTDFHLFDQLL------GPEGKPANpalvekwlERLKMAHKLELEDGRISNLK------------LSKGQKKRLALLLAL 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 483 LKDAPILILDEMTSNVDPV-NESLIQDAITEL-AKNRTVLVVAHHLKTIQKADQILVFQKGNLLE-KGKHGELLAKN 556
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHfRREFYQVLLPLLqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-277 |
1.84e-13 |
|
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: 70.92 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 27 YGLSSIAMIV-IVFSILF---------QIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMII 96
Cdd:cd18542 1 YLLAILALLLaTALNLLIpllirriidSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 97 KLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTI 176
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 177 KQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVL 256
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260
....*....|....*....|.
gi 446410310 257 LIAGAILVIKGNLDVLNFIIF 277
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAF 261
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
336-554 |
2.27e-13 |
|
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: 71.67 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 336 IDFSYEKDEFKMEkLSFSIAEKTMTALVGESGSGKTTITNL---LLRfydVHKGKITLGGTDirdipydeLLD------- 405
Cdd:COG4148 5 VDFRLRRGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEV--------LQDsargifl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 -----RISIVMQNVQLFDN-TIEENIRVGKKGATKeeiikAAKKARIHDFIMSLpkgyetdigengGI----------LS 469
Cdd:COG4148 73 pphrrRIGYVFQEARLFPHlSVRGNLLYGRKRAPR-----AERRISFDEVVELL------------GIghlldrrpatLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 470 GGQRQRISIARAFLKDAPILILDEMTSNVD--------PVNESLIQDAitelakNRTVLVVAHHLKTIQK-ADQILVFQK 540
Cdd:COG4148 136 GGERQRVAIGRALLSSPRLLLMDEPLAALDlarkaeilPYLERLRDEL------DIPILYVSHSLDEVARlADHVVLLEQ 209
|
250
....*....|....
gi 446410310 541 GNLLEKGKHGELLA 554
Cdd:COG4148 210 GRVVASGPLAEVLS 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
347-547 |
2.75e-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: 69.67 E-value: 2.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTdirdIPYD---ELLDRISIVM-QNVQL-FDNTI 421
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKrrkKFLRRIGVVFgQKTQLwWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 422 EENIRVGKKgatKEEIIKAAKKARIHDFIMSLPKGYETDIGENGgiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPV 501
Cdd:cd03267 113 IDSFYLLAA---IYDLPPARFKKRLDELSELLDLEELLDTPVRQ--LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446410310 502 NESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03267 188 AQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
351-548 |
3.23e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 3.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPyDELLDRISIV--MQNVQLFDN-TIEENIRV 427
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVrtFQHVRLFREmTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GK---------KGATKEEIIKAAKKARIHDFIMSLPKGYETDIG-ENGGILSGGQRQRISIARAFLKDAPILILDEMTSN 497
Cdd:PRK11300 104 AQhqqlktglfSGLLKTPAFRRAESEALDRAATWLERVGLLEHAnRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446410310 498 VDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGK 548
Cdd:PRK11300 184 LNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGT 237
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
22-278 |
3.90e-13 |
|
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: 69.90 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 22 VFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKF 101
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 102 SLGFYTNERLGEINTILHKDVDNM-SLVVGHMwSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSE 180
Cdd:cd18557 83 EIAFFDKHKTGELTSRLSSDTSVLqSAVTDNL-SQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 181 KIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSldnelmnKTKKFGE---TSKAASRFKAKQLSIF----GFLLDIGY 253
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEK-------EIRRYSEaldRSYRLARKKALANALFqgitSLLIYLSL 234
|
250 260
....*....|....*....|....*...
gi 446410310 254 LVLLIAGAILVIKGNL---DVLNFIIFA 278
Cdd:cd18557 235 LLVLWYGGYLVLSGQLtvgELTSFILYT 262
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
350-524 |
4.35e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 4.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISivMQNVqLFDN-TIEENIRV- 427
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNA-MKPAlTVAENLEFw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 -GKKGATKEEIIKAAKKARIHDfIMSLPKGYetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:PRK13539 98 aAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALF 166
|
170
....*....|....*....
gi 446410310 507 QDAITE-LAKNRTVLVVAH 524
Cdd:PRK13539 167 AELIRAhLAQGGIVIAATH 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
348-553 |
4.45e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 69.63 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVQL-FDNTIEENIR 426
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGK----------KGATKEEIIKAAKKARIHDFImslpkgyetdiGENGGILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:PRK10253 104 RGRyphqplftrwRKEDEEAVTKAMQATGITHLA-----------DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 497 NVDPVNESLIQDAITELAKNR--TVLVVAHHL-KTIQKADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
14-269 |
5.33e-13 |
|
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: 69.78 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 14 KRDLIISSVFFALYGLSSIAMivivfSILFQ-IFD----GTSLASLYKYFIAIGLLVVFKGICNMVAD--MKKHSAGFDI 86
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAG-----SFFFQiLIDdiipSGDINLLNIISIGLILLYLFQSLLSYIRSylLLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 87 vqQIRERMIIKLKKFSLGFYTNERLGEINTILHkDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVP 166
Cdd:cd18570 76 --RLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 167 IALIFLYLTIKQSEKI--ENQNNSALLDmvSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSI 244
Cdd:cd18570 153 LYILIILLFNKPFKKKnrEVMESNAELN--SYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSI 230
|
250 260
....*....|....*....|....*
gi 446410310 245 FGFLLDIGYLVLLIAGAILVIKGNL 269
Cdd:cd18570 231 KGLISLIGSLLILWIGSYLVIKGQL 255
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
351-541 |
7.08e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGG--TDIRDiPYDELLDRISIVMQNVQLFDN-TIEENIRV 427
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRS-PRDAIALGIGMVHQHFMLVPNlTVAENIVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 G---------KKGATKEEIIKAAKK--------ARIHDfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILI 490
Cdd:COG3845 104 GleptkggrlDRKAARARIRELSERygldvdpdAKVED-------------------LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 491 LDEMTSNVDP--VnESLIqDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:COG3845 165 LDEPTAVLTPqeA-DELF-EILRRLAAEgKSIIFITHKLREVMAiADRVTVLRRG 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
331-499 |
7.39e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.36 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDellDR-ISI 409
Cdd:PRK09452 15 VELRGISKSFDGKEV-ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRhVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDN-TIEENIRVG--KKGATKEEI----IKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARAF 482
Cdd:PRK09452 91 VFQSYALFPHmTVFENVAFGlrMQKTPAAEItprvMEALRMVQLEEFAQRKPHQ-----------LSGGQQQRVAIARAV 159
|
170
....*....|....*..
gi 446410310 483 LKDAPILILDEMTSNVD 499
Cdd:PRK09452 160 VNKPKVLLLDESLSALD 176
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-553 |
9.34e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 9.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTitnlLLRFYD----VHKGKITLGGTDIRDIPYDELLDRISIVMQNVQL-FDNTIEEN 424
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTT----LLRAINgtltPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 425 IRVGKK-------GATK------EEIIKAAKKARIHDfimslpkgyeTDIGEnggiLSGGQRQRISIARAFLKDAPILIL 491
Cdd:PRK09536 98 VEMGRTphrsrfdTWTEtdraavERAMERTGVAQFAD----------RPVTS----LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 492 DEMTSNVDpVNESL-IQDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK09536 164 DEPTASLD-INHQVrTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
347-543 |
1.37e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 67.53 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYD---ELLDR-ISIVMQNVQLF-DNTI 421
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQFHHLLpDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 422 EENIR----VGKKgATKEeiikAAKKARIhdfiMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSN 497
Cdd:PRK11629 105 LENVAmpllIGKK-KPAE----INSRALE----MLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446410310 498 VDPVNESLIQDAITEL--AKNRTVLVVAHHLKTIQKADQILVFQKGNL 543
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
331-547 |
1.65e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.22 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSI----AEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD- 405
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASRALFDIdlevKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 ---RISIVMQ--NVQLFDNTIEENIRVGKK--GATKEEIIK-AAKKARIhdfimslpKGYETDIGENGGI-LSGGQRQRI 476
Cdd:PRK13643 82 vrkKVGVVFQfpESQLFEETVLKDVAFGPQnfGIPKEKAEKiAAEKLEM--------VGLADEFWEKSPFeLSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
335-547 |
2.83e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 335 NIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI--RDIPYDELLDRISIVM 411
Cdd:PRK10261 19 NIAFMQEQQKIAaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 QNVQLFD-------------------NTIEENIRVgKKGATKEEIIKAAKkaRIHDFImSLPKGyETDIGENGGILSGGQ 472
Cdd:PRK10261 99 RHVRGADmamifqepmtslnpvftvgEQIAESIRL-HQGASREEAMVEAK--RMLDQV-RIPEA-QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 473 RQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRT--VLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
347-541 |
2.93e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDirdipYDELLDR------ISIVMQNVQLFDN- 419
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNIN-----YNKLDHKlaaqlgIGIIYQELSVIDEl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 420 TIEENIRVGKKGATKEEIIKAA--KKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSN 497
Cdd:PRK09700 96 TVLENLYIGRHLTKKVCGVNIIdwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446410310 498 VDPVNESLIQDAITELAKNRTVLV-VAHHLKTIQK-ADQILVFQKG 541
Cdd:PRK09700 176 LTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
347-554 |
4.09e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIrdipydELLDR--ISIVMQNVQL-FDNTIEE 423
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPL------AKLNRaqRKAFRRDIQMvFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 424 -NIRvgkkgATKEEII-----------KAAKKARIHDFI--MSLPkgyETDIGENGGILSGGQRQRISIARAFLKDAPIL 489
Cdd:PRK10419 102 vNPR-----KTVREIIreplrhllsldKAERLARASEMLraVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNRTV--LVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
331-555 |
6.37e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 66.18 E-value: 6.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEkDEFKMEKLSFSIAEKTMTALVGESGSGKTTI-TNL--LLRfydVHKGKITLGGtdiRDIPYDE----- 402
Cdd:PRK13638 2 LATSDLWFRYQ-DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLsgLLR---PQKGAVLWQG---KPLDYSKrglla 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 403 LLDRISIVMQN--VQLFDNTIEENIRVGKK--GATKEEIikaakkARIHDFIMSL--PKGYETDIGEnggILSGGQRQRI 476
Cdd:PRK13638 75 LRQQVATVFQDpeQQIFYTDIDSDIAFSLRnlGVPEAEI------TRRVDEALTLvdAQHFRHQPIQ---CLSHGQKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTI-QKADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
.
gi 446410310 555 K 555
Cdd:PRK13638 226 C 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
334-558 |
7.70e-12 |
|
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: 64.47 E-value: 7.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRF--YDVHKGKITLGGTDIRDIPYDELLdRISIV 410
Cdd:cd03217 2 EIKDLHVSVGGKEiLKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERA-RLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MqnvqLFDNTIE-ENIRVGkkgatkeeiikaakkarihDFIMSLPKGyetdigenggiLSGGQRQRISIARAFLKDAPIL 489
Cdd:cd03217 81 L----AFQYPPEiPGVKNA-------------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELA-KNRTVLVVAHHLKTIQ--KADQILVFQKGNLLEKG--KHGELLAKNGY 558
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGdkELALEIEKKGY 200
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
358-553 |
8.07e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 358 TMTALVGESGSGKTTITNLLLrFYD----VHKGKITLGGTDIRDipydELLDRISIVMQNVQLF--DNTIEENIRVGKKG 431
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALA-FRSpkgvKGSGSVLLNGMPIDA----KEMRAISAYVQQDDLFipTLTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 432 ATKEEIIKAAKKARIHDFI--MSLPKGYETDIGENGGI--LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQ 507
Cdd:TIGR00955 127 RMPRRVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVV 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446410310 508 DAITELA-KNRTVLVVAHH--LKTIQKADQILVFQKGNLLEKGKHGELL 553
Cdd:TIGR00955 207 QVLKGLAqKGKTIICTIHQpsSELFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
350-554 |
9.96e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKtTITNL-LLRF-------YDvhKGKITLGGTDIRDIPYDELL----DRISIVMQNVQLF 417
Cdd:PRK15134 28 VSLQIEAGETLALVGESGSGK-SVTALsILRLlpsppvvYP--SGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 418 DN---TIEENI-------RVGKKGATKEEI--------IKAAKKaRIHDFimslPKGyetdigenggiLSGGQRQRISIA 479
Cdd:PRK15134 105 LNplhTLEKQLyevlslhRGMRREAARGEIlncldrvgIRQAAK-RLTDY----PHQ-----------LSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 480 RAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
350-493 |
1.08e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 65.27 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDiPYdelLDRiSIVMQNVQLFD--NTIEeNIRV 427
Cdd:COG4525 26 VSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PG---ADR-GVVFQKDALLPwlNVLD-NVAF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 428 GKKGATkeeIIKAAKKARIHDFI--MSLpKGYETD-IGEnggiLSGGQRQRISIARAFLKDAPILILDE 493
Cdd:COG4525 100 GLRLRG---VPKAERRARAEELLalVGL-ADFARRrIWQ----LSGGMRQRVGIARALAADPRFLLMDE 160
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
339-551 |
1.13e-11 |
|
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: 65.12 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 339 SYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKItlgGTDIRDIPYdelldrisivmqnvqlfd 418
Cdd:cd03237 7 KKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSY------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 419 ntieenirvgkkgatKEEIIKAAKKARIHDFIMSLPKG------YETDIGENGGI----------LSGGQRQRISIARAF 482
Cdd:cd03237 66 ---------------KPQYIKADYEGTVRDLLSSITKDfythpyFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 483 LKDAPILILDEMTSNVDPVNESLIQDAITELAKN--RTVLVVAHHLKTIQK-ADQILVFQKgnllEKGKHGE 551
Cdd:cd03237 131 SKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFEG----EPSVNGV 198
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
360-526 |
1.14e-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: 67.50 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 360 TALVGESGSGKTTITNLLlrfydvhKGKIT--LGGTDiRDIPYDELLDRIS-IVMQNvqLFDNTIEENIRVGKK------ 430
Cdd:COG1245 102 TGILGPNGIGKSTALKIL-------SGELKpnLGDYD-EEPSWDEVLKRFRgTELQD--YFKKLANGEIKVAHKpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 431 ------GATKEEIIKAAKKARIHDFI--MSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDpVN 502
Cdd:COG1245 172 ipkvfkGTVRELLEKVDERGKLDELAekLGLENILDRDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLD-IY 246
|
170 180
....*....|....*....|....*.
gi 446410310 503 ESL-IQDAITELAK-NRTVLVVAHHL 526
Cdd:COG1245 247 QRLnVARLIRELAEeGKYVLVVEHDL 272
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
331-543 |
1.24e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.26 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI-----RDipydellD 405
Cdd:PRK10851 3 IEIANIKKSFGRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVsrlhaRD-------R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 RISIVMQNVQLFDN-TIEENIRVGKKGATKEE-----IIKaAKKARIHDFIM--SLPKGYETDigenggiLSGGQRQRIS 477
Cdd:PRK10851 75 KVGFVFQHYALFRHmTVFDNIAFGLTVLPRRErpnaaAIK-AKVTQLLEMVQlaHLADRYPAQ-------LSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 478 IARAFLKDAPILILDEMTSNVDP-VNESL---IQDAITELaKNRTVLVVAHHLKTIQKADQILVFQKGNL 543
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAqVRKELrrwLRQLHEEL-KFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
328-555 |
1.39e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.25 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 328 DNDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTitnLLLRFYDVHK---GKITLGGtdiRDIPYD--- 401
Cdd:PRK13636 3 DYILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKST---LFQNLNGILKpssGRILFDG---KPIDYSrkg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 402 --ELLDRISIVMQNV--QLFDNTIEENIRVG--KKGATKEEIIKAAKKARIHDFIMSLpKGYETDIgenggiLSGGQRQR 475
Cdd:PRK13636 77 lmKLRESVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHL-KDKPTHC------LSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 476 ISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQ-KADQILVFQKGNLLEKGKHGEL 552
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
...
gi 446410310 553 LAK 555
Cdd:PRK13636 230 FAE 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
361-554 |
1.57e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.99 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 361 ALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIP--------YDE-----LLDRISIVMQNVQLF------DNTI 421
Cdd:PRK10619 35 SIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvADKnqlrlLRTRLTMVFQHFNLWshmtvlENVM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 422 EENIRVG--KKGATKEEIIKAAKKARIHDfimSLPKGYETDigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVD 499
Cdd:PRK10619 115 EAPIQVLglSKQEARERAVKYLAKVGIDE---RAQGKYPVH-------LSGGQQQRVSIARALAMEPEVLLFDEPTSALD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 500 P--VNESL-IQDAITELAKnrTVLVVAHHLKTIQKADQILVF-QKGNLLEKGKHGELLA 554
Cdd:PRK10619 185 PelVGEVLrIMQQLAEEGK--TMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLFG 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
345-524 |
1.62e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.90 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 345 FKMEKLSFSIAEKTMT-------------ALVGESGSGKTTITNLLLRFYDVHKGKITLGgTDIrDIPY-D---ELLDRi 407
Cdd:PRK11147 320 FEMENVNYQIDGKQLVkdfsaqvqrgdkiALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-TKL-EVAYfDqhrAELDP- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 sivmqnvqlfDNTIEENIRVGKKgatkeEIIKAAKKARI----HDFIMSlPKGYETDIGEnggiLSGGQRQRISIARAFL 483
Cdd:PRK11147 397 ----------EKTVMDNLAEGKQ-----EVMVNGRPRHVlgylQDFLFH-PKRAMTPVKA----LSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446410310 484 KDAPILILDEMTSNVDPVNESLIQDAITELAKnrTVLVVAH 524
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
348-554 |
1.83e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 64.86 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNVqlfDNTIEENIRV 427
Cdd:COG4167 30 KPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 428 GK------KGATKEEIikAAKKARIHDFIMS---LPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNV 498
Cdd:COG4167 107 GQileeplRLNTDLTA--EEREERIFATLRLvglLPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 499 DPVNESLIQDAITELAKNRTV--LVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:COG4167 181 DMSVRSQIINLMLELQEKLGIsyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
360-548 |
2.57e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 65.28 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 360 TALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD----RISIVMQNVQLFDN-TIEENIRVGKKGATK 434
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPpekrRIGYVFQDARLFPHyKVRGNLRYGMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 435 EEIikaakkarihDFIMSLpKGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVD-PVNESLIqDAITEL 513
Cdd:PRK11144 107 AQF----------DKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELL-PYLERL 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 446410310 514 AK--NRTVLVVAHHLKTIQK-ADQILVfqkgnlLEKGK 548
Cdd:PRK11144 175 AReiNIPILYVSHSLDEILRlADRVVV------LEQGK 206
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
348-561 |
3.93e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.54 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKT----TITNLLLRFYDVHKGKITLGGTDIRDIPYDE---LLDR-ISIVMQN------ 413
Cdd:COG4170 24 DRVSLTLNEGEIRGLVGESGSGKSliakAICGITKDNWHVTADRFRWNGIDLLKLSPRErrkIIGReIAMIFQEpsscld 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 414 --VQLFDNtIEENIRVG--------KKGATKEEIIKAAKKARI--HDFIM-SLPkgYEtdigenggiLSGGQRQRISIAR 480
Cdd:COG4170 104 psAKIGDQ-LIEAIPSWtfkgkwwqRFKWRKKRAIELLHRVGIkdHKDIMnSYP--HE---------LTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 481 AFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTI-QKADQILVFQKGNLLEKGKHGELLAKNG 557
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILKSPH 251
|
....*
gi 446410310 558 Y-YTK 561
Cdd:COG4170 252 HpYTK 256
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
331-555 |
3.96e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.05 E-value: 3.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIV 410
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNV--QLFDNTIEENIRVG------KKGATKEEIIKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARAF 482
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 483 LKDAPILILDEMTSNVDPVNESLIQDAITELAKN--RTVLVVAHHLKTI-QKADQILVFQKGNLLEKGKHGELLAK 555
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
347-524 |
4.84e-11 |
|
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: 62.87 E-value: 4.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELldrisIVMQNVQLFD-NTIEENI 425
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RVGKKgATKEEIIKAAKKARIHDFI--MSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNE 503
Cdd:TIGR01184 76 ALAVD-RVLPDLSKSERRAIVEEHIalVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 446410310 504 SLIQDAITELAKNR--TVLVVAH 524
Cdd:TIGR01184 151 GNLQEELMQIWEEHrvTVLMVTH 173
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
347-547 |
5.22e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.49 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHK---GKITLGGTDI-------RDIPYDELldRISIVMQNVQL 416
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVqregrlaRDIRKSRA--NTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 FDN-TIEENIRVGKKGAT--------------KEEIIKAAKKARIHDFIMslpkgyetdigENGGILSGGQRQRISIARA 481
Cdd:PRK09984 98 VNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFAH-----------QRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 482 FLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLK-TIQKADQILVFQKGNLLEKG 547
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
347-547 |
6.57e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 6.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDEL--LDR-ISIVMQNV-------QL 416
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqaLRRdIQFIFQDPyasldprQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 FDNTIEENIRVGKKGATKEeiiKAAKKARIHDFIMSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKA---AAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVS 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446410310 497 NVDPVNESLIQDAITELAKNRTV--LVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:PRK10261 493 ALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
350-554 |
7.93e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKT-TITNLL------LRfydVHKGKITLGGTDIrdIPYDELLDRISIVMQNVQ------- 415
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSlTCAAALgilpagVR---QTAGRVLLDGKPV--APCALRGRKIATIMQNPRsafnplh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 416 -LFDNTIEENIRVGKKG--ATKEEIIKA------AKKARIHDFIMSlpkgyetdigenggilsGGQRQRISIARAFLKDA 486
Cdd:PRK10418 97 tMHTHARETCLALGKPAddATLTAALEAvglenaARVLKLYPFEMS-----------------GGMLQRMMIALALLCEA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 487 PILILDEMTSNVDPVNESLIQDAITELAKNRT--VLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK10418 160 PFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
32-277 |
1.14e-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: 62.81 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 32 IAMIVIVFSILFQIF--------------DGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIK 97
Cdd:cd18541 3 LGILFLILVDLLQLLipriigraidaltaGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 98 LKKFSLGFYTNERLGEINTILHKDVDNMSLVVGH--MwsrMFGD-FLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYL 174
Cdd:cd18541 83 LLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPgiL---YLVDaLFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 175 TIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYL 254
Cdd:cd18541 160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
|
250 260
....*....|....*....|...
gi 446410310 255 VLLIAGAILVIKGNLDVLNFIIF 277
Cdd:cd18541 240 IVLWYGGRLVIRGTITLGDLVAF 262
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
351-555 |
1.22e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.06 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSI-AEKTMtALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR---ISIVMQN--VQLfdntieeN 424
Cdd:PRK11308 35 SFTLeRGKTL-AVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQNpyGSL-------N 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 425 IRvgKK-GATKEE--II-----KAAKKARIHDfIMSL----PKGYetdiGENGGILSGGQRQRISIARAFLKDAPILILD 492
Cdd:PRK11308 107 PR--KKvGQILEEplLIntslsAAERREKALA-MMAKvglrPEHY----DRYPHMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 493 EMTSNVD------PVNesLIQDAITELakNRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAK 555
Cdd:PRK11308 180 EPVSALDvsvqaqVLN--LMMDLQQEL--GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
334-554 |
1.26e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.83 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYeKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDE-------LLDR 406
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArarrgigYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 ISIVMQNVQLFDN-----TIEENIRVGKKGATKEEIIKAAKKARIHDFImslpkgyetdigenGGILSGGQRQRISIARA 481
Cdd:PRK10895 86 EASIFRRLSVYDNlmavlQIRDDLSAEQREDRANELMEEFHIEHLRDSM--------------GQSLSGGERRRVEIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 482 FLKDAPILILDEMTSNVDPVNESLIQDAITELAKNRT-VLVVAHHLK-TIQKADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLgVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
351-541 |
1.33e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNVQLF-DNTIEENIRVG 428
Cdd:PRK11288 24 SFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgVAIIYQELHLVpEMTVAENLYLG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 429 KKGATKEEIIKAAKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSnvdpvneSLIQD 508
Cdd:PRK11288 104 QLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTS-------SLSAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446410310 509 AITEL--------AKNRTVLVVAHHLKTI-QKADQILVFQKG 541
Cdd:PRK11288 175 EIEQLfrvirelrAEGRVILYVSHRMEEIfALCDAITVFKDG 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
350-543 |
1.96e-10 |
|
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: 60.14 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMqnvqlfdntiEENIRVG 428
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP----------EDRKREG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 429 kkgatkeeiikaakkarihdFIMSLPkgyetdIGEN---GGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESL 505
Cdd:cd03215 89 --------------------LVLDLS------VAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446410310 506 IQDAITELA-KNRTVLVVAHHLKTI-QKADQILVFQKGNL 543
Cdd:cd03215 143 IYRLIRELAdAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
331-541 |
2.10e-10 |
|
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: 59.00 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDirdipydelldRISIV 410
Cdd:cd03221 1 IELENLSKTYGGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQnvqlfdntieenirvgkkgatkeeiikaakkarihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILI 490
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446410310 491 LDEMTSNVDPVNESLIQDAITELakNRTVLVVAH---HLKTIqkADQILVFQKG 541
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEY--PGTVILVSHdryFLDQV--ATKIIELEDG 143
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
331-545 |
2.52e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 62.77 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEkDEFKMEKLSFSIA--EKTmtALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDirdipydelldRIS 408
Cdd:COG0488 316 LELEGLSKSYG-DKTLLDDLSLRIDrgDRI--GLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETV-----------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQLFD--NTIEENIRVGKKGATKEEIIKAAKK-----ARIHDFImslpkgyetdigengGILSGGQRQRISIARA 481
Cdd:COG0488 382 YFDQHQEELDpdKTVLDELRDGAPGGTEQEVRGYLGRflfsgDDAFKPV---------------GVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 482 FLKDAPILILDEMTSNVDPvnESLiqDAITELAKN--RTVLVVAH--HLktIQK-ADQILVFQKGNLLE 545
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDI--ETL--EALEEALDDfpGTVLLVSHdrYF--LDRvATRILEFEDGGVRE 509
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
334-525 |
2.53e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 334 ENIDFSYEKDEFKMEK-LSFSIAEKTMTALVGESGSGKTTITNLLLRfydVHKGKITLGGTDIRDIPYDelldrisivmQ 412
Cdd:COG2401 32 EAFGVELRVVERYVLRdLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGCVDVPDNQFG----------R 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 413 NVQLFDNtieenirVGKKGATKE--EIIKAAKkarIHDFIMSLPKGYEtdigenggiLSGGQRQRISIARAFLKDAPILI 490
Cdd:COG2401 99 EASLIDA-------IGRKGDFKDavELLNAVG---LSDAVLWLRRFKE---------LSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 446410310 491 LDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHH 525
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHH 196
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
350-554 |
2.99e-10 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.96 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVMQNV-----------QLFD 418
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrisQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 419 NTIEENIRVgkKGATKEEIIKAAKK--ARIHDFIMSLPKgyetdigenggILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:PRK15112 112 FPLRLNTDL--EPEQREKQIIETLRqvGLLPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 497 NVDPVNESLIQDAITELAKNRTV--LVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
331-499 |
3.60e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 61.78 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTitnlLLRFY----DVHKGKITLGGTDIRDIpydELLDR 406
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVagleRITSGEIWIGGRVVNEL---EPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 -ISIVMQNVQLFDN-TIEENIRVGKK--GATKEEI----IKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISI 478
Cdd:PRK11650 77 dIAMVFQNYALYPHmSVRENMAYGLKirGMPKAEIeervAEAARILELEPLLDRKPRE-----------LSGGQRQRVAM 145
|
170 180
....*....|....*....|.
gi 446410310 479 ARAFLKDAPILILDEMTSNVD 499
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLD 166
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
331-555 |
3.72e-10 |
|
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: 62.51 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLL--LRFYDVHKGKI-------------------- 388
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV-LKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 389 ----TLGGT---------DIRDIPYDELLDRISIVMQ-------NVQLFDNTIEENIRVGKKGatKEEIIKAA---KKAR 445
Cdd:TIGR03269 80 epcpVCGGTlepeevdfwNLSDKLRRRIRKRIAIMLQrtfalygDDTVLDNVLEALEEIGYEG--KEAVGRAVdliEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 446 IHDFIMSLPKGyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVA 523
Cdd:TIGR03269 158 LSHRITHIARD-----------LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTS 226
|
250 260 270
....*....|....*....|....*....|...
gi 446410310 524 HHLKTIQK-ADQILVFQKGNLLEKGKHGELLAK 555
Cdd:TIGR03269 227 HWPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
337-525 |
3.77e-10 |
|
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: 59.68 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 337 DFSYEKDEFKM-EKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI---RDIPYDELL-------- 404
Cdd:TIGR01189 5 NLACSRGERMLfEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILylghlpgl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 405 -DRISiVMQNVQLF-------DNTIEENI-RVGKKGATKeeiikaakkarihdfimsLPKGYetdigenggiLSGGQRQR 475
Cdd:TIGR01189 85 kPELS-ALENLHFWaaihggaQRTIEDALaAVGLTGFED------------------LPAAQ----------LSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446410310 476 ISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITE-LAKNRTVLVVAHH 525
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTHQ 186
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
52-277 |
4.45e-10 |
|
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: 60.91 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 52 ASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVgh 131
Cdd:cd18551 33 GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELI-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 132 mwSRMFGDFLIGAVVFVG----LASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVL 207
Cdd:cd18551 111 --TSGLPQLVTGVLTVVGavvlMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTV 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 208 KSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIF 277
Cdd:cd18551 189 KASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAF 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
333-524 |
6.24e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 61.62 E-value: 6.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 333 FENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGgtdiRDIpydelldRISIVMQ 412
Cdd:COG0488 1 LENLSKSFGGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGL-------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 413 NVQLFDN-TIEENI-----RVGKKGATKEEIIKA--------AKKARIHDFIMSLpKGY--ETDIGE--NG-GI------ 467
Cdd:COG0488 69 EPPLDDDlTVLDTVldgdaELRALEAELEELEAKlaepdedlERLAELQEEFEAL-GGWeaEARAEEilSGlGFpeedld 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 468 -----LSGGQRQRISIARAFLKDAPILILDEMTSNVDpvnesliQDAITELA---KNR--TVLVVAH 524
Cdd:COG0488 148 rpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEeflKNYpgTVLVVSH 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
361-550 |
7.29e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 59.69 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 361 ALVGESGSGKTTITNLLLRFYDVHKGKITLGGTdirdiPYDELLDRISIVMQNVQLFD-NTIEENIRVGKKGATKEEIIK 439
Cdd:PRK11247 42 AVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAEAREDTRLMFQDARLLPwKKVIDNVGLGLKGQWRDAALQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 440 AAKKArihdfimslpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR-- 517
Cdd:PRK11247 117 ALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgf 185
|
170 180 190
....*....|....*....|....*....|....
gi 446410310 518 TVLVVAHHL-KTIQKADQILvfqkgnLLEKGKHG 550
Cdd:PRK11247 186 TVLLVTHDVsEAVAMADRVL------LIEEGKIG 213
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
347-493 |
7.42e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDiPYDELldriSIVMQNVQLFD-NTIEENI 425
Cdd:PRK11248 17 LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER----GVVFQNEGLLPwRNVQDNV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 426 RVGKK--GATKEEIIKAAKK--ARI------HDFIMSLpkgyetdigenggilSGGQRQRISIARAFLKDAPILILDE 493
Cdd:PRK11248 92 AFGLQlaGVEKMQRLEIAHQmlKKVglegaeKRYIWQL---------------SGGQRQRVGIARALAANPQLLLLDE 154
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
350-553 |
9.50e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTitnLLLRFYDV--HKGKITLGGTDIRDIPYDEL-LDRISIVMQNVQLFdntieeNIR 426
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLlpGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPF------AMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 V-------GKKGATKEEIIKAakkarIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAP-------ILILD 492
Cdd:PRK03695 86 VfqyltlhQPDKTRTEAVASA-----LNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPdinpagqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 493 EMTSNVDPVNESLIQDAITELA-KNRTVLVVAHHL-KTIQKADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK03695 159 EPMNSLDVAQQAALDRLLSELCqQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
51-276 |
1.22e-09 |
|
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: 59.71 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 51 LASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVG 130
Cdd:cd18544 37 LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 131 HMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSF 210
Cdd:cd18544 117 SGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLF 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 211 SNNKSldnelmnKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFII 276
Cdd:cd18544 197 NREKR-------EFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAV 255
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
45-210 |
1.67e-09 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 58.96 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 45 IFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDN 124
Cdd:cd18584 27 FLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 125 M----SLVVGHMWSRMFGDFLIGAVVFvglaSIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEY 200
Cdd:cd18584 107 LdgyfARYLPQLVLAAIVPLLILVAVF----PLDWVSALILLVTAPLIPLFMILIGKAAQAASRRQWAALSRLSGHFLDR 182
|
170
....*....|
gi 446410310 201 VRGIPVLKSF 210
Cdd:cd18584 183 LRGLPTLKLF 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
350-554 |
1.74e-09 |
|
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: 60.20 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKI-TLGGTDIRDIPYDELLDR------ISIVMQNVQLFDN-TI 421
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPGPDGRgrakryIGILHQEYDLYPHrTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 422 EENIrvgKKGATKEEIIKAAKKARIHDFIMSlpkGYETDIGEN-----GGILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:TIGR03269 383 LDNL---TEAIGLELPDELARMKAVITLKMV---GFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 497 NVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLA 554
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
34-307 |
2.31e-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: 58.68 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 34 MIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGE 113
Cdd:cd18563 22 TKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 114 INTILHKDVDNM-SLVVGHmwsrmFGDFLIGAVVFVGLA----SIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNS 188
Cdd:cd18563 102 LMSRVTSDTDRLqDFLSDG-----LPDFLTNILMIIGIGvvlfSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 189 ALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGN 268
Cdd:cd18563 177 RWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGT 256
|
250 260 270
....*....|....*....|....*....|....*....
gi 446410310 269 LDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYER 307
Cdd:cd18563 257 MTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
361-541 |
2.36e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 361 ALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIR-DIPYDELLDRISIVMQNVQLFDN-TIEENIRVGKKGATKEEII 438
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAENIFLGREFVNRFGRI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 439 KAAKKARIHDFI---MSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNV-DPVNESLIQdAITEL- 513
Cdd:PRK10762 114 DWKKMYAEADKLlarLNLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLFR-VIRELk 188
|
170 180
....*....|....*....|....*....
gi 446410310 514 AKNRTVLVVAHHLKTI-QKADQILVFQKG 541
Cdd:PRK10762 189 SQGRGIVYISHRLKEIfEICDDVTVFRDG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
331-555 |
3.36e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 58.66 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFKMEKL---SFSIAEKTMTALVGESGSGKTT---ITNLLLRfydVHKGKITLGGTDIRDIPYDEL- 403
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALnnvSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 404 LDRISIVM--QNVQLFDN-TIEENIRVGKK--GATKEEIikaakKARIHDFImslpkgyetdigENGGI----------L 468
Cdd:PRK11153 79 KARRQIGMifQHFNLLSSrTVFDNVALPLElaGTPKAEI-----KARVTELL------------ELVGLsdkadrypaqL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 469 SGGQRQRISIARAFLKDAPILILDEMTSNVDPVNesliQDAITELAK--NR----TVLVVAHHLKTI-QKADQILVFQKG 541
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDPAT----TRSILELLKdiNRelglTIVLITHEMDVVkRICDRVAVIDAG 217
|
250
....*....|....
gi 446410310 542 NLLEKGKHGELLAK 555
Cdd:PRK11153 218 RLVEQGTVSEVFSH 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
331-536 |
4.72e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEFkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKItlggtdIRDIPYdelldRISIV 410
Cdd:PRK09544 5 VSLENVSVSFGQRRV-LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKL-----RIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 411 MQNVQL---FDNTIEENIRVgKKGATKEEIIKAAKK---ARIHDFIMSLpkgyetdigenggiLSGGQRQRISIARAFLK 484
Cdd:PRK09544 73 PQKLYLdttLPLTVNRFLRL-RPGTKKEDILPALKRvqaGHLIDAPMQK--------------LSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 485 DAPILILDEMTSNVDpVNESL-IQDAITELAK--NRTVLVVAHHLKTIQ-KADQIL 536
Cdd:PRK09544 138 RPQLLVLDEPTQGVD-VNGQVaLYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVL 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
467-540 |
5.68e-09 |
|
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: 55.62 E-value: 5.68e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 467 ILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNEsliqDAITELAKNR--TVLVVAHHLKTIQKADQILVFQK 540
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE----DRLYQLLKELgiTVISVGHRPSLWKFHDRVLDLDG 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
350-558 |
6.90e-09 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 56.61 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRF--YDVHKGKITLGGTDIRDIPYDElldR----ISIVMQN--------VQ 415
Cdd:COG0396 19 VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDE---RaragIFLAFQYpveipgvsVS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 416 LFDNTIEENIRvGKKGATKEEIIKAAKKARIhdfiMSLPKGYeTDIGENGGiLSGGQRQRISIARAFLKDAPILILDEMT 495
Cdd:COG0396 96 NFLRTALNARR-GEELSAREFLKLLKEKMKE----LGLDEDF-LDRYVNEG-FSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 496 SNVDPVNESLIQDAITELA-KNRTVLVVAHH---LKTIqKADQILVFQKGNLLEKGKHgEL---LAKNGY 558
Cdd:COG0396 169 SGLDIDALRIVAEGVNKLRsPDRGILIITHYqriLDYI-KPDFVHVLVDGRIVKSGGK-ELaleLEEEGY 236
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
336-552 |
7.02e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 7.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 336 IDFSYEKDEFK-MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYD----VHKGKITLGGTDIRDIPYDELLD----R 406
Cdd:PRK11022 11 VHFGDESAPFRaVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNlvgaE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 407 ISIVMQNVQLFDN-------TIEENIRV---GKKGATKEEIIKAAKKARIHDFIMSLpkgyetDIGENGgiLSGGQRQRI 476
Cdd:PRK11022 91 VAMIFQDPMTSLNpcytvgfQIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRL------DVYPHQ--LSGGMSQRV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 477 SIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTI-QKADQILVFQKGNLLEKGKHGEL 552
Cdd:PRK11022 163 MIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
17-280 |
7.43e-09 |
|
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: 57.46 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLSSIAMIvIVFSILFQIFDGTSLASLYKY--FIAIGLLVVfkGICNMVADMKKHS----AGFDIVQQI 90
Cdd:cd18578 11 LLLGLIGAIIAGAVFPVFA-ILFSKLISVFSLPDDDELRSEanFWALMFLVL--AIVAGIAYFLQGYlfgiAGERLTRRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 91 RERMIIKLKKFSLGFYTNER--LGEINTILHKDVDNMSLVVGhmwsRMFGDFLIGAV-VFVGLA---SIDFKLAIIMAVS 164
Cdd:cd18578 88 RKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVG----DRLGLILQAIVtLVAGLIiafVYGWKLALVGLAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 165 VPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFsnnkSLDNELMNKTKKFGETSKAASRFKAKQLSI 244
Cdd:cd18578 164 VPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASL----TLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 446410310 245 -FGFLLDIGYLVLLIA---GAILVIKGNLDVLNFII--FAVI 280
Cdd:cd18578 240 gFGLSQSLTFFAYALAfwyGGRLVANGEYTFEQFFIvfMALI 281
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
358-541 |
9.39e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 358 TMTALVGESGSGKTTITNLLLRFYDVhkGKITLGGTDIRDIPYDELLDRIS--IVMQNVQLFDNTIEENIRVGK-----K 430
Cdd:TIGR00956 790 TLTALMGASGAGKTTLLNVLAERVTT--GVITGGDRLVNGRPLDSSFQRSIgyVQQQDLHLPTSTVRESLRFSAylrqpK 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 431 GATKEEiikaakKARIHDFIMSL---PKGYETDIGENGGILSGGQRQRISIARAFL-KDAPILILDEMTSNVDPVNESLI 506
Cdd:TIGR00956 868 SVSKSE------KMEYVEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVaKPKLLLFLDEPTSGLDSQTAWSI 941
|
170 180 190
....*....|....*....|....*....|....*...
gi 446410310 507 QDAITELAKN-RTVLVVAHHLKTI--QKADQILVFQKG 541
Cdd:TIGR00956 942 CKLMRKLADHgQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
361-554 |
1.32e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 361 ALVGESGSGKTTITNLLLRFYDVH--KGKITLGGTDirdiPYDELLDRISIVMQNVQLFDN-TIEENI------RVgKKG 431
Cdd:PLN03211 98 AVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRK----PTKQILKRTGFVTQDDILYPHlTVRETLvfcsllRL-PKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 432 ATKEEIIKAAKKArIHDfiMSLPKGYETDIGeNGGI--LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNE-SLIQD 508
Cdd:PLN03211 173 LTKQEKILVAESV-ISE--LGLTKCENTIIG-NSFIrgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446410310 509 AITELAKNRTVLVVAHH--LKTIQKADQILVFQKGNLLEKGKHGELLA 554
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQpsSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
353-536 |
1.48e-08 |
|
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: 54.29 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 353 SIAEKTMTALVGESGSGKTTItnlllrfydvhkgkitlggtdIRDIPYdelldrisivmqnvqlfdNTIEENIRVGKKGA 432
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTI---------------------LDAIGL------------------ALGGAQSATRRRSG 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 433 TKEEIIKAAKKARIHDFIMSLpkgyetdigenggilSGGQRQRISIARAF----LKDAPILILDEMTSNVDPVNESLIQD 508
Cdd:cd03227 58 VKAGCIVAAVSAELIFTRLQL---------------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122
|
170 180
....*....|....*....|....*....
gi 446410310 509 AITELA-KNRTVLVVAHHLKTIQKADQIL 536
Cdd:cd03227 123 AILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
349-547 |
2.21e-08 |
|
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: 54.85 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 349 KLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGtdiRDIPydeLLDrISIVMQNvqlfDNTIEENIRVG 428
Cdd:cd03220 40 DVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSS---LLG-LGGGFNP----ELTGRENIYLN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 429 K--KGATKEEIikAAKKARIHDFiMSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLI 506
Cdd:cd03220 109 GrlLGLSRKEI--DEKIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446410310 507 QDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:cd03220 182 QRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
361-545 |
2.59e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 361 ALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDElldRISIVMQNV----QLFD-----NTIEeNI------ 425
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA---RAKLRAKHVgfvfQSFMliptlNALE-NVelpall 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RVGKKGATKEEIIKAAKKARIHDFIMSLPKGyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESL 505
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-----------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446410310 506 IQDAITELakNR----TVLVVAHHLKTIQKADQILVFQKGNLLE 545
Cdd:PRK10584 185 IADLLFSL--NRehgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
337-551 |
2.99e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 337 DFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITlggTDIRdipydelldrISIVMQNVQL 416
Cdd:PRK13409 345 DLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELK----------ISYKPQYIKP 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 -FDNTIEENIR-VGKKGAT---KEEIIKAakkarihdfiMSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILIL 491
Cdd:PRK13409 412 dYDGTVEDLLRsITDDLGSsyyKSEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 492 DEMTSNVDpVNESLI-QDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFqKGnllEKGKHGE 551
Cdd:PRK13409 478 DEPSAHLD-VEQRLAvAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVF-EG---EPGKHGH 536
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
349-548 |
3.13e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.50 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 349 KLSFSIAEKTMTALVGESGSGKT-TITNL--LLRFYDVHKGKITLGGTDIRDIPYDEL----LDRISIVMQNVQlfdNTI 421
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILNLPEKELnklrAEQISMIFQDPM---TSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 422 EENIRVGK---------KGATK----EEIIK---------AAKKARI--HDFimslpkgyetdigenggilSGGQRQRIS 477
Cdd:PRK09473 111 NPYMRVGEqlmevlmlhKGMSKaeafEESVRmldavkmpeARKRMKMypHEF-------------------SGGMRQRVM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446410310 478 IARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKGK 548
Cdd:PRK09473 172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGN 245
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
45-308 |
3.83e-08 |
|
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: 54.80 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 45 IFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDN 124
Cdd:cd18576 26 ALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 125 MSLVVGHMWSRMFGDF--LIGAVVFvgLASIDFKLAIIMAVSVP-IALIFLYL--TIKQ-SEKIENQnnsaLLDMVSLFV 198
Cdd:cd18576 106 IQDTLTTTLAEFLRQIltLIGGVVL--LFFISWKLTLLMLATVPvVVLVAVLFgrRIRKlSKKVQDE----LAEANTIVE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 199 EYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNL---DVLNFI 275
Cdd:cd18576 180 ETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELtagDLVAFL 259
|
250 260 270
....*....|....*....|....*....|...
gi 446410310 276 IFAVIskeFYKPFASMEQHYMYYVSAVDSYERL 308
Cdd:cd18576 260 LYTLF---IAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
345-553 |
4.03e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.79 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 345 FKMEKLSFSIAEKTM-------------TALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDRISIVM 411
Cdd:PRK10575 12 FALRNVSFRVPGRTLlhplsltfpagkvTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 QNVQLFDN-TIEENIRVGK---KGATKEeiIKAAKKARIHDFI-MSLPKGYETDIGENggiLSGGQRQRISIARAFLKDA 486
Cdd:PRK10575 92 QQLPAAEGmTVRELVAIGRypwHGALGR--FGAADREKVEEAIsLVGLKPLAHRLVDS---LSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 487 PILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELL 553
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
348-525 |
4.86e-08 |
|
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: 53.65 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDI---RDIPYDELL-----DRISIVMqnvqlfdn 419
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLdfqRDSIARGLLylghaPGIKTTL-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 420 TIEENIRVGKKGATKEEIIKAAKKARIHDFiMSLPKGYetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVD 499
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*..
gi 446410310 500 PVNESLIQDAIT-ELAKNRTVLVVAHH 525
Cdd:cd03231 158 KAGVARFAEAMAgHCARGGMVVLTTHQ 184
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
335-533 |
5.17e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.42 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 335 NIDFSYEkDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRD--IPYDELLDRI---SI 409
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlCTYQKQLCFVghrSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQLFDNTIEEnIRVGKKGATKEEIIKAAKKARIHDFIMslpkgyetdigengGILSGGQRQRISIARAFLKDAPIL 489
Cdd:PRK13540 85 INPYLTLRENCLYD-IHFSPGAVGITELCRLFSLEHLIDYPC--------------GLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITE-LAKNRTVLVVAHHLKTIQKAD 533
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSHQDLPLNKAD 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
320-541 |
6.43e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 320 KVNGIVPKDNDI-AFENIDFSYEKDEfkmeklsfsiaektMTALVGESGSGKTTITNLLLRFY-------DVHKGKITLG 391
Cdd:TIGR02633 3 EMKGIVKTFGGVkALDGIDLEVRPGE--------------CVGLCGENGAGKSTLMKILSGVYphgtwdgEIYWSGSPLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 392 GTDIRDIPYDElldrISIVMQNVQLFDN-TIEENIRVGKKGATKEEIIK-AAKKARIHDFIMSLpkgyETDIGENG---G 466
Cdd:TIGR02633 69 ASNIRDTERAG----IVIIHQELTLVPElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLREL----QLDADNVTrpvG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 467 ILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:TIGR02633 141 DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
360-540 |
6.79e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 51.99 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 360 TALVGESGSGKTTITNLLLRFYDVHKGK-ITLGGTDIRDIPYDELLdrisivmqnvqlfdntieenirvgkkgatkeeii 438
Cdd:smart00382 5 ILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL---------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 439 kaakkarihdfimslpkgyETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQ-------DAIT 511
Cdd:smart00382 51 -------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrlLLLL 111
|
170 180
....*....|....*....|....*....
gi 446410310 512 ELAKNRTVLVVAHHLKTIQKADQILVFQK 540
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
85-307 |
7.57e-08 |
|
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: 54.01 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 85 DIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDF--LIGAVVFvgLASIDFKLAIIMA 162
Cdd:cd18545 70 RILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLltLVGIVII--MFSLNVRLALVTL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 163 VSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSN---NKSLDNELMNKTKKfgeTSKAASRFka 239
Cdd:cd18545 148 AVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARedeNEEIFDELNRENRK---ANMRAVRL-- 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 240 kqLSIFGFLLD----IGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYER 307
Cdd:cd18545 223 --NALFWPLVElisaLGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAER 292
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
351-517 |
8.53e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.49 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDElldR----ISIVMQNVQLFDN-TIEENI 425
Cdd:COG1137 23 SLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK---RarlgIGYLPQEASIFRKlTVEDNI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 426 RvgkkgATKE--EIIKAAKKAR----IHDFimSLpkgyeTDIGENGGI-LSGGQRQRISIARAFLKDAPILILDEMTSNV 498
Cdd:COG1137 100 L-----AVLElrKLSKKEREERleelLEEF--GI-----THLRKSKAYsLSGGERRRVEIARALATNPKFILLDEPFAGV 167
|
170 180
....*....|....*....|.
gi 446410310 499 DP--VNEslIQDAITELaKNR 517
Cdd:COG1137 168 DPiaVAD--IQKIIRHL-KER 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-545 |
8.71e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 8.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 342 KDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIR-DIPYDELLDRISIVMQNVQ---LF 417
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITESRRdngFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 418 DN-TIEENIRV-------GKKGATKeeIIKAAKKARIHDFIMSLPKGYETDIGENGGILSGGQRQRISIARAFLKDAPIL 489
Cdd:PRK09700 354 PNfSIAQNMAIsrslkdgGYKGAMG--LFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHLKTIQKA-DQILVFQKGNLLE 545
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
350-552 |
9.13e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 9.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTdirdiPYDELLDR------ISIVMQNVQLFDN-TIE 422
Cdd:PRK15439 30 IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN-----PCARLTPAkahqlgIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 423 ENIRVGKKGatkeeiiKAAKKARIHDFIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPV- 501
Cdd:PRK15439 105 ENILFGLPK-------RQASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAe 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446410310 502 NESLIQDAITELAKNRTVLVVAHHLKTI-QKADQILVFQKGNLLEKGKHGEL 552
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
351-561 |
1.06e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.94 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 351 SFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLD-RISIVMqnvqLFDN---------- 419
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvRSDIQM----IFQDplaslnprmt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 420 ---TIEENIRVGKKGATKEEIikaakKARIHDFIMSLpkgyetdigengGIL-----------SGGQRQRISIARAFLKD 485
Cdd:PRK15079 117 igeIIAEPLRTYHPKLSRQEV-----KDRVKAMMLKV------------GLLpnlinryphefSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 486 APILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAKNGY-YTK 561
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHpYTK 259
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
14-307 |
1.66e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 53.25 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 14 KRDLIISSVFFALYGLSSIAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRER 93
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 94 MIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGhmWSRM---FGDFLIGAVVFVgLASIDFKLAIIMAVSVP---- 166
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIIS--WGLVdlvWGITYMIGILIV-MLILNWKLALIVLAVVPvlav 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 167 IALIFLYLTIKQSEKIENQNNsallDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFG 246
Cdd:cd18540 158 VSIYFQKKILKAYRKVRKINS----RITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 247 FLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYER 307
Cdd:cd18540 234 FLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
86-308 |
2.00e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 52.87 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 86 IVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSV 165
Cdd:cd18550 70 VMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 166 PIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEY--VRGIPVLKSFSNNKSLdnelmnkTKKFGETSKAASRFKAKQ-- 241
Cdd:cd18550 150 PLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDE-------AARFARRSRELRDLGVRQal 222
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446410310 242 -----LSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYERL 308
Cdd:cd18550 223 agrwfFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
82-271 |
2.13e-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: 52.88 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 82 AGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMS--LVVGhmwsrmFGDFLIGAVVFVG----LASIDF 155
Cdd:cd18546 66 TGERLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSelLQTG------LVQLVVSLLTLVGiavvLLVLDP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 156 KLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFsnNKSLDNElmnktKKFGETSKA-- 233
Cdd:cd18546 140 RLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAF--RRERRNA-----ERFAELSDDyr 212
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446410310 234 ASRFKAKQL-SIFG----FLLDIGYLVLLIAGAILVIKGNLDV 271
Cdd:cd18546 213 DARLRAQRLvAIYFpgveLLGNLATAAVLLVGAWRVAAGTLTV 255
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
337-551 |
2.37e-07 |
|
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: 53.63 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 337 DFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLlrfydvhKGKITlggTDIRDIPYDElldRISIVMQNVQ- 415
Cdd:COG1245 346 DLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKIL-------AGVLK---PDEGEVDEDL---KISYKPQYISp 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 416 LFDNTIEENIRVGKKGAT-----KEEIIKAakkarihdfiMSLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILI 490
Cdd:COG1245 413 DYDGTVEEFLRSANTDDFgssyyKTEIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 491 LDEMTSNVDpVNESL-IQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFqKGnllEKGKHGE 551
Cdd:COG1245 479 LDEPSAHLD-VEQRLaVAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVF-EG---EPGVHGH 538
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
349-557 |
2.96e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 349 KLSFSIAEKTMTALVGESGSGKTTITNlllrfydvhkgkitlggtdirDIPYDELLDRISIVMQNvqLFDNTIeenIRVG 428
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLVN---------------------EGLYASGKARLISFLPK--FSRNKL---IFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 429 KKGatkeeiikaakkarihdFIMSLPKGYETdIGENGGILSGGQRQRISIARAFLKDAP--ILILDEMTSNVDPVNESLI 506
Cdd:cd03238 67 QLQ-----------------FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446410310 507 QDAITEL-AKNRTVLVVAHHLKTIQKADQILVFQKGnlleKGKHGELLAKNG 557
Cdd:cd03238 129 LEVIKGLiDLGNTVILIEHNLDVLSSADWIIDFGPG----SGKSGGKVVFSG 176
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
350-562 |
4.28e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.01 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTT----ITNLLlrfydvH--KGKITLGGTDirdiPYD---ELLDRISIVM-QNVQLF-D 418
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTtikmLTGIL------VptSGEVRVLGYV----PFKrrkEFARRIGVVFgQRSQLWwD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 419 NTIEENIRVgkkgaTKE--EIIKAAKKARIHDFIMSLpkgyetDIGEnggI-------LSGGQRQRISIARAFLKDAPIL 489
Cdd:COG4586 111 LPAIDSFRL-----LKAiyRIPDAEYKKRLDELVELL------DLGE---LldtpvrqLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 490 ILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGELLAKNGYYTKL 562
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTI 252
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
139-308 |
4.30e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 51.74 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 139 DFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDN 218
Cdd:cd18555 125 DLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 219 ELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYY 298
Cdd:cd18555 205 KWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQF 284
|
170
....*....|
gi 446410310 299 VSAVDSYERL 308
Cdd:cd18555 285 ILLKSYLERL 294
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
97-307 |
4.52e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 51.80 E-value: 4.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 97 KLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTI 176
Cdd:cd18565 96 HVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQ 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 177 KQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVL 256
Cdd:cd18565 176 RRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVAT 255
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 257 LIAGAILVIKGN------LDVLNFIIFAVISKEFYKPFASMEQhymyyvsAVDSYER 307
Cdd:cd18565 256 FVVGGYWVLDGPplftgtLTVGTLVTFLFYTQRLLWPLTRLGD-------LIDQYQR 305
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
139-308 |
5.30e-07 |
|
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: 51.41 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 139 DFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDN 218
Cdd:cd18568 125 DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRW 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 219 ELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYY 298
Cdd:cd18568 205 RWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDEL 284
|
170
....*....|
gi 446410310 299 VSAVDSYERL 308
Cdd:cd18568 285 QETRISVERL 294
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
347-554 |
1.20e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.57 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLrfyDVHKG--KITLGGTDIRDIPYDELLDR---------ISIVMQNVQ 415
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAIC---GVTKDnwRVTADRMRFDDIDLLRLSPRerrklvghnVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 416 lfdNTIEENIRVGKK------GAT------------KEEIIKAAKKARI--HDFIM-SLPkgYEtdigenggiLSGGQRQ 474
Cdd:PRK15093 100 ---SCLDPSERVGRQlmqnipGWTykgrwwqrfgwrKRRAIELLHRVGIkdHKDAMrSFP--YE---------LTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 475 RISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR--TVLVVAHHLKTIQK-ADQILVFQKGNLLEKGKHGE 551
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQTVETAPSKE 245
|
...
gi 446410310 552 LLA 554
Cdd:PRK15093 246 LVT 248
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
358-541 |
1.24e-06 |
|
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: 49.16 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 358 TMTALVGESGSGKTTITNLL-LRFYD-VHKGKITLGGtdirdIPYDELLDRIS-IVMQNVQLFDN-TIEENIRvgkkgat 433
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLaGRKTAgVITGEILING-----RPLDKNFQRSTgYVEQQDVHSPNlTVREALR------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 434 keeiIKAAKKArihdfimslpkgyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL 513
Cdd:cd03232 102 ----FSALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
170 180 190
....*....|....*....|....*....|.
gi 446410310 514 AKN-RTVLVVAHH--LKTIQKADQILVFQKG 541
Cdd:cd03232 155 ADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
348-493 |
1.25e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 348 EKLSFSIAEKTMTALVGESGSGKTTitnlLLR----FYDVHKGKITLGGTDI---RDIPYDELL---------DRIsivm 411
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTS----LLRilagLARPDAGEVLWQGEPIrrqRDEYHQDLLylghqpgikTEL---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 qnvqlfdnTIEENIRVGKKGA---TKEEIIKAAKKARIHDFiMSLPKGYetdigenggiLSGGQRQRISIARAFLKDAPI 488
Cdd:PRK13538 90 --------TALENLRFYQRLHgpgDDEALWEALAQVGLAGF-EDVPVRQ----------LSAGQQRRVALARLWLTRAPL 150
|
....*
gi 446410310 489 LILDE 493
Cdd:PRK13538 151 WILDE 155
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
17-280 |
1.52e-06 |
|
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: 50.17 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLSSIAMIvIVFSILFQIFDGTS---------LASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIV 87
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMT-IVFGDLFDAFTDFGsgesspdefLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 88 QQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMwsrmFGDFLIGAVVFVGLASIDF----KLAIIMAV 163
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEK----LGLLIQSLSTFIAGFIIAFiyswKLTLVLLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 164 SVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLD---NELMNKTKKFGetsKAASRFKAK 240
Cdd:cd18577 156 TLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIkrySKALEKARKAG---IKKGLVSGL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446410310 241 QLSIFGFLLDIGYLVLLIAGAILVIKGNL---DVLNfIIFAVI 280
Cdd:cd18577 233 GLGLLFFIIFAMYALAFWYGSRLVRDGEIspgDVLT-VFFAVL 274
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
322-541 |
1.61e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 322 NGIVPKDNDI-AFENIDFSYEKDEfkmeklsfsiaektMTALVGESGSGKTTITNLLLRFY--DVHKGKITLGGTD---- 394
Cdd:PRK13549 9 KNITKTFGGVkALDNVSLKVRAGE--------------IVSLCGENGAGKSTLMKVLSGVYphGTYEGEIIFEGEElqas 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 395 -IRDIpydellDR--ISIVMQNVQLFDN-TIEENIRVGkkgatkEEIIKAAkkaRIHDFIM-----SLPKGYETDIGENG 465
Cdd:PRK13549 75 nIRDT------ERagIAIIHQELALVKElSVLENIFLG------NEITPGG---IMDYDAMylraqKLLAQLKLDINPAT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 466 --GILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQK-ADQILVFQKG 541
Cdd:PRK13549 140 pvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLkAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
347-496 |
1.89e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDIPYDELLDR-ISIVMQNV-QLFDNTIEEN 424
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENgISMVHQELnLVLQRSVMDN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 425 IRVGKKgATKEEIIKAAKKARIHDFIMSlpkgyETDIG----ENGGILSGGQRQRISIARAFLKDAPILILDEMTS 496
Cdd:PRK10982 94 MWLGRY-PTKGMFVDQDKMYRDTKAIFD-----ELDIDidprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
361-527 |
2.24e-06 |
|
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: 50.78 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 361 ALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIrdipydelLDRISIVMQNVQL---FDNTieENIRVGK-------- 429
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--------LTNISDVHQNMGYcpqFDAI--DDLLTGRehlylyar 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 430 -KGATKEEIIKAAKKArihdfIMSLpkGYETDIGENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQD 508
Cdd:TIGR01257 2039 lRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180
....*....|....*....|
gi 446410310 509 AITELAKN-RTVLVVAHHLK 527
Cdd:TIGR01257 2112 TIVSIIREgRAVVLTSHSME 2131
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
339-526 |
3.30e-06 |
|
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: 48.90 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 339 SYEKDEFKMEKLSfSIAEKTMTALVGESGSGKTTITNLLlrfydvhKGKIT--LGGTDIRDiPYDELLD----------- 405
Cdd:cd03236 9 RYGPNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKIL-------AGKLKpnLGKFDDPP-DWDEILDefrgselqnyf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 406 --------RISIVMQNVQL----FDNTIEENIRVGKKGATKEEIIKAakkarihdfiMSLPKGYETDIGEnggiLSGGQR 473
Cdd:cd03236 80 tkllegdvKVIVKPQYVDLipkaVKGKVGELLKKKDERGKLDELVDQ----------LELRHVLDRNIDQ----LSGGEL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446410310 474 QRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHL 526
Cdd:cd03236 146 QRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEdDNYVLVVEHDL 199
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
21-224 |
3.54e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). 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: 350054 [Multi-domain] Cd Length: 290 Bit Score: 49.07 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 21 SVFFALYGL-SSIAMIVIVFSILFQIFDGT-SLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKL 98
Cdd:cd18781 1 TVLLQWISLlANIAFVFSIANLLQKLLEGKlTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 99 KKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWSRMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQ 178
Cdd:cd18781 81 LRLGPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQKI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446410310 179 SEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKsLDNELMNKT 224
Cdd:cd18781 161 AKKLLSKYWGSYTDLGDSFLENLQGLTTLKIYQADE-RRHEEMNEE 205
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
141-280 |
5.79e-06 |
|
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: 48.16 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 141 LIGAVVFVglASIDFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNEL 220
Cdd:cd18548 127 LIGAIIMA--FRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERF 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 221 MNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDV---------LNFIIFAVI 280
Cdd:cd18548 205 DKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVgdlvafinyLMQILMSLM 273
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
324-524 |
6.78e-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: 48.98 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 324 IVPKDNDIAFENIDFSYEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTD----IRDIP 399
Cdd:TIGR00954 445 VEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklfyVPQRP 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 400 Y---DELLDRIsivmqnvqLFDNTIEENIRvgkKGATKEEIIKAAKKARIHDFIMslpkgyetdigENGG---------I 467
Cdd:TIGR00954 525 YmtlGTLRDQI--------IYPDSSEDMKR---RGLSDKDLEQILDNVQLTHILE-----------REGGwsavqdwmdV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 468 LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNEsliqDAITELAKNR--TVLVVAH 524
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE----GYMYRLCREFgiTLFSVSH 637
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
468-525 |
6.96e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 6.96e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 468 LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN-RT-VLVVAHH 525
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETqLLFVSHH 461
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
462-557 |
8.06e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 462 GENGGILSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQ 539
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*...
gi 446410310 540 KGNLLEKGKHGELLAKNG 557
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
346-543 |
9.91e-06 |
|
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: 48.28 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 346 KMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYD-VHKGKITLGG--TDIRD-----------IPYDELLDRISIVM 411
Cdd:TIGR02633 275 RVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNpaqairagiamVPEDRKRHGIVPIL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 412 ---QNVQLfdNTIEENIRVGKKGATKEE--IIKAAKKARIHDFIMSLPKGYetdigenggiLSGGQRQRISIARAFLKDA 486
Cdd:TIGR02633 355 gvgKNITL--SVLKSFCFKMRIDAAAELqiIGSAIQRLKVKTASPFLPIGR----------LSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 487 PILILDEMTSNVDPVNESLIQDAITELAKNR-TVLVVAHHL-KTIQKADQILVFQKGNL 543
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQLAQEGvAIIVVSSELaEVLGLSDRVLVIGEGKL 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
328-524 |
1.58e-05 |
|
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: 47.62 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 328 DNDIAFENIDFSYEkDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDirdipydelldRI 407
Cdd:TIGR03719 320 DKVIEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV-----------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 408 SIVMQNVQLFD--NTIEENI-------RVGKKgatkeEIIKAAKKARIhDFimslpKGyeTDIGENGGILSGGQRQRISI 478
Cdd:TIGR03719 388 AYVDQSRDALDpnKTVWEEIsggldiiKLGKR-----EIPSRAYVGRF-NF-----KG--SDQQKKVGQLSGGERNRVHL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446410310 479 ARAFLKDAPILILDEMTSNVDPvnESL--IQDAITELAKnrTVLVVAH 524
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDV--ETLraLEEALLNFAG--CAVVISH 498
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
471-501 |
1.98e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 1.98e-05
10 20 30
....*....|....*....|....*....|.
gi 446410310 471 GQRQRISIARAFLKDAPILILDEMTSNVDPV 501
Cdd:NF033858 401 GIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
367-522 |
2.41e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.94 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 367 GSGKTTITNLLLRFYDVHKGKITLGGT--DIRDiPYD----------EllDRIS--IVMqnvqlfDNTIEENI------R 426
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKpvRIRS-PRDairagiayvpE--DRKGegLVL------DLSIRENItlasldR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKKGatkeeII-KAAKKARIHDFIMSL---PKGYETDIGEnggiLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVN 502
Cdd:COG1129 359 LSRGG-----LLdRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
170 180
....*....|....*....|.
gi 446410310 503 ESLIQDAITELAKN-RTVLVV 522
Cdd:COG1129 430 KAEIYRLIRELAAEgKAVIVI 450
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
466-536 |
2.67e-05 |
|
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: 45.29 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 466 GILSGGQRQ------RISIARAFLKDAPILILDEMTSNVDP--VNESLIqDAITELA--KNRTVLVVAHHLKTIQKADQI 535
Cdd:cd03240 114 GRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenIEESLA-EIIEERKsqKNFQLIVITHDEELVDAADHI 192
|
.
gi 446410310 536 L 536
Cdd:cd03240 193 Y 193
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
347-547 |
2.71e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 347 MEKLSFSIAEKTMTALVGESGSGKTTITNLLL---------RFYDVhKGKITLGGTDIRDIPYDELLDRISIVMQNVQ-L 416
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggapRGARV-TGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 FDNTIEENIRVGKKGATKEEIIKAAKKARIHDFIMSLpKGYETDIGENGGILSGGQRQRISIARAFLK---------DAP 487
Cdd:PRK13547 96 FAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALAL-AGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELAK--NRTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:PRK13547 175 YLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHG 237
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
468-557 |
3.30e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 468 LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKN--RTVLVVAHHLKTIQK-ADQILVFQKgnll 544
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYlSDRIHVFEG---- 147
|
90
....*....|...
gi 446410310 545 EKGKHGELLAKNG 557
Cdd:cd03222 148 EPGVYGIASQPKG 160
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
350-499 |
3.33e-05 |
|
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: 44.95 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTT----ITNLLLRFYDVhKGKITLGGtdirdIPYDELLDRI--SIVMQNvqlfdntiEE 423
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNG-----IPYKEFAEKYpgEIIYVS--------EE 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 424 NIRVgkKGATKEEIIKAAKKARIHDFImslpKGyetdigenggiLSGGQRQRISIARAFLKDAPILILDEMTSNVD 499
Cdd:cd03233 92 DVHF--PTLTVRETLDFALRCKGNEFV----RG-----------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
44-280 |
5.08e-05 |
|
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: 45.17 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 44 QIFDGTSLASLYKYFIAIGLLVVFKGICnmvadmkkhSAG-FDIVQQIRERMIIKLKK--------FSLGFYTNERLGEI 114
Cdd:cd18575 25 QGFAAGNTALLNRAFLLLLAVALVLALA---------SALrFYLVSWLGERVVADLRKavfahllrLSPSFFETTRTGEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 115 NTILHKDVDNMSLVVGH---MWSRMFgDFLIGAVVFVGLASidFKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALL 191
Cdd:cd18575 96 LSRLTTDTTLIQTVVGSslsIALRNL-LLLIGGLVMLFITS--PKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 192 DMVSLFVEYVRGIPVLKSFSNNKsldnelmNKTKKFGETSKAASRFKAKQLSIFGFLldIGYLVLLIAGAILVI--KGNL 269
Cdd:cd18575 173 DLSAFAEETLSAIKTVQAFTRED-------AERQRFATAVEAAFAAALRRIRARALL--TALVIFLVFGAIVFVlwLGAH 243
|
250 260
....*....|....*....|.
gi 446410310 270 DVLN----------FIIFAVI 280
Cdd:cd18575 244 DVLAgrmsagelsqFVFYAVL 264
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
468-543 |
6.11e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 6.11e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 468 LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAK-NRTVLVVAHHLKTI-QKADQILVFQKGNL 543
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
57-287 |
1.08e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 44.43 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 57 YFIAIGLLV--VFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGHMWS 134
Cdd:cd18564 54 LLAAAALVGiaLLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 135 RMFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYL---TIKQSEKIENQNNSAlldMVSLFVEYVRGIPVLKSFS 211
Cdd:cd18564 134 PLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRfsrRIKEASREQRRREGA---LASVAQESLSAIRVVQAFG 210
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446410310 212 NNKSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKP 287
Cdd:cd18564 211 REEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKP 286
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
468-511 |
1.14e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 43.68 E-value: 1.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 446410310 468 LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAIT 511
Cdd:PRK13543 138 LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
80-281 |
1.43e-04 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 44.01 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 80 HSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMslvvGHMWSRMFGDFLIGAVVFVG----LASIDF 155
Cdd:cd18585 60 HDATFRLLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTL----DNLYLRVLSPPVVALLVILAtilfLAFFSP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 156 KLAIIMAVSVPIALIFL-YLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKTKKFGETSKAA 234
Cdd:cd18585 136 ALALILLAGLLLAGVVIpLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRL 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446410310 235 SRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLD--VLNFIIFAVIS 281
Cdd:cd18585 216 ARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALDgaLLAMLVFAVLA 264
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
350-547 |
1.44e-04 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 43.53 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGtdirdipydelldRISIVMqNVQL-FDN--TIEENIR 426
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSALL-ELGAgFHPelTGRENIY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 427 VGKK--GATKEEIikAAKKARIHDFimslpkgyeTDIGE-------NggiLSGGQRQRISIARAFLKDAPILILDEMTSN 497
Cdd:COG1134 111 LNGRllGLSRKEI--DEKFDEIVEF---------AELGDfidqpvkT---YSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446410310 498 VDPV--NESLiqDAITELAKN-RTVLVVAHHLKTIQK-ADQILVFQKGNLLEKG 547
Cdd:COG1134 177 GDAAfqKKCL--ARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDG 228
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
331-536 |
5.50e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 331 IAFENIDFSYEKDEfkMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRDI--PYdelldrIS 408
Cdd:PRK13541 2 LSLHQLQFNIEQKN--LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIakPY------CT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 409 IVMQNVQL-FDNTIEENIRVGKKGATKEEIIKAA-KKARIHDFIMSlpKGYEtdigenggiLSGGQRQRISIARAFLKDA 486
Cdd:PRK13541 74 YIGHNLGLkLEMTVFENLKFWSEIYNSAETLYAAiHYFKLHDLLDE--KCYS---------LSSGMQKIVAIARLIACQS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446410310 487 PILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQIL 536
Cdd:PRK13541 143 DLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
350-536 |
5.73e-04 |
|
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: 41.83 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLrfYDVHKGKITLGGTD---IRDIPYDELLDRISIVMQN------------- 413
Cdd:cd03271 14 IDVDIPLGVLTCVTGVSGSGKSSLINDTL--YPALARRLHLKKEQpgnHDRIEGLEHIDKVIVIDQSpigrtprsnpaty 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 414 VQLFDnTI--------------EENIRVGKKGATKEEIIK-AAKKAriHDFIMSLPK-------------GYETdIGENG 465
Cdd:cd03271 92 TGVFD-EIrelfcevckgkrynRETLEVRYKGKSIADVLDmTVEEA--LEFFENIPKiarklqtlcdvglGYIK-LGQPA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 466 GILSGGQRQRISIARAFLKDAP---ILILDEMTSNVDPVNESLIQDAITEL-AKNRTVLVVAHHLKTIQKADQIL 536
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCADWII 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
318-541 |
5.79e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 318 PDKVNgiVPKDNDIAFENIDfsyEKDEFKMEKLSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRD 397
Cdd:PRK10982 240 PDKEN--KPGEVILEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 398 IPYDELLD----------RISIVMQNVQLFDNTIEENIR--VGKKGATKEEIIKAAKKARIHDFIMSLPkGYETDIGEng 465
Cdd:PRK10982 315 HNANEAINhgfalvteerRSTGIYAYLDIGFNSLISNIRnyKNKVGLLDNSRMKSDTQWVIDSMRVKTP-GHRTQIGS-- 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 466 giLSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELA-KNRTVLVVAHHL-KTIQKADQILVFQKG 541
Cdd:PRK10982 392 --LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
444-536 |
6.54e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.69 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 444 ARIHDFIMSLPKGYETdIGENGGILSGGQRQRISIARAFLKDA---PILILDEMTSNV--DPVNESLiqDAITELAKN-R 517
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIR-LGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfDDIKKLL--EVLQRLVDKgN 883
|
90
....*....|....*....
gi 446410310 518 TVLVVAHHLKTIQKADQIL 536
Cdd:TIGR00630 884 TVVVIEHNLDVIKTADYII 902
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
443-557 |
7.06e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 443 KARIhDFIMSLPKGYETdIGENGGILSGGQRQRISIAR---AFLKDApILILDEMTSNVDPVNESLIQDAITEL-AKNRT 518
Cdd:cd03270 115 RERL-GFLVDVGLGYLT-LSRSAPTLSGGEAQRIRLATqigSGLTGV-LYVLDEPSIGLHPRDNDRLIETLKRLrDLGNT 191
|
90 100 110
....*....|....*....|....*....|....*....
gi 446410310 519 VLVVAHHLKTIQKADQILVFQKGnlleKGKHGELLAKNG 557
Cdd:cd03270 192 VLVVEHDEDTIRAADHVIDIGPG----AGVHGGEIVAQG 226
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
59-308 |
7.49e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 41.69 E-value: 7.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 59 IAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMIIKLKKFSLGFYTNERLGEINTILHKDVDNMSLVVGH-----MW 133
Cdd:cd18589 40 TVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSEnlsllMW 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 134 SRMFGDFLIGAVVFVGLasidfKLAIIMAVSVPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNN 213
Cdd:cd18589 120 YLARGLFLFIFMLWLSP-----KLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 214 KsldnelmnktkkfGETSKAASRF-KAKQL---------------SIFGFLLDIGylvLLIAGAILVIKGNLDVLNFIIF 277
Cdd:cd18589 195 E-------------GEAQRYRQRLqKTYRLnkkeaaayavsmwtsSFSGLALKVG---ILYYGGQLVTAGTVSSGDLVTF 258
|
250 260 270
....*....|....*....|....*....|.
gi 446410310 278 AVISKEFYKPFASMEQHYMYYVSAVDSYERL 308
Cdd:cd18589 259 VLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
136-278 |
9.11e-04 |
|
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: 41.31 E-value: 9.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 136 MFGDFLIGAVVFVGLASIDFKLAIIMAVSVPIALIFLYLTIKQSEKI--ENQNNSAllDMVSLFVEYVRGIPVLKSFSNN 213
Cdd:cd18543 119 LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAsrRAQDQAG--DLATVVEESVTGIRVVKAFGRE 196
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446410310 214 KSLDNELMNKTKKFGETSKAASRFKAKQLSIFGFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFA 278
Cdd:cd18543 197 RRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFS 261
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
462-518 |
9.73e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 40.37 E-value: 9.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446410310 462 GENGGILSGGQRQRISIARAF----LKDAPILILDEMTSNVDPVNESLIQDAITELAKNRT 518
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTS 149
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
420-541 |
1.28e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 420 TIEENIRVG--KKGATKEEIIKAAKKARIHD-FIMSL----PKGyETDIGEnggiLSGGQRQRISIARAFLKDAPILILD 492
Cdd:PRK11288 347 SVADNINISarRHHLRAGCLINNRWEAENADrFIRSLniktPSR-EQLIMN----LSGGNQQKAILGRWLSEDMKVILLD 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446410310 493 EMTSNVDPVNESLIQDAITELAKN-RTVLVVAHHL-KTIQKADQILVFQKG 541
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLpEVLGVADRIVVMREG 472
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
345-536 |
1.72e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 39.76 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 345 FKmeklSFsiAEKT-------MTALVGESGSGKTTITNLLlRFydvhkgkiTLGGTDIRDIPYDELLD--------RISI 409
Cdd:cd03278 9 FK----SF--ADKTtipfppgLTAIVGPNGSGKSNIIDAI-RW--------VLGEQSAKSLRGEKMSDvifagsetRKPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 410 VMQNVQL-FDNTIEE-NI----RVgkkgatkEEIIKAAKKARIHdfiMSLpkgyetdigenggiLSGGQRQRISIARAF- 482
Cdd:cd03278 74 NFAEVTLtFDNSDGRySIisqgDV-------SEIIEAPGKKVQR---LSL--------------LSGGEKALTALALLFa 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446410310 483 ---LKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQIL 536
Cdd:cd03278 130 ifrVRPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLY 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
466-499 |
2.60e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.37 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|....
gi 446410310 466 GILSGGQRQRISIARAFLKDAPILILDEMTSNVD 499
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
468-543 |
2.80e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 2.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 468 LSGGQRQRISIARAFLKDAPILILDEMTSNVDPVNESLIQDAITELAKNR-TVLVVAHHLKTIQK-ADQILVFQKGNL 543
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGvAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
468-536 |
6.61e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 6.61e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446410310 468 LSGGQRQRISIARAF----LKDAPILILDEMTSNVDPVNESLIQDAITELAKNRTVLVVAHHLKTIQKADQIL 536
Cdd:pfam02463 1078 LSGGEKTLVALALIFaiqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
350-543 |
6.75e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.24 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 350 LSFSIAEKTMTALVGESGSGKTTITNLLLRFYDVHKGKITLGGTDIRD-------------IPYDELldRISIVMqnvql 416
Cdd:COG3845 277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsprerrrlgvayIPEDRL--GRGLVP----- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 417 fDNTIEENI--------RVGKKGATKEEIIKAAKKARIHDF-ImsLPKGYETDIGEnggiLSGGQRQRISIARAFLKDAP 487
Cdd:COG3845 350 -DMSVAENLilgryrrpPFSRGGFLDRKAIRAFAEELIEEFdV--RTPGPDTPARS----LSGGNQQKVILARELSRDPK 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446410310 488 ILILDEMTSNVDPVNESLIQDAITELA-KNRTVLVVAHHLKTIQK-ADQILVFQKGNL 543
Cdd:COG3845 423 LLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
17-308 |
7.88e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 38.73 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 17 LIISSVFFALYGLssiAMIVIVFSILFQIFDGTSLASLYKYFIAIGLLVVFKGICNMVADMKKHSAGFDIVQQIRERMII 96
Cdd:cd18782 7 VLALSFVVQLLGL---ANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 97 KLKKFSLGFYTNERLGEINTILHkDVDNMSlvvghmwsrmfgDFLIG-----------AVVFVG-LASIDFKLAIIMAVS 164
Cdd:cd18782 84 HLLRLPLGFFDKRPVGELSTRIS-ELDTIR------------GFLTGtalttlldvlfSVIYIAvLFSYSPLLTLVVLAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446410310 165 VPIALIFLYLTIKQSEKIENQNNSALLDMVSLFVEYVRGIPVLKSFSNNKSLDNELMNKtkkFGETSKAAsrFKAKQLSI 244
Cdd:cd18782 151 VPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNR---YARSLGEG--FKLTVLGT 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446410310 245 F-----GFLLDIGYLVLLIAGAILVIKGNLDVLNFIIFAVISKEFYKPFASMEQHYMYYVSAVDSYERL 308
Cdd:cd18782 226 TsgslsQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| |
