|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-732 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 1029.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 17 AAHAWPTAALLLLLVDWLLLRPVLPGIFSLLVP-EVPLLRVWAVGLSRWAILGLGVRGVLGVTAGarGWLAALQPLVAAL 95
Cdd:TIGR00958 1 AALAYLLPWFSLLLVDWALLRDLLQGIFGLLLPfEKGLYVLWLEGTLRLGVLWLGALGILLNKAG--GLLAAVKPLVAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 96 GLALPGLASFRKLSAWGALREGDNAGLLHWNsrldAFVLSYVAALPAAALWHKLGGFWAP-----SGHKGAGDMLCRMLG 170
Cdd:TIGR00958 79 CLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETADLLFRLLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 171 FLDSKKGRLHLVLVLLILSCLGEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHS 250
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 251 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 330
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 331 FLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVS 410
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 411 GMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLN 490
Cdd:TIGR00958 395 GMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 570
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALI 650
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 651 RKPRLLILDDATSALDAgnqlRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 730
Cdd:TIGR00958 634 RKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
..
gi 56717 731 MV 732
Cdd:TIGR00958 710 LV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
193-734 |
2.39e-143 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 432.28 E-value: 2.39e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 193 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNP 272
Cdd:COG1132 37 ELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 273 TGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESL 352
Cdd:COG1132 117 TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 353 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAVS 432
Cdd:COG1132 197 AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 433 SGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP-CSPLSGSLAPLNMKGLVKFQDVSFAYPnhPNVQ 511
Cdd:COG1132 277 VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeIPDPPGAVPLPPVRGEIEFENVSFSYP--GDRP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI 591
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGLtRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQL 671
Cdd:COG1132 435 RYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 672 RVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 734
Cdd:COG1132 514 LIQEALER--LMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRL 574
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
192-470 |
2.08e-136 |
|
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: 403.78 E-value: 2.08e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 192 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 271
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 272 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 351
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 352 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 431
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 56717 432 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
484-712 |
4.54e-122 |
|
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: 364.48 E-value: 4.54e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 484 GSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ 563
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 564 YDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 643
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSV 712
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
194-733 |
1.23e-112 |
|
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: 356.84 E-value: 1.23e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKTAPSfarnMWLMCILTIASTVLEFAGDGIYNITMGHMHSRV----HGEVFRAVLHQETGFFL 269
Cdd:COG2274 173 LATPLFTQVVIDRVLPNQDLST----LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIdlrlSSRFFRHLLRLPLSFFE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KNPTGSITSRVTeDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 349
Cdd:COG2274 249 SRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREES 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 350 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGILYLGGQLVVR 428
Cdd:COG2274 328 EASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKlRRLSNLLSTLSGLLQQLAT-VALLWLGAYLVID 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 429 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP-CSPLSGSLAPLNMKGLVKFQDVSFAYPNH 507
Cdd:COG2274 407 GQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 508 pNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSF 587
Cdd:COG2274 487 -SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTI 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 588 RENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDA 667
Cdd:COG2274 566 RENITLGDP-DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 668 GNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 733
Cdd:COG2274 645 ETEAIILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
495-734 |
6.38e-96 |
|
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: 297.14 E-value: 6.38e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGRSFRENIAYGLTRtPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 654
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 734
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
256-733 |
4.70e-94 |
|
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: 303.93 E-value: 4.70e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 256 VFRAVLHQETGFFLKNPTGSITSRVTEDT----SNVCESISDKLNLFLWYLGRglclLAFMIWGSFYLTVVTLLSLPLLF 331
Cdd:TIGR02204 97 VFAHLISLSPSFFDKNRSGEVVSRLTTDTtllqSVIGSSLSMALRNALMCIGG----LIMMFITSPKLTSLVLLAVPLVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 332 LLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK--EALAYVTE-VWTMS 408
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQriRTRALLTAiVIVLV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 409 VSGMllkVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP--CSPLSGSL 486
Cdd:TIGR02204 253 FGAI---VGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 487 APLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH 566
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 567 HYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTpTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALA 646
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIA 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 647 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 726
Cdd:TIGR02204 489 RAILKDAPILLLDEATSALDAESEQLVQQALETL--MKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG 566
|
....*..
gi 56717 727 CYRSMVE 733
Cdd:TIGR02204 567 LYARLAR 573
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
254-728 |
4.57e-90 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 293.16 E-value: 4.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 254 GEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLL 333
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 334 PRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKF-----RQKLEEMKPLNKKEALAYVTEVWTMS 408
Cdd:TIGR02203 171 MRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFdavsnRNRRLAMKMTSAGSISSPITQLIASL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 409 VSGMLLkvgilYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPcSPLSGSLAP 488
Cdd:TIGR02203 251 ALAVVL-----FIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP-EKDTGTRAI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY 568
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 LHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARA 648
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 649 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCY 728
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
192-470 |
8.40e-81 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 259.40 E-value: 8.40e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 192 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 271
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 272 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 351
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 352 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 431
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 56717 432 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18572 251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
360-726 |
1.34e-78 |
|
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: 262.39 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 360 LEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKPLnkKEAL--AYVTEVWTM-SVSGMLLKVGILYLGGQLVVRGAV 431
Cdd:COG4988 201 LDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtMKVL--RVAFlsSAVLEFFASlSIALVAVYIGFRLLGGSLTLFAAL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 432 ssgnlvsFVLYqLqftrAVEVLLSI-------YPSMQkSVGASEKIFEYLDRTPCSPLSGSL-APLNMKGLVKFQDVSFA 503
Cdd:COG4988 279 -------FVLL-L----APEFFLPLrdlgsfyHARAN-GIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 504 YPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLF 583
Cdd:COG4988 346 YPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLF 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 584 GRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 663
Cdd:COG4988 424 AGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 664 ALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 726
Cdd:COG4988 503 HLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
192-470 |
1.15e-76 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 248.77 E-value: 1.15e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 192 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVleFAG--DGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 269
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSV--AAGirGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 349
Cdd:cd18784 89 TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 350 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 429
Cdd:cd18784 169 DSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 56717 430 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18784 249 QISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
368-731 |
1.03e-75 |
|
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: 255.90 E-value: 1.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 368 TVRSFANEEGEAQKFRQKLEEmkplnkKEALAyvTEVWTmsvSGMLLKVG-----------ILYLGGQLVVRGAVSSGNL 436
Cdd:COG5265 230 TVKYFGNEAREARRYDEALAR------YERAA--VKSQT---SLALLNFGqaliialgltaMMLMAAQGVVAGTMTVGDF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 437 VSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLNMK-GLVKFQDVSFAYpnHPNVQVLQG 515
Cdd:COG5265 299 VLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGgGEVRFENVSFGY--DPERPILKG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 516 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGl 595
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 596 tRtP--TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRV 673
Cdd:COG5265 456 -R-PdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 674 QRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 731
Cdd:COG5265 534 QAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
493-726 |
4.94e-75 |
|
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: 242.13 E-value: 4.94e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 493 GLVKFQDVSFAY-PNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT 571
Cdd:cd03254 1 GEIEFENVNFSYdEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIR 651
Cdd:cd03254 78 MIGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 726
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
218-731 |
2.28e-74 |
|
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: 254.67 E-value: 2.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 218 RNMWLMCILTIASTVL---EFAGDGIYNITMGHMHSRVHGEV----FRAVLHQETGFFLKNPTGSITSRVTEdTSNVCES 290
Cdd:TIGR01846 173 RGLSTLSVLALAMLAVaifEPALGGLRTYLFAHLTSRIDVELgarlYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 291 ISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVR 370
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 371 SFANEEGEAQKFRQKLEemkplnkkealAYVTEVWTMSVSGMLLKVGI-----------LYLGGQLVVRGAVSSGNLVSF 439
Cdd:TIGR01846 332 ATATEPQFQNRWDRQLA-----------AYVAASFRVTNLGNIAGQAIeliqkltfailLWFGAHLVIGGALSPGQLVAF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 440 VLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDrTPCSPLSGSLAPL-NMKGLVKFQDVSFAY-PNHPnvQVLQGLT 517
Cdd:TIGR01846 401 NMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALpELRGAITFENIRFRYaPDSP--EVLSNLN 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 518 FTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTR 597
Cdd:TIGR01846 478 LDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 598 TPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLL 677
Cdd:TIGR01846 558 AP-FEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNM 636
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 56717 678 YESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 731
Cdd:TIGR01846 637 REIC--RGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
495-731 |
2.54e-74 |
|
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: 240.21 E-value: 2.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 654
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 731
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
495-731 |
3.72e-74 |
|
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: 239.82 E-value: 3.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 654
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 731
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
347-733 |
5.36e-71 |
|
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: 242.36 E-value: 5.36e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 347 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA-LAYVTEVWTMSVSGMLLkVGILYLGGQL 425
Cdd:COG4987 186 RLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLArLSALAQALLQLAAGLAV-VAVLWLAAPL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 426 VVRGAVSSGNLVSFVLyqlqFTRAV-EVLLSIYPSMQ---KSVGASEKIFEYLDRTPCSPLSGSLAPLNMKGLVKFQDVS 501
Cdd:COG4987 265 VAAGALSGPLLALLVL----AALALfEALAPLPAAAQhlgRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVS 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 502 FAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPL 581
Cdd:COG4987 341 FRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPH 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 582 LFGRSFRENIAygLTR-TPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDD 660
Cdd:COG4987 420 LFDTTLRENLR--LARpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDE 497
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 661 ATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 733
Cdd:COG4987 498 PTEGLDAATEQALLADLLEA--LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
495-733 |
9.43e-70 |
|
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: 228.52 E-value: 9.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 573
Cdd:cd03252 1 ITFEHVRFRYkPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEPLLFGRSFRENIAygLTRT-PTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 652
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIA--LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMV 732
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
.
gi 56717 733 E 733
Cdd:cd03252 235 Q 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
242-728 |
1.12e-69 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 239.15 E-value: 1.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 242 NITMgHMHSRVhgevFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTV 321
Cdd:PRK11176 95 KVVM-TMRRRL----FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 322 VTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYV 401
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 402 TEVWTMSVSGMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPcSP 481
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ-EK 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 482 LSGSLAPLNMKGLVKFQDVSFAYP--NHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 559
Cdd:PRK11176 329 DEGKRVIERAKGDIEFRNVTFTYPgkEVP---ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 560 PLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQ 639
Cdd:PRK11176 406 DLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHL 719
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHA 563
|
....*....
gi 56717 720 QLMERGGCY 728
Cdd:PRK11176 564 ELLAQNGVY 572
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
192-470 |
8.20e-68 |
|
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: 225.13 E-value: 8.20e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 192 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 271
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 272 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 351
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 352 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 431
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 56717 432 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
495-710 |
6.45e-66 |
|
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: 215.71 E-value: 6.45e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPR 654
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEG 710
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
359-726 |
8.03e-63 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 220.60 E-value: 8.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 359 ALEALSAMPTVRSFANEEGEAQKFRQKLEEMkplnkkeaLAYVTEV--WTMSVSGM------LLKVGILYLGGQLVVRGA 430
Cdd:PRK13657 198 VSDAIGNVSVVQSYNRIEAETQALRDIADNL--------LAAQMPVlsWWALASVLnraastITMLAILVLGAALVQKGQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 431 VSSGNLVSFV-LYQLQFTRaVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPL-NMKGLVKFQDVSFAYPNHP 508
Cdd:PRK13657 270 LRVGEVVAFVgFATLLIGR-LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLgRVKGAVEFDDVSFSYDNSR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 nvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFR 588
Cdd:PRK13657 349 --QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 589 ENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 668
Cdd:PRK13657 427 DNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 669 NQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 726
Cdd:PRK13657 506 TEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
493-716 |
1.85e-58 |
|
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: 197.43 E-value: 1.85e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 493 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 572
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPLLFGRSFRENIAYGLTRTpTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 652
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLA-DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQG 716
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
267-734 |
2.72e-58 |
|
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: 210.37 E-value: 2.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 267 FFLKNPTGSITSRVTeDTSNVCESI-SDKLNLFL--WYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRrlgKVYQS 343
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFK---RTFNK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 344 LAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMkpLNKkeALAYV-TEVWTM---SVSGMLLKVGIL 419
Cdd:TIGR01193 322 LNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDY--LNK--SFKYQkADQGQQaikAVTKLILNVVIL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 420 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFE-YLDRTPCSPLSGSLAPLNMKGLVKFQ 498
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINKKKRTELNNLNGDIVIN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 499 DVSFAYPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQ 578
Cdd:TIGR01193 478 DVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLIL 658
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 659 DDATSALDAgnqLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 734
Cdd:TIGR01193 636 DESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
192-450 |
2.06e-55 |
|
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: 191.32 E-value: 2.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 192 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMC--ILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 269
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPDGDPETQALNVYSLAllLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 349
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 350 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 429
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 56717 430 AVSSGNLVSFVLYQLQFTRAV 450
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
255-739 |
1.49e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 197.63 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 255 EVFRAVLHQETGFFLKNPTGSITSRVTEDTsnvcESISDklnLFLWYLG---RGLCLLAFMIWGSFYLTVVTLLSLPLLF 331
Cdd:PRK10790 103 DVMDAALRQPLSAFDTQPVGQLISRVTNDT----EVIRD---LYVTVVAtvlRSAALIGAMLVAMFSLDWRMALVAIMIF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 332 LLPRRLGKVYQSLAV----KVQESLAKSTQVALEALSAMPTVrsfaneegeaQKFRQKLEEMKPLNKKEALAYVTEVWTM 407
Cdd:PRK10790 176 PAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVI----------QQFRQQARFGERMGEASRSHYMARMQTL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 408 SVSGMLLK-----------VGILYLGGqLVVRGAVSSGNLVSFVLYqlqFTRAVEVL--LSIYPSM-QKSVGASEKIFEY 473
Cdd:PRK10790 246 RLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISY---LGRLNEPLieLTTQQSMlQQAVVAGERVFEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 474 LDRtPCSPLSGSLAPLNmKGLVKFQDVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 553
Cdd:PRK10790 322 MDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 554 VLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGltRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGN 633
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGN 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 634 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVC 713
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQAV 553
|
490 500 510
....*....|....*....|....*....|..
gi 56717 714 EQGTHLQLMERGGCYRSMV------EALAAPS 739
Cdd:PRK10790 554 EQGTHQQLLAAQGRYWQMYqlqlagEELAASV 585
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
412-712 |
4.68e-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: 195.74 E-value: 4.68e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 412 MLLKVGILYLGGQLVVRGAVSSGNLV--SFVLyqlqfTRA---VEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSL 486
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAMIaaSILM-----GRAlapIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 487 -APlnmKGLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD 565
Cdd:COG4618 325 pRP---KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 566 HHYLHTQVAAVGQEPLLFGRSFRENIAygltR--TPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 643
Cdd:COG4618 401 REELGRHIGYLPQDVELFDGTIAENIA----RfgDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRI 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 644 ALARALIRKPRLLILDDATSALD-AGNQLRVQRLLyespEWASR--TVLLITQQLSLAERAHHILFLKEGSV 712
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDdEGEAALAAAIR----ALKARgaTVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
416-734 |
4.79e-53 |
|
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: 193.57 E-value: 4.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 416 VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPL-NMKGL 494
Cdd:TIGR01192 255 MCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELpNVKGA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:TIGR01192 335 VEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGRSFRENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 654
Cdd:TIGR01192 413 TVFQDAGLFNRSIRENIRLGRE-GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 734
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
192-470 |
2.28e-50 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 177.92 E-value: 2.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 192 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVleFAG--DGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 269
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSL--SAGlrGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 349
Cdd:cd18590 89 KTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 350 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 429
Cdd:cd18590 169 DSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 56717 430 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18590 249 HLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
422-731 |
2.06e-49 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 182.60 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 422 GGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSpLSGSLAPLNMKGLVKFQDVS 501
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEGRGELDVNIRQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 502 FAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPL 581
Cdd:PRK10789 321 FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 582 LFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDA 661
Cdd:PRK10789 400 LFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 662 TSALDAGNQlrvQRLLYESPEW-ASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 731
Cdd:PRK10789 479 LSAVDGRTE---HQILHNLRQWgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
464-707 |
1.05e-48 |
|
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: 179.79 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 464 VGASEKIFEYLDRT--PCSPLSGSLAPLNMKglVKFQDVSFAYPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAA 541
Cdd:TIGR02857 291 VAAAEALFAVLDAAprPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 542 LLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFP 621
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 622 QGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERA 701
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
....*.
gi 56717 702 HHILFL 707
Cdd:TIGR02857 524 DRIVVL 529
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
412-717 |
2.96e-48 |
|
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: 179.08 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 412 MLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAplNM 491
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLP--EP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 492 KGLVKFQDVSFAYPNhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT 571
Cdd:TIGR01842 314 EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFGRSFRENIAYgLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIR 651
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 652 KPRLLILDDATSALD-AGNQLRVQRLLyeSPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDeEGEQALANAIK--ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
493-717 |
4.86e-46 |
|
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: 163.43 E-value: 4.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 493 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 572
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPLLFGRSFRENIAygltrtP----TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARA 648
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 649 LIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLItqqlslaerAHH---------ILFLKEGSVCEQGT 717
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTI---------AHRldtiidsdrILVLDKGRVVEFDS 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
494-717 |
5.58e-45 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 161.75 E-value: 5.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 573
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEPLL-FGRSFRENIAYGltRTPTM----------EEITAVAMES-GAHDFIsgfpqgyDTEVgetgNQLSGGQRQ 641
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALG--RYPHLglfgrpsaedREAVEEALERtGLEHLA-------DRPV----DELSGGERQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 642 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
513-663 |
2.26e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 156.27 E-value: 2.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 513 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGR-SFRENI 591
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 592 AYGLtrtpTMEEITAVAMESGAHDFISGFPQGY--DTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 663
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
495-717 |
6.34e-44 |
|
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: 157.88 E-value: 6.34e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPL--LFGRSFRENIAYGLTRT----PTMEEITAVAMES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 647
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLglprEEIRERVEEALELvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 648 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
457-731 |
3.89e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 165.02 E-value: 3.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 457 YPSMQKSVGASEKIFEYLDrTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGK 536
Cdd:PRK11174 311 YHAKAQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 537 ST-VAALLQNL-YQptgGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGltrTPTM--EEITAVAMESG 612
Cdd:PRK11174 390 TSlLNALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG---NPDAsdEQLQQALENAW 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 613 AHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLIT 692
Cdd:PRK11174 464 VSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVT 541
|
250 260 270
....*....|....*....|....*....|....*....
gi 56717 693 QQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 731
Cdd:PRK11174 542 HQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
377-735 |
9.05e-43 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 163.84 E-value: 9.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 377 GEAQKFRQKLE--EMKPLNKKEALAYVTEVWT---MSVSGMLLkVGILYLGGQLVvRGAVSSGNLVS-FVLYQLQftrAV 450
Cdd:PRK11160 217 GAEDRYRQQLEqtEQQWLAAQRRQANLTGLSQalmILANGLTV-VLMLWLAAGGV-GGNAQPGALIAlFVFAALA---AF 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 451 EVLLSIYPSMQ---KSVGASEKIFEYLDRTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTA 527
Cdd:PRK11160 292 EALMPVAGAFQhlgQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 528 LVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTrTPTMEEITAV 607
Cdd:PRK11160 371 LLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEV 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 608 AMESGAHDFISGfPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPewASRT 687
Cdd:PRK11160 450 LQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKT 526
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 56717 688 VLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEAL 735
Cdd:PRK11160 527 VLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
410-695 |
1.70e-42 |
|
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: 162.14 E-value: 1.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 410 SGMLLKVGILYLGGQLVVRGAVSSGN-----LVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLD-----RTPC 479
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRlapvtLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDaagpvAEGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 480 SPLSGSLAPlnMKGLVKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 559
Cdd:TIGR02868 322 APAAGAVGL--GKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 560 PLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQ 639
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGE 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQL 695
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
494-716 |
1.39e-41 |
|
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: 151.50 E-value: 1.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH---YL 569
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQEPLL-------FGRSFRE--NIAYGLTRTPTMEEITAVAMESG--AHDFISGFPqgydtevgetgNQLSGG 638
Cdd:cd03257 81 RKEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVglPEEVLNRYP-----------HELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
496-710 |
6.72e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.81 E-value: 6.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAA 575
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 VGQEPLLFGRSFRENIAYGLT---RTPTMEEITAvAMESgahdFisGFPQGY-DTEVGEtgnqLSGGQRQAVALARALIR 651
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQlreRKFDRERALE-LLER----L--GLPPDIlDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 710
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
495-711 |
1.09e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 148.00 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYP--NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLyQPTGGKVlldgeplvqydhhYLHT 571
Cdd:cd03250 1 ISVEDASFTWDsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFGRSFRENIAYGLTRTPTMEE--ITAVAMESgahDfISGFPQGYDTEVGETGNQLSGGQRQAVALARAL 649
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEERYEkvIKACALEP---D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 650 IRKPRLLILDDATSALDAgnqlRVQRLLYES---PEWA-SRTVLLITQQLSLAERAHHILFLKEGS 711
Cdd:cd03250 143 YSDADIYLLDDPLSAVDA----HVGRHIFENcilGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
495-724 |
9.03e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 146.36 E-value: 9.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYLHTQVA 574
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGR-SFRENI-----AYGLTRTPTMEEI----TAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 644
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIdellELFGLTDAADRKVG---------------TLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 723
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
.
gi 56717 724 R 724
Cdd:COG1131 221 R 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
490-733 |
9.72e-40 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 158.27 E-value: 9.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY------------QPTG------ 551
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 552 ------------------------------------GKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGl 595
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 596 TRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQR 675
Cdd:PTZ00265 1320 KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 676 LLYESPEWASRTVLLITQQLSLAERAHHILFL----KEGS-VCEQGTHLQLME-RGGCYRSMVE 733
Cdd:PTZ00265 1400 TIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
494-717 |
1.98e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 146.10 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 572
Cdd:COG1124 1 MLEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPLL-------FGRSFREniAYGLTRTPTMEEITAVAMES-G-AHDFISGFPqgydtevgetgNQLSGGQRQAV 643
Cdd:COG1124 81 VQMVFQDPYAslhprhtVDRILAE--PLRIHGLPDREERIAELLEQvGlPPSFLDRYP-----------HQLSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
495-700 |
3.00e-39 |
|
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: 144.54 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPN-HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQydhhyLHTQV 573
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEPLLFG-RSFRENIAYGLT-RTPTMEEITAVAMES----GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 647
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElQGVPKAEARERAEELlelvGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 648 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS----LAER 700
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeavfLADR 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
491-724 |
7.23e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.21 E-value: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG---GKVLLDGEPLVQYDHH 567
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQVAAVGQEPL--LFGRSFRENIAYGL-TRTPTMEEITAVAMES----GAHDFISGFPQgydtevgetgnQLSGGQR 640
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALeNLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 641 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGTHL 719
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPE 228
|
....*
gi 56717 720 QLMER 724
Cdd:COG1123 229 EILAA 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
498-716 |
1.82e-38 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 141.03 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVG 577
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QepllfgrsfreniaygltrtptmeeitavAMES-GAHDFIsgfPQGYDTevgetgnqLSGGQRQAVALARALIRKPRLL 656
Cdd:cd03214 80 Q-----------------------------ALELlGLAHLA---DRPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 657 ILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
465-717 |
2.05e-38 |
|
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: 150.05 E-value: 2.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 465 GASEKIFEYLDRTPCSPLSGSLAPLNMKG------LVKFQDVSFAYPNHPN--VQVLQGLTFTLYPGKVTALVGPNGSGK 536
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAaaaaepLLEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 537 STVAALLQNLYQPTGGKVLLDGEPLVQYDH---HYLHTQVAAVGQEPL--LFGR-SFRENIAYGLT--RTPTMEEITAVA 608
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNPRmTVGDIIAEPLRlhGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 609 MES----G-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEW 683
Cdd:COG1123 385 AELlervGlPPDLADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRE 453
|
250 260 270
....*....|....*....|....*....|....*
gi 56717 684 ASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG1123 454 LGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
194-470 |
2.44e-38 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 144.19 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKT-APSFARNMW-----LMCILTIAS-------TVLEFAGDGIYNitmghmhsRVHGEVFRAV 260
Cdd:cd18573 13 MSVPFAIGKLIDVASKESGdIEIFGLSLKtfalaLLGVFVVGAaanfgrvYLLRIAGERIVA--------RLRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 261 LHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 340
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 341 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILY 420
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 56717 421 LGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
498-712 |
3.77e-38 |
|
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: 139.66 E-value: 3.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVG 577
Cdd:cd03246 4 ENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLI 657
Cdd:cd03246 83 QDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 56717 658 LDDATSALDAGNQLRVQRLLyESPEWASRTVLLITQQLSLAERAHHILFLKEGSV 712
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
494-726 |
5.38e-38 |
|
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: 141.92 E-value: 5.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLhTQV 573
Cdd:COG4555 1 MIEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRK 652
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYespEWAS--RTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERGG 726
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILR---ALKKegKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
496-710 |
1.25e-37 |
|
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: 139.52 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAA 575
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 VGQEP--LLFGRSFRENIAYGL----TRTPTMEEITAVAMEsgahdfisgfpqgydtEVGETG------NQLSGGQRQAV 643
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLenlgLPEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEG 710
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
255-707 |
1.33e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 151.72 E-value: 1.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 255 EVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDK-----------LNLFLWYLGRGlCLLAFMIWGSFYLTVVT 323
Cdd:PTZ00265 135 EFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKfitiftyasafLGLYIWSLFKN-ARLTLCITCVFPLIYIC 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 324 LLSLPLLFLLPRRLGKVYQSLAVKVQEslakstqvalEALSAMPTVRSFANEEGEAQKFrqKLEEmKPLNKKEALAYVTE 403
Cdd:PTZ00265 214 GVICNKKVKINKKTSLLYNNNTMSIIE----------EALVGIRTVVSYCGEKTILKKF--NLSE-KLYSKYILKANFME 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 404 VWTMS-VSGMLL---KVGILYlGGQLVVRGAVSS--------GNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIF 471
Cdd:PTZ00265 281 SLHIGmINGFILasyAFGFWY-GTRIIISDLSNQqpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 472 EYLDRTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG 551
Cdd:PTZ00265 360 EIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 552 GKVLL-DGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTME---------------------------- 602
Cdd:PTZ00265 440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakca 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 603 ----------------------------EITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 654
Cdd:PTZ00265 520 gdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFL 707
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
247-734 |
2.96e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 150.51 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 247 HMHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLF---LWYLgrglcLLAFMIWGSfyLTVVT 323
Cdd:PLN03232 980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqLWQL-----LSTFALIGT--VSTIS 1052
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 324 LLSLPLLFLLPRRLGKVYQSLAVKVQ--ESLAKSTQVAL--EALSAMPTVRSFaneegeaqkfrQKLEEMKPLNKKEALA 399
Cdd:PLN03232 1053 LWAIMPLLILFYAAYLYYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY-----------KAYDRMAKINGKSMDN 1121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 400 YVTEVWTMSVSGMLLKVGILYLGGQLV-------VRGAVSSGNLVSF-------VLYQLQFTRAVEVLLSIYPSMQKSVG 465
Cdd:PLN03232 1122 NIRFTLANTSSNRWLTIRLETLGGVMIwltatfaVLRNGNAENQAGFastmgllLSYTLNITTLLSGVLRQASKAENSLN 1201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 466 ASEKIFEYLD------------RTPCS-PLSGSlaplnmkglVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGP 531
Cdd:PLN03232 1202 SVERVGNYIDlpseataiiennRPVSGwPSRGS---------IKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGR 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 532 NGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIaygltrTPTMEEITAVAMES 611
Cdd:PLN03232 1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDADLWEA 1344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 612 --GAH--DFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRT 687
Cdd:PLN03232 1345 leRAHikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCT 1422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 56717 688 VLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMER-GGCYRSMVEA 734
Cdd:PLN03232 1423 MLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRdTSAFFRMVHS 1470
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
491-692 |
4.23e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 4.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQydhhyL 569
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQEPLLFG-RSFRENIAYGL-TRTPTMEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAV 643
Cdd:COG1116 79 GPDRGVVFQEPALLPwLTVLDNVALGLeLRGVPKAERRERARELlelvGLAGFEDAYP-----------HQLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWAS--RTVLLIT 692
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLR--LWQEtgKTVLFVT 196
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
495-710 |
5.30e-37 |
|
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: 138.01 E-value: 5.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYP-NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH----HYL 569
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQEP-LLFGRSFRENIAYGL----TRTPTMEE-----ITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQ 639
Cdd:cd03255 81 RRHIGFVFQSFnLLPDLTALENVELPLllagVPKKERREraeelLERVGLGDRLNHYPS---------------ELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 710
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
496-710 |
7.68e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 135.45 E-value: 7.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAA 575
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 VGQepllfgrsfreniaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRL 655
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 656 LILDDATSALDAGNQLRVQRLLYESPEWAsRTVLLITQQLSLAERA-HHILFLKEG 710
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
495-716 |
5.96e-36 |
|
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: 135.39 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY-----QPTGGKVLLDGEPL--VQYDHH 567
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQVAAVGQEPLLFGRSFRENIAYGLT-----RTPTMEEITAVAMESGahdfisgfpqGYDTEVGE--TGNQLSGGQR 640
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKA----------ALWDEVKDrlHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 641 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
497-716 |
2.20e-35 |
|
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: 132.05 E-value: 2.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 497 FQDVSFAYPnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHyLHTQVAAV 576
Cdd:cd03247 3 INNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 577 GQEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetGNQLSGGQRQAVALARALIRKPRLL 656
Cdd:cd03247 81 NQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 657 ILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQG 716
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
251-731 |
6.00e-35 |
|
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: 143.55 E-value: 6.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 251 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 330
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLY 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 331 FLLPRRLgkVYQSLAVKVQESLAKSTQVAL--EALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVtevwtms 408
Cdd:TIGR00957 1119 FFVQRFY--VASSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSI------- 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 409 VSGMLLKVGILYLGGQLVV---------RGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPC 479
Cdd:TIGR00957 1186 VANRWLAVRLECVGNCIVLfaalfavisRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 480 SP--LSGSLAPLNM--KGLVKFQDVSFAYpnHPNVQ-VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV 554
Cdd:TIGR00957 1266 APwqIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 555 LLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI----AYGltrtptmEEITAVAME-SGAHDFISGFPQGYDTEVG 629
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYS-------DEEVWWALElAHLKTFVSALPDKLDHECA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 630 ETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyeSPEWASRTVLLITQQLSLAERAHHILFLKE 709
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDYTRVIVLDK 1494
|
490 500
....*....|....*....|..
gi 56717 710 GSVCEQGTHLQLMERGGCYRSM 731
Cdd:TIGR00957 1495 GEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
193-470 |
2.80e-34 |
|
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: 132.67 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 193 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNP 272
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 273 TGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESL 352
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 353 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKealAYVTEVWTMSVSGMLLKVG---ILYLGGQLVVRG 429
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR---AARLSALFSPLIGLLTALGtalVLLYGGYLVLQG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 56717 430 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd07346 252 SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
491-710 |
4.49e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 130.16 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKST---VAALLQnlyQPTGGKVLLDGEPLVQYDH 566
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLD---RPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 567 hylhTQVAA--------VGQEPLLFGR-SFRENIAY-----GLTRTPTMEEITAVAMESGAHDFISGFPqgydtevgetg 632
Cdd:COG1136 78 ----RELARlrrrhigfVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRP----------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 633 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 710
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
194-470 |
5.51e-34 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 131.99 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKTAPSFARN-------MWLMCILTIAST-------VLEFAGDGIYnitmghmhSRVHGEVFRA 259
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEALralnqavLILLGVVLIGSIatflrswLFTLAGERVV--------ARLRKRLFSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 260 VLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGK 339
Cdd:cd18780 85 IIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 340 VYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGIL 419
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 56717 420 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18780 245 WYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
490-714 |
2.58e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 128.28 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKST-VAALLqNLYQPTGGKVLLDGEPLVQYDHHy 568
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 lhtqVAAVGQEpLLFGRSF----RENIAYGLT------RTPTMEEITAV--AMES-GAHDFIsgfpqgyDTEVGEtgnqL 635
Cdd:COG1121 77 ----IGYVPQR-AEVDWDFpitvRDVVLMGRYgrrglfRRPSRADREAVdeALERvGLEDLA-------DRPIGE----L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 636 SGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYespEWAS--RTVLLITQQLSLAER-AHHILFLKEGSV 712
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR---ELRRegKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
..
gi 56717 713 CE 714
Cdd:COG1121 218 AH 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
495-712 |
4.70e-33 |
|
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: 125.20 E-value: 4.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHtQVA 574
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGR-SFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnQLSGGQRQAVALARALIRKP 653
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 654 RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSV 712
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
495-710 |
5.35e-33 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 125.38 E-value: 5.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY--LHTQ 572
Cdd:cd03229 1 LELKNVSKRYGQK---TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPLLF-GRSFRENIAYGLtrtptmeeitavamesgahdfisgfpqgydtevgetgnqlSGGQRQAVALARALIR 651
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALGL----------------------------------------SGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 710
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
495-716 |
5.14e-32 |
|
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: 123.78 E-value: 5.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylHTQVA 574
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLF-GRSFRENIAYGLT-RTPTMEEITAVAMESGAHDFISGFPQGYDTEvgetgnqLSGGQRQAVALARALIRK 652
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKlRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
499-712 |
7.63e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.75 E-value: 7.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 499 DVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDhhyLHTQVAAVGQ 578
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EP--LLFGRSFRENIAYGLTRTPTMEEITAVAMES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPRL 655
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 656 LILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSV 712
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
495-717 |
2.11e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 123.69 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG-EPLVQYDHHYLHTQV 573
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEP--LLFGRSFRENIAYGL----TRTPTMEEI-----TAVAMEsgahDFISGFPQgydtevgetgnQLSGGQRQA 642
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLenlgVPREEMRKRvdealKLVGME----DFRDREPH-----------LLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 643 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
490-717 |
7.36e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 7.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 569
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQEP--LLFGRSFRENIAYGL-----TRTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQA 642
Cdd:PRK13632 82 RKKIGIIFQNPdnQFIGATVEDDIAFGLenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 643 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
491-717 |
2.39e-30 |
|
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: 119.70 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 570
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVG---QEPLLFGrSF--RENIAYGLTRTPTM--EEITAVAME-------SGAHDFisgFPqgydtevgetgNQLS 636
Cdd:COG1127 79 ELRRRIGmlfQGGALFD-SLtvFENVAFPLREHTDLseAEIRELVLEklelvglPGAADK---MP-----------SELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 637 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQ 715
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
..
gi 56717 716 GT 717
Cdd:COG1127 224 GT 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
511-717 |
3.82e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.84 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQE-PLLFGRSFRE 589
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHsSLAFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 590 NIAYGLTRTPTM----EEITAVAME-SGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALI-------RKPRLLI 657
Cdd:COG4559 95 VVALGRAPHGSSaaqdRQIVREALAlVGLAHLAGRSYQ-----------TLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 658 LDDATSALDAGNQLRVQRLLYespEWASR--TVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLAR---QLARRggGVVAVLHDLNLAAQyADRILLLHQGRLVAQGT 223
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
494-721 |
4.47e-30 |
|
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: 118.84 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 572
Cdd:cd03258 1 MIELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVG----QEPLLFGRSFRENIAYGL--TRTPtMEEITAVAME----SGAHDFISGFPqgydtevgetgNQLSGGQRQA 642
Cdd:cd03258 81 RRRIGmifqHFNLLSSRTVFENVALPLeiAGVP-KAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 643 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQL 721
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
490-725 |
6.63e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 119.73 E-value: 6.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 569
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQEP--LLFGRSFRENIAYGL-----TRTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQA 642
Cdd:PRK13635 80 RRQVGMVFQNPdnQFVGATVQDDVAFGLenigvPREEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 643 VALARALIRKPRLLILDDATSALD-AGNQ--LRVQRLLYESpewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHL 719
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDpRGRRevLETVRQLKEQ---KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*.
gi 56717 720 QLMERG 725
Cdd:PRK13635 226 EIFKSG 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
251-737 |
7.02e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 127.55 E-value: 7.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 251 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFL---WYLGRGLCLLAFM----IWGSFYLTVVT 323
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqiFQLLSTFVLIGIVstisLWAIMPLLVLF 1066
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 324 LLSLPLlfllprrlgkvYQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFaneegeaqkfrQKLEEMKPLNKK--EA 397
Cdd:PLN03130 1067 YGAYLY-----------YQSTAreVKRLDSITRSPVYAQfgEALNGLSTIRAY-----------KAYDRMAEINGRsmDN 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 398 LAYVTEVwTMSvSGMLLKVGILYLGG-------QLVVRGAVSSGNLVSF-------VLYQLQFTRAVEVLLSIYPSMQKS 463
Cdd:PLN03130 1125 NIRFTLV-NMS-SNRWLAIRLETLGGlmiwltaSFAVMQNGRAENQAAFastmgllLSYALNITSLLTAVLRLASLAENS 1202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 464 VGASEKIFEYLD------------RTPCS-PLSGSlaplnmkglVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALV 529
Cdd:PLN03130 1203 LNAVERVGTYIDlpseaplviennRPPPGwPSSGS---------IKFEDVVLRYrPELP--PVLHGLSFEISPSEKVGIV 1271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 530 GPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIaygltrTPTMEEITAVAM 609
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLW 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 610 ES--GAH--DFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWAS 685
Cdd:PLN03130 1346 ESleRAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKS 1423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 56717 686 RTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL-MERGGCYRSMVEALAA 737
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQSTGA 1476
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
495-717 |
1.17e-29 |
|
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: 117.60 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEP---LVQYDHHYLHT 571
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFGR-SFRENIAYGLTRTPTM--EEITAVAME-------SGAHDFisgFPqgydtevgetgNQLSGGQRQ 641
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREIVLEkleavglRGAEDL---YP-----------AELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 642 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
494-717 |
1.49e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.40 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH--YLHT 571
Cdd:COG1126 1 MIEIENLHKSFGDL---EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFG-RSFRENIAYGLTRTPTM--EEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVA 644
Cdd:COG1126 78 KVGMVFQQFNLFPhLTVLENVTLAPIKVKKMskAEAEERAMELlervGLADKADAYP-----------AQLSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 645 LARALIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelVGEVLDVMRDLAKE----GMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
194-470 |
3.26e-29 |
|
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: 117.97 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 273
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 274 GSITSRVTEDTSNVCESISDKLNLFLwylgRGLCLL----AFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 349
Cdd:cd18576 93 GELTSRLSNDVTQIQDTLTTTLAEFL----RQILTLiggvVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 350 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 429
Cdd:cd18576 169 DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 56717 430 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18576 249 ELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
491-717 |
3.58e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.43 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydhhylh 570
Cdd:COG3842 2 AMPALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAA----VG---QEPLLFG-RSFRENIAYGLT-RTPTMEEITA--------VAMESGAHDFISgfpqgydtevgetgn 633
Cdd:COG3842 70 TGLPPekrnVGmvfQDYALFPhLTVAENVAFGLRmRGVPKAEIRArvaellelVGLEGLADRYPH--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 634 QLSGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRVQ------RLLYESPewasRTVLLIT--QQ--LSLAERahh 703
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDA--KLREEmreelrRLQRELG----ITFIYVThdQEeaLALADR--- 205
|
250
....*....|....
gi 56717 704 ILFLKEGSVCEQGT 717
Cdd:COG3842 206 IAVMNDGRIEQVGT 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
489-667 |
4.65e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 4.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydhHY 568
Cdd:COG1129 5 LEMRGISK----SF-----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-----RF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 LHTQ------VAAVGQEPLLF-GRSFRENIA-------YGLTRTPTMEEITAVAMES-GAHdfISgfPqgyDTEVGEtgn 633
Cdd:COG1129 71 RSPRdaqaagIAIIHQELNLVpNLSVAENIFlgreprrGGLIDWRAMRRRARELLARlGLD--ID--P---DTPVGD--- 140
|
170 180 190
....*....|....*....|....*....|....
gi 56717 634 qLSGGQRQAVALARALIRKPRLLILDDATSALDA 667
Cdd:COG1129 141 -LSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
498-717 |
5.02e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.71 E-value: 5.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEpLVQYDHHYLHTQVAAVG 577
Cdd:COG1118 6 RNISKRFGS---FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR-DLFTNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QEPLLFgR--SFRENIAYGLT-RTPTMEEITAVAME----SGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALI 650
Cdd:COG1118 82 QHYALF-PhmTVAENIAFGLRvRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 651 RKPRLLILDDATSALDAgnQLRVQ------RLLYESPewasRTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 717
Cdd:COG1118 150 VEPEVLLLDEPFGALDA--KVRKElrrwlrRLHDELG----GTTVFVTHDQEEAlELADRVVVMNQGRIEQVGT 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
496-713 |
5.08e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.94 E-value: 5.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHhylhtQVAA 575
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 VGQEpLLFGRSF----RENIAYGLTRTPTM-------------EEITAVAMESGAHDFISgfpqgydtevgetgnQLSGG 638
Cdd:cd03235 73 VPQR-RSIDRDFpisvRDVVLMGLYGHKGLfrrlskadkakvdEALERVGLSELADRQIG---------------ELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyesPEWAS--RTVLLITQQLSLAER-AHHILFLKEGSVC 713
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL---RELRRegMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
495-714 |
6.86e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.15 E-value: 6.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLY---QPTGGKVLLDGEPLVQYDHH---Y 568
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 LHTQVAAVGQE-PLLFGRSFRENIAY-----GLTRTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQA 642
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 643 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspewASR---TVLLITQQLSLAERAHH-ILFLKEGSVCE 714
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE----INRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
494-704 |
6.90e-29 |
|
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: 114.50 E-value: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQPTGGKVLLDGEPLVQYDHHYlH 570
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT---LLRilaGLLPPSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQEPLLFGR-SFRENIA-----YGLTRTPT--MEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQA 642
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRfwaalYGLRADREaiDEALEAVGLAGLADLPVR---------------QLSAGQKRR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 643 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLyesPEWASR--TVLLITQQLSLAERAHHI 704
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELI---AAHLARggAVLLTTHQPLELAAARVL 200
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
495-710 |
1.53e-28 |
|
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: 113.78 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ--YDHHYLHTQ 572
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPLLFG-RSFRENIAYGLTRTPTM--EEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVAL 645
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKGMskAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 646 ARALIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLA-ERAHHILFLKEG 710
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
495-722 |
2.83e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.34 E-value: 2.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:PRK11231 3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLL-FGRSFRENIAYGltRTPTM----------EEITAVAMEsgahdfisgfpqgyDTEVGETGNQ----LSGGQ 639
Cdd:PRK11231 80 LLPQHHLTpEGITVRELVAYG--RSPWLslwgrlsaedNARVNQAME--------------QTRINHLADRrltdLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTH 718
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTP 222
|
....
gi 56717 719 LQLM 722
Cdd:PRK11231 223 EEVM 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
511-717 |
2.21e-27 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLL-FGRSFRE 589
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 590 NIAYGLT----RTPTMEEITAVAMESgahdfisgfpqgydTEVGETGN----QLSGGQRQAVALARALIR------KPRL 655
Cdd:PRK13548 96 VVAMGRAphglSRAEDDALVAAALAQ--------------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 656 LILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGT 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
495-722 |
2.60e-27 |
|
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: 111.24 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLF-GRSFRENIAYGLT---------RTPTMEEITAVAMESGahdfisGFPQGYDtevgetgNQLSGGQRQAVA 644
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKllkwpkekiRERADELLALVGLDPA------EFADRYP-------HELSGGQQQRVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 722
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
493-717 |
3.32e-27 |
|
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: 109.81 E-value: 3.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 493 GLVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT 571
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFGRSFRENI-AYGLTrtpTMEEITAVamesgahdfisgfpqgydTEVGETGNQLSGGQRQAVALARALI 650
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEY---SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 651 RKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
495-724 |
5.20e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 5.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGEPLVQYDHHYLHT 571
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEP--LLFGRSFRENIAYGLTRT----PTMEEITA-VAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 644
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRavprPEMIKIVRdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMER 724
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
194-470 |
9.34e-27 |
|
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: 111.03 E-value: 9.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFT---GRITD----WILQDKTAPSF----ARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLH 262
Cdd:cd18577 13 AALPLMTivfGDLFDaftdFGSGESSPDEFlddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 263 QETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFmiwgSFY----LTVVTLLSLPLLFLLPRRLG 338
Cdd:cd18577 93 QDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFII----AFIyswkLTLVLLATLPLIAIVGGIMG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 339 KVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGI 418
Cdd:cd18577 169 KLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALA 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 56717 419 LYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18577 249 FWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
510-723 |
2.07e-26 |
|
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: 107.91 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqyDHHYLHTQVAA----VGQEPLLFGR 585
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPPHERARAgigyVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 -SFRENI---AYGLTR---TPTMEEITAVamesgahdfisgFP---QGYDTEVGetgnQLSGGQRQAVALARALIRKPRL 655
Cdd:cd03224 90 lTVEENLllgAYARRRakrKARLERVYEL------------FPrlkERRKQLAG----TLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 656 LILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLITQQLSLA-ERAHHILFLKEGSVCEQGTHLQLME 723
Cdd:cd03224 154 LLLDEPSEGLapkiveeifEAIRELRDEGV----------TILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
500-724 |
2.24e-26 |
|
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: 110.53 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 500 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGEPLVQYDH----HYLHTQ 572
Cdd:COG0444 9 VYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrKIRGRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPL-----LF--GRSFRENIAY--GLTRtptmEEITAVAME-------SGAHDFISGFPqgydtevgetgNQLS 636
Cdd:COG0444 88 IQMIFQDPMtslnpVMtvGDQIAEPLRIhgGLSK----AEARERAIEllervglPDPERRLDRYP-----------HELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 637 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQ 715
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVvAEIADRVAVMYAGRIVEE 232
|
....*....
gi 56717 716 GTHLQLMER 724
Cdd:COG0444 233 GPVEELFEN 241
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
495-717 |
3.47e-26 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 107.81 E-value: 3.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQydHHYLHTQVA 574
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFI-----SGFPQGYDtevgetgNQLSGGQRQAVALARA 648
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 649 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 717
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
517-723 |
3.75e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 108.50 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 517 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL----HTQVAAVGQEPLLF-GRSFRENI 591
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGL-TRTPTMEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:cd03294 124 AFGLeVQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 667 AGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 723
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
496-712 |
5.78e-26 |
|
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: 107.27 E-value: 5.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT---Q 572
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPLLFGR-SFRENIAYG-LTRTPTM---------EEI-------TAVAMESGAHDFISgfpqgydtevgetgnQ 634
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGrLGRRSTWrslfglfpkEEKqralaalERVGLLDKAYQRAD---------------Q 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 635 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSV 712
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
495-724 |
7.55e-26 |
|
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: 106.55 E-value: 7.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylHTQVA 574
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGR-SFRENIAYGLTRTPT---------MEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 644
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKKLpkaeikervAEALDLVQLEGYANRKPS---------------QLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 645 LARALIRKPRLLILDDATSALDAgnQLRvQRLLYESPEWASR---TVLLIT--QQ--LSLAERahhILFLKEGSVCEQGT 717
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDL--KLR-KDMQLELKRLQKElgiTFVFVThdQEeaLTMSDR---IAVMNKGKIQQIGT 214
|
....*..
gi 56717 718 HLQLMER 724
Cdd:cd03300 215 PEEIYEE 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
491-721 |
1.47e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 570
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQEP--LLFGRSFRENIAYGLT-----RTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAV 643
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 721
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
522-716 |
1.52e-25 |
|
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: 105.07 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 522 PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH-YLHTQVAAVG---QEPLLFGR-SFRENIAYGLT 596
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGlvfQQYALFPHlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 597 RTPTMEEITAVAMESGAHDfISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRL 676
Cdd:cd03297 102 RKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 56717 677 LYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
494-717 |
1.68e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.76 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYpNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 573
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEP--LLFGRSFRENIAYGLTR----TPTMEEITAVAMES-GAHDFISGFPQGydtevgetgnqLSGGQRQAVALA 646
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLENhavpYDEMHRRVSEALKQvDMLERADYEPNA-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 647 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
498-723 |
2.35e-25 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 106.03 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVG 577
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QE-PLLFGRSFRENIAYG-------------LTRTPTMEEITAVAMESGAHDFIsgfpqgydtevgetgNQLSGGQRQAV 643
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGrypwhgalgrfgaADREKVEEAISLVGLKPLAHRLV---------------DSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 722
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 56717 723 E 723
Cdd:PRK10575 237 R 237
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
195-470 |
4.25e-25 |
|
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: 105.97 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDWILQDKTApsfaRNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRV----HGEVFRAVLHQETGFFLK 270
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDL----EALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVvrdlRNDLFDKLLRLPLSFFDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 271 NPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQE 350
Cdd:cd18552 93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 351 SLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKPLNKKEALAYVTEVwtMSVSGMllkVGILYLGGQL 425
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERlrrlsMKIARARALSSPLMEL--LGAIAI---ALVLWYGGYQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 56717 426 VVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18552 248 VISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
510-724 |
5.41e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 109.77 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQnLyQPTGGKVLLDGEPLVQYDHHYL-----HTQVaaVGQEPllF 583
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPSEGEIRFDGQDLDGLSRRALrplrrRMQV--VFQDP--F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 584 G-----RSFRENIAYGLT---RTPTMEEITAVAMESGAhdfisgfpqgydtEVG---ETGN----QLSGGQRQAVALARA 648
Cdd:COG4172 373 GslsprMTVGQIIAEGLRvhgPGLSAAERRARVAEALE-------------EVGldpAARHryphEFSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 649 LIRKPRLLILDDATSALDAGNQLRVQRLL----------YespewasrtvLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQILDLLrdlqrehglaY----------LFISHDLAVVRAlAHRVMVMKDGKVVEQGP 509
|
....*..
gi 56717 718 HLQLMER 724
Cdd:COG4172 510 TEQVFDA 516
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
499-717 |
7.74e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 499 DVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvQYDHHYL---HTQVAA 575
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 VGQEP--LLFGRSFRENIAYG-LTRTPTMEEITAVAMESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALARALIRK 652
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFEN-------KPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGT 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
510-710 |
9.65e-25 |
|
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: 103.28 E-value: 9.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAA-----VG----QEP 580
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED----ARARlrarhVGfvfqSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 581 LLFGRSFRENIAYGL-------TRTPTMEEITAVAMESGAHDFisgfPqgydtevgetgNQLSGGQRQAVALARALIRKP 653
Cdd:COG4181 101 LLPTLTALENVMLPLelagrrdARARARALLERVGLGHRLDHY----P-----------AQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 654 RLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 710
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
489-712 |
1.44e-24 |
|
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: 100.58 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhy 568
Cdd:cd03216 1 LELRGITK----RF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 lhtqvaavgqepllfGRSFRENIAYGltrtptmeeITAVamesgaHdfisgfpqgydtevgetgnQLSGGQRQAVALARA 648
Cdd:cd03216 66 ---------------FASPRDARRAG---------IAMV------Y-------------------QLSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 649 LIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLS-LAERAHHILFLKEGSV 712
Cdd:cd03216 97 LARNARLLILDEPTAALTpaeVERLFKVIRRLRAQ----GVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
495-721 |
1.49e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.58 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhHYLHTQVA 574
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--------YSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQE--------PLLFGRSFRENIAY-----GLTRTPTMEEITAVAMESGAHDFIsgfpqgyDTEVGetgnQLSGGQRQ 641
Cdd:cd03263 72 AARQSlgycpqfdALFDELTVREHLRFyarlkGLPKSEIKEEVELLLRVLGLTDKA-------NKRAR----TLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 642 AVALARALIRKPRLLILDDATSALDAgnqlRVQRLLYESPEWA--SRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTH 718
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDP----ASRRAIWDLILEVrkGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSP 216
|
...
gi 56717 719 LQL 721
Cdd:cd03263 217 QEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
510-716 |
2.07e-24 |
|
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: 101.59 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH-----------YLHTQVaavgQ 578
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpeerglYPKMKV----I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EPLLFGRSFReniayGLTRTPTMEEITavamesgahDFISGFpqgydtEVGETGN----QLSGGQRQAVALARALIRKPR 654
Cdd:cd03269 89 DQLVYLAQLK-----GLKKEEARRRID---------EWLERL------ELSEYANkrveELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
496-717 |
2.68e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 102.14 E-value: 2.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNHPnvqvlqgLTFTLY--PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQ- 572
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA----Er 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 -VAAVGQEPLLFGR-SFRENIAYGLTrtPTM-------EEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAV 643
Cdd:COG3840 72 pVSMLFQENNLFPHlTVAQNIGLGLR--PGLkltaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 644 ALARALIRKPRLLILDDATSALDAGnqLRvQRLLYESPEWASR---TVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPA--LR-QEMLDLVDELCRErglTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
494-714 |
5.23e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 102.07 E-value: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPN------HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-- 565
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 566 -HHYLHTQVAAVGQEPL-------LFGRSFRENIAYGLTRTPTMEEITAVAMESG---AHDFISGFPQgydtevgetgnQ 634
Cdd:PRK10419 83 qRKAFRRDIQMVFQDSIsavnprkTVREIIREPLRHLLSLDKAERLARASEMLRAvdlDDSVLDKRPP-----------Q 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 635 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVC 713
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
.
gi 56717 714 E 714
Cdd:PRK10419 232 E 232
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
474-734 |
5.77e-24 |
|
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: 101.91 E-value: 5.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 474 LDRTPCSPLSGslaplnMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 553
Cdd:cd03288 5 ISGSSNSGLVG------LGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 554 VLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRT-PTMEEITAVAMesgAHDFISGFPQGYDTEVGETG 632
Cdd:cd03288 78 IVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTdDRLWEALEIAQ---LKNMVKSLPGGLDAVVTEGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 633 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 712
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
250 260
....*....|....*....|...
gi 56717 713 CEQGTHLQLM-ERGGCYRSMVEA 734
Cdd:cd03288 233 VECDTPENLLaQEDGVFASLVRT 255
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
494-724 |
9.24e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.94 E-value: 9.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG----EPLVqyDHHYL 569
Cdd:PRK09493 1 MIEFKNVSKHFGPT---QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKV--DERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQEPLLFGR-SFRENIAYGLTRT----------PTMEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGG 638
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHlTALENVMFGPLRVrgaskeeaekQARELLAKVGLAERAHHYPS---------------ELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDA---GNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCE 714
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPelrHEVLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAE 216
|
250
....*....|
gi 56717 715 QGTHLQLMER 724
Cdd:PRK09493 217 DGDPQVLIKN 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
361-733 |
2.10e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 106.75 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 361 EALSAMPTVRSFANEegeaQKFRQKL-----EEMKPLNKKEALAYVTEVWTMSVSGM--LLKVGIL-YLGGQLVVRGAVS 432
Cdd:PLN03130 484 EVLAAMDTVKCYAWE----NSFQSKVqtvrdDELSWFRKAQLLSAFNSFILNSIPVLvtVVSFGVFtLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 433 SGNLVS---FVLYQLQ--FTRAVEVLLSIyPSMQKSVGASEKIFeyldrTPCSPLSGSLAPLNMKglvkfqDVSFAYPNH 507
Cdd:PLN03130 560 SLSLFAvlrFPLFMLPnlITQAVNANVSL-KRLEELLLAEERVL-----LPNPPLEPGLPAISIK------NGYFSWDSK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 508 PNVQVLQGLTFTLYPGKVTALVGPNGSGK-STVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRS 586
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNAT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 587 FRENIAYGLTRTPTMEEiTAVAMESGAHDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:PLN03130 695 VRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 667 AgnqlRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 733
Cdd:PLN03130 773 A----HVGRQVFDKcikDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
195-470 |
3.37e-23 |
|
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: 100.20 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDWILQDKtapSFARNMWLMCILTIASTVLEfagdGIYNITMGHMHSRVhgeVFRA-------VLHQETGF 267
Cdd:cd18551 17 AQPLLVKNLIDALSAGG---SSGGLLALLVALFLLQAVLS----ALSSYLLGRTGERV---VLDLrrrlwrrLLRLPVSF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 268 FLKNPTGSITSRVTEDTSNVCESISDKL-NLFLwylgrGLCLL----AFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQ 342
Cdd:cd18551 87 FDRRRSGDLVSRVTNDTTLLRELITSGLpQLVT-----GVLTVvgavVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 343 SLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEAL--AYVTEVWTMSVSGMLLkvGILY 420
Cdd:cd18551 162 KASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKieALIGPLMGLAVQLALL--VVLG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 56717 421 LGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18551 240 VGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
494-717 |
3.48e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.26 E-value: 3.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 573
Cdd:PRK13652 3 LIETRDLCYSYSG--SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEP--LLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR 651
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGT 717
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRIVAYGT 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
495-712 |
3.65e-23 |
|
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: 98.25 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH---YLHT 571
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQE-PLLFGRSFRENIAYGL---------TRTPTMEEITAVAMESGAHDFisgfpqgydtevgetGNQLSGGQRQ 641
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALevtgvppreIRKRVPAALELVGLSHKHRAL---------------PAELSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 642 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyESPEWASRTVLLITQQLSLAER-AHHILFLKEGSV 712
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
499-716 |
3.97e-23 |
|
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: 98.03 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 499 DVSFAYPNHpnvQVLQGLTFTLYPGkVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYLHTQVAAVGQ 578
Cdd:cd03264 5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EPLLFGR-SFRENIAY-----GLTRTPTMEEITAVAMESGAHDFisgfpqgYDTEVGetgnQLSGGQRQAVALARALIRK 652
Cdd:cd03264 80 EFGVYPNfTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLS-LAERAHHILFLKEGSVCEQG 716
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
510-666 |
4.08e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 100.96 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL-----HTQV------AA--- 575
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplrrRMQMvfqdpyASlnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 ---VGQ---EPLLfgrsfreniAYGLTRTPTMEEITAVAMES-G-AHDFISGFPqgydtevgetgNQLSGGQRQAVALAR 647
Cdd:COG4608 111 rmtVGDiiaEPLR---------IHGLASKAERRERVAELLELvGlRPEHADRYP-----------HEFSGGQRQRIGIAR 170
|
170
....*....|....*....
gi 56717 648 ALIRKPRLLILDDATSALD 666
Cdd:COG4608 171 ALALNPKLIVCDEPVSALD 189
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
496-692 |
6.08e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 98.78 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNH-PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL--------VQYDH 566
Cdd:COG4525 5 TVRHVSVRYPGGgQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrgVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 567 HylhtqvaavgqePLLFGRSFRENIAYGL--------TRTPTMEEITA-VAMESGAHDFISgfpqgydtevgetgnQLSG 637
Cdd:COG4525 85 D------------ALLPWLNVLDNVAFGLrlrgvpkaERRARAEELLAlVGLADFARRRIW---------------QLSG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 56717 638 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT 692
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLIT 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
495-716 |
7.76e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 97.29 E-value: 7.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqyDHHYLHTQVA 574
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFG-RSFRENI-----AYGLTRTPTMEEITAVAMESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARA 648
Cdd:cd03268 76 ALIEAPGFYPnLTARENLrllarLLGIRKKRIDEVLDVVGLKDSAKKKVKGF---------------SLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 649 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSVCEQG 716
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
495-717 |
7.78e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 7.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYP-NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 573
Cdd:COG1135 2 IELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVG----QEPLLFGRSFRENIAY-----GLTRtptmEEITAVAME-------SGAHDFisgFPqgydtevgetgNQLSG 637
Cdd:COG1135 82 RKIGmifqHFNLLSSRTVAENVALpleiaGVPK----AEIRKRVAEllelvglSDKADA---YP-----------SQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 638 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspewASR----TVLLITQQLSLAER-AHHILFLKEGSV 712
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD----INRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 56717 713 CEQGT 717
Cdd:COG1135 220 VEQGP 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
512-717 |
1.31e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.19 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ-----------------YDHHYLHTQVA 574
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaelrnqklgfiYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQ--EPLLFGRSFRENIaygltRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVALARALIRK 652
Cdd:PRK11629 104 ALENvaMPLLIGKKKPAEI-----NSRALEMLAAVGLEHRANHRPS---------------ELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
492-674 |
1.31e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.41 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 492 KGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL--VQYDHHYL 569
Cdd:PRK09452 12 SPLVELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTqvaaVGQEPLLFGR-SFRENIAYGL--TRTPTmEEITAVAMESGA----HDFISGFPQgydtevgetgnQLSGGQRQA 642
Cdd:PRK09452 89 NT----VFQSYALFPHmTVFENVAFGLrmQKTPA-AEITPRVMEALRmvqlEEFAQRKPH-----------QLSGGQQQR 152
|
170 180 190
....*....|....*....|....*....|..
gi 56717 643 VALARALIRKPRLLILDDATSALDAgnQLRVQ 674
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDY--KLRKQ 182
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
495-716 |
1.37e-22 |
|
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: 96.41 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAY---PNHPNVQVLQGltftlypgKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHYLHT 571
Cdd:cd03298 1 VRLDKIRFSYgeqPMHFDLTFAQG--------EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAPP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 Q---VAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALAR 647
Cdd:cd03298 68 AdrpVSMLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 648 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
270-733 |
1.59e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.90 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KN-PTGSITSRVTEDtSNVCESISDKLNlFLWylGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 348
Cdd:PLN03232 393 KNfASGKVTNMITTD-ANALQQIAEQLH-GLW--SAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLT 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 349 QESLA---KSTQVALEALSAMPTVRSFANE---EGEAQKFRQklEEMKPLNKKEALAYVTE--VWTMSVSGMLLKVGI-L 419
Cdd:PLN03232 469 KEGLQwtdKRVGIINEILASMDTVKCYAWEksfESRIQGIRN--EELSWFRKAQLLSAFNSfiLNSIPVVVTLVSFGVfV 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 420 YLGGQLVVRGAVSSGNLVSFVLYQLQFtraVEVLLSIYPSMQKSVGASEKIFEYLDR--TPCSPLSGSLAPLNMKglvkf 497
Cdd:PLN03232 547 LLGGDLTPARAFTSLSLFAVLRSPLNM---LPNLLSQVVNANVSLQRIEELLLSEERilAQNPPLQPGAPAISIK----- 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 qDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGK-STVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAV 576
Cdd:PLN03232 619 -NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYV 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 577 GQEPLLFGRSFRENIAYGLTRTPTM--EEITAVAMEsgaHDfISGFPqGYD-TEVGETGNQLSGGQRQAVALARALIRKP 653
Cdd:PLN03232 685 PQVSWIFNATVRENILFGSDFESERywRAIDVTALQ---HD-LDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 654 RLLILDDATSALDAgnqlRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 730
Cdd:PLN03232 760 DIYIFDDPLSALDA----HVAHQVFDScmkDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835
|
...
gi 56717 731 MVE 733
Cdd:PLN03232 836 LME 838
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
495-674 |
1.81e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.38 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEpLVQYdhhyLHTQ-- 572
Cdd:COG3839 4 LELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-DVTD----LPPKdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 -VAAVGQEPLLF-GRSFRENIAYGLT--RTPTmEEItavamesgahdfisgfpqgyDTEVGETG-------------NQL 635
Cdd:COG3839 76 nIAMVFQSYALYpHMTVYENIAFPLKlrKVPK-AEI--------------------DRRVREAAellgledlldrkpKQL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 56717 636 SGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRVQ 674
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDA--KLRVE 171
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
491-726 |
1.87e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 570
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQEP--LLFGRSFRENIAYGLTRT----PTMEEITAVAME-SGAHDFISGFPQgydtevgetgnQLSGGQRQAV 643
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKERVNEALElVGMQDFKEREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLME 723
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
...
gi 56717 724 RGG 726
Cdd:PRK13650 230 RGN 232
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
511-716 |
1.88e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV-----LLDG-EPLVQYDH--HYLHTQVAAVGQEPLL 582
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 583 F-GRSFRENIAYG--LTRTPTMEEITAVAMESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILD 659
Cdd:PRK11264 97 FpHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 660 DATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG 716
Cdd:PRK11264 170 EPTSALDpelVGEVLNTIRQLAQE----KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
512-678 |
2.27e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.32 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI 591
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGLT---RTPTMEEITAVAMEsgahdFisGFPqgyDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 668
Cdd:PRK10247 102 IFPWQirnQQPDPAIFLDDLER-----F--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170
....*....|
gi 56717 669 NQLRVQRLLY 678
Cdd:PRK10247 172 NKHNVNEIIH 181
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
488-716 |
3.37e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.53 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 488 PLNMKGLvkfqDVSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH 567
Cdd:PRK09536 3 MIDVSDL----SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQVAAVGQE-PLLFGRSFRENIAYG----LTRTPTMEEI--TAV--AMESGahdfisGFPQGYDTEVGEtgnqLSGG 638
Cdd:PRK09536 74 AASRRVASVPQDtSLSFEFDVRQVVEMGrtphRSRFDTWTETdrAAVerAMERT------GVAQFADRPVTS----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDAGNQLR----VQRLLYEspewaSRTVLLITQQLSLAER-AHHILFLKEGSVC 713
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRtlelVRRLVDD-----GKTAVAAIHDLDLAARyCDELVLLADGRVR 218
|
...
gi 56717 714 EQG 716
Cdd:PRK09536 219 AAG 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
503-707 |
3.84e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 94.61 E-value: 3.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 503 AYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVlldgeplvqydHHYLHTQVAAVGQ---E 579
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 580 PLLFGRSFRENIAYG------LTRTPTMEEITAV--AMES-GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALI 650
Cdd:NF040873 67 PDSLPLTVRDLVAMGrwarrgLWRRLTRDDRAAVddALERvGLADLA-------GRQLGE----LSGGQRQRALLAQGLA 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 651 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFL 707
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
510-717 |
4.13e-22 |
|
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: 95.97 E-value: 4.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFG 584
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 R-SFRENIAYGLTRT-----------PTMEEITAVAMEsgAHDFIsGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRK 652
Cdd:cd03219 89 ElTVLENVMVAAQARtgsglllararREEREARERAEE--LLERV-GLADLADRPAGE----LSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
510-717 |
4.93e-22 |
|
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: 96.26 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFG 584
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 R-SFRENIA------------YGLTRTP----TMEEITAVAMES----GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAV 643
Cdd:COG0411 93 ElTVLENVLvaaharlgrgllAALLRLPrarrEEREARERAEELlervGLADRA-------DEPAGN----LSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
495-674 |
6.02e-22 |
|
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: 94.63 E-value: 6.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHYL---HT 571
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-----DVTDLppkDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALI 650
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELL------QIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180
....*....|....*....|....
gi 56717 651 RKPRLLILDDATSALDAgnQLRVQ 674
Cdd:cd03301 147 REPKVFLMDEPLSNLDA--KLRVQ 168
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
256-470 |
9.91e-22 |
|
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: 96.01 E-value: 9.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 256 VFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCL----LAFMIWGSFYLTVVTLLSLPLLF 331
Cdd:cd18575 75 VFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL----RNLLLliggLVMLFITSPKLTLLVLLVIPLVV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 332 LLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVTEVWTMSVSG 411
Cdd:cd18575 151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA----AFAAALRRIRARALLTALV 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 412 MLLK----VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18575 227 IFLVfgaiVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
511-712 |
1.01e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.13 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQY-DHHYLHTQVAAvgqepLLFGRSFRE 589
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEArEDTRLMFQDAR-----LLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 590 NIAYGLT---RTPTMEEITAVAMESGAHDFISGfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:PRK11247 101 NVGLGLKgqwRDAALQALAAVGLADRANEWPAA---------------LSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 56717 667 AGNQLRVQRLLyESpEWASR--TVLLITQQLS----LAERahhILFLKEGSV 712
Cdd:PRK11247 166 ALTRIEMQDLI-ES-LWQQHgfTVLLVTHDVSeavaMADR---VLLIEEGKI 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
509-717 |
1.44e-21 |
|
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: 94.28 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLF 583
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH----RIARLGigyvpEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 584 GR-SFRENI---AYGLTRTP----TMEEITAVamesgahdfisgFPqgydtEVGE----TGNQLSGGQRQAVALARALIR 651
Cdd:COG0410 91 PSlTVEENLllgAYARRDRAevraDLERVYEL------------FP-----RLKErrrqRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 652 KPRLLILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 717
Cdd:COG0410 154 RPKLLLLDEPSLGLapliveeifEIIRRLNREGV----------TILLVEQNARFAlEIADRAYVLERGRIVLEGT 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
485-716 |
1.67e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 94.72 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 485 SLAPLNMKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNL--------YQPTGGKVLL 556
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 557 DGEPLvqYDHHY----LHTQVAAVGQEPLLFGRSFRENIAYGL-----TRTPTMEEI-----TAVAMesgahdfisgfpq 622
Cdd:COG1117 76 DGEDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSELDEIveeslRKAAL------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 623 gYDtEV----GETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLIT---QQl 695
Cdd:COG1117 141 -WD-EVkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVThnmQQ- 215
|
250 260
....*....|....*....|..
gi 56717 696 slAER-AHHILFLKEGSVCEQG 716
Cdd:COG1117 216 --AARvSDYTAFFYLGELVEFG 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
489-717 |
3.28e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.42 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKFQDVS---FAYPNHpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD 565
Cdd:PRK11308 6 LQAIDLKKHYPVKrglFKPERL--VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 566 HHY---LHTQVAAVGQ-----------------EPLLfgrsfrenIAYGLTRTPTMEEITAVAMESGAHdfisgfPQGYD 625
Cdd:PRK11308 84 PEAqklLRQKIQIVFQnpygslnprkkvgqileEPLL--------INTSLSAAERREKALAMMAKVGLR------PEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 626 tevgETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHI 704
Cdd:PRK11308 150 ----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEV 225
|
250
....*....|...
gi 56717 705 LFLKEGSVCEQGT 717
Cdd:PRK11308 226 MVMYLGRCVEKGT 238
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
194-442 |
3.31e-21 |
|
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: 94.79 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDK-TAPSFARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRV----HGEVFRAVLHQETGFF 268
Cdd:cd18541 16 LLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRF----LWRYLIFGASRRIeydlRNDLFAHLLTLSPSFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 269 LKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 348
Cdd:cd18541 92 QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 349 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVTeVW-----TMSVSGMLLKVGILYLGG 423
Cdd:cd18541 172 QEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEE----YVEKNLRLAR-VDalffpLIGLLIGLSFLIVLWYGG 246
|
250
....*....|....*....
gi 56717 424 QLVVRGAVSSGNLVSFVLY 442
Cdd:cd18541 247 RLVIRGTITLGDLVAFNSY 265
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
511-716 |
4.18e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQNLyqPTGGKVLLDGEPLVQYDHHYL---HTQVAAVGQEP--LLFG 584
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 R-SFRENIAYGLT-RTPTM-----EEITAVAMESGAHDFISgfPQGYDTEvgetgnqLSGGQRQAVALARALIRKPRLLI 657
Cdd:PRK15134 378 RlNVLQIIEEGLRvHQPTLsaaqrEQQVIAVMEEVGLDPET--RHRYPAE-------FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 658 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAeRA--HHILFLKEGSVCEQG 716
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV-RAlcHQVIVLRQGEVVEQG 508
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
513-740 |
6.52e-21 |
|
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: 98.48 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 513 LQGLTFTLYPGKVTALVGPNGSGKST-VAALLQNLyQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRSFRENI 591
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEM-DKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGltrTPTMEEITAVAMESGA--HDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAgn 669
Cdd:TIGR00957 720 LFG---KALNEKYYQQVLEACAllPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-- 793
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 670 qlRVQRLLYES---PE--WASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEALAAPSD 740
Cdd:TIGR00957 794 --HVGKHIFEHvigPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
512-717 |
7.08e-21 |
|
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: 92.40 E-value: 7.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQY--DHHylhtQVAAVGQEPLLFGR-SFR 588
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKR----DISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 589 ENIAYGL-TRTPTMEEITAVAMEsgahdfISGFpQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDA 667
Cdd:cd03299 90 KNIAYGLkKRKVDKKEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 56717 668 GNQLRVQRLLYESPEWASRTVLLITQQL----SLAERahhILFLKEGSVCEQGT 717
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFeeawALADK---VAIMLNGKLIQVGK 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
518-724 |
7.26e-21 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 94.78 E-value: 7.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 518 FTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH-HYLHT---QVAAVGQEPLLFG-RSFRENIA 592
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgIFLPPhrrRIGYVFQEARLFPhLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 593 YGLTRTPT------MEEITAVAmesGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:COG4148 100 YGRKRAPRaerrisFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 667 AGnqlRVQRLL-Y-ES-PEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMER 724
Cdd:COG4148 166 LA---RKAEILpYlERlRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
482-727 |
9.55e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.72 E-value: 9.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 482 LSGSLAPLNMKGLVKfqdvsfAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL 561
Cdd:PRK13537 1 GPMSVAPIDFRNVEK------RYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 562 VQYDHHyLHTQVAAVGQ----EP--------LLFGRSFRENIAYGLTRTPTMEEITavAMESGAhdfisgfpqgyDTEVG 629
Cdd:PRK13537 72 PSRARH-ARQRVGVVPQfdnlDPdftvrenlLVFGRYFGLSAAAARALVPPLLEFA--KLENKA-----------DAKVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 630 EtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRvqRLLYE---SPEWASRTVLLITQQLSLAER-AHHIL 705
Cdd:PRK13537 138 E----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP--QAR--HLMWErlrSLLARGKTILLTTHFMEEAERlCDRLC 209
|
250 260
....*....|....*....|...
gi 56717 706 FLKEGSVCEQGTHLQLMERG-GC 727
Cdd:PRK13537 210 VIEEGRKIAEGAPHALIESEiGC 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
477-735 |
1.07e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 97.93 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 477 TPCSPLSGslAPLNMK-GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL 555
Cdd:PTZ00243 1292 EPASPTSA--APHPVQaGSLVFEGVQMRYREGLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 556 LDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPtmEEITAVAMESGAHDFISGFPQGYDTEVGETGNQL 635
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 636 SGGQRQAVALARALIRKPRLLIL-DDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCE 714
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSA--FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
250 260
....*....|....*....|..
gi 56717 715 QGTHLQL-MERGGCYRSMVEAL 735
Cdd:PTZ00243 1525 MGSPRELvMNRQSIFHSMVEAL 1546
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
505-716 |
1.51e-20 |
|
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: 90.89 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 505 PNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqYDhhyLHTQVAAVGQEPLLFG 584
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FD---VVKEPAEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 RSF--------RENIAY-----GLTRTPTMEEITAVAMESGAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALIR 651
Cdd:cd03266 85 DSTglydrltaRENLEYfaglyGLKGDELTARLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 652 KPRLLILDDATSALD--AGNQLR-VQRLLYEspewASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03266 154 DPPVLLLDEPTTGLDvmATRALReFIRQLRA----LGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
492-717 |
1.70e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 492 KGLVKfqdvSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvQYDHhylht 571
Cdd:COG4152 5 KGLTK----RFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPED----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 qVAAVG---QEPLLFGR-SFRENIAY-----GLTRtptmeeitAVAMESgAHDFISGFpqgydtEVGETGN----QLSGG 638
Cdd:COG4152 70 -RRRIGylpEERGLYPKmKVGEQLVYlarlkGLSK--------AEAKRR-ADEWLERL------GLGDRANkkveELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
510-738 |
1.91e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.77 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEP--------- 580
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 581 --LLFGRSFRENIAygLTRTPTMEEITAVAMESG-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLI 657
Cdd:PRK15112 106 isQILDFPLRLNTD--LEPEQREKQIIETLRQVGlLPDHASYYP-----------HMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 658 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGthlqlmerggcyrSMVEALA 736
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERG-------------STADVLA 239
|
..
gi 56717 737 AP 738
Cdd:PRK15112 240 SP 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
490-665 |
2.22e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.12 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydHHYL 569
Cdd:PRK15439 7 TAPPLLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC----ARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVG-----QEPLLF-GRSFRENIAYGLTRTP-TMEEITAVAMESGAHdfisgfpqgYDTEVgeTGNQLSGGQRQA 642
Cdd:PRK15439 80 PAKAHQLGiylvpQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ---------LDLDS--SAGSLEVADRQI 148
|
170 180
....*....|....*....|...
gi 56717 643 VALARALIRKPRLLILDDATSAL 665
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASL 171
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
494-710 |
2.30e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH---YLH 570
Cdd:PRK10908 1 MIRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQE-PLLFGRSFRENIAYGLTRTPTMEE-----ITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 644
Cdd:PRK10908 79 RQIGMIFQDhHLLMDRTVYDNVAIPLIIAGASGDdirrrVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQLSL-AERAHHILFLKEG 710
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLiSRRSYRMLTLSDG 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
194-470 |
2.92e-20 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 91.72 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKtapsFARNMWLMCILTIASTVLEFAGDGIYNITMG----HMHSRVHGEVFRAVLHQETGFFL 269
Cdd:cd18542 16 LLIPLLIRRIIDSVIGGG----LRELLWLLALLILGVALLRGVFRYLQGYLAEkasqKVAYDLRNDLYDHLQRLSFSFHD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCLLAF----MIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLA 345
Cdd:cd18542 92 KARTGDLMSRCTSDVDTIRRFLAFGLVELV----RAVLLFIGaliiMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 346 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeaLAYVTEVW--TMSVSGMLLKVGILYLGG 423
Cdd:cd18542 168 EEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIK--LAKLLAKYwpLMDFLSGLQIVLVLWVGG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 56717 424 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18542 246 YLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
491-716 |
4.22e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.95 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 570
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQEP--LLFGRSFRENIAYG-----LTRTP----TMEEITAVAMESGAHdfisgfpqgydtevgETGNQLSGGQ 639
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEverrVEEALKAVRMWDFRD---------------KPPYHLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG 716
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAaEWADQVIVLKEGRVLAEG 220
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-716 |
5.17e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.97 E-value: 5.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ-----PTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEP-LL 582
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 583 FGRSFRENIAYGL------TRTPTMEEITAVAMESGahdfisgfpQGYD---TEVGETGNQLSGGQRQAVALARALIRKP 653
Cdd:PRK14247 95 PNLSIFENVALGLklnrlvKSKKELQERVRWALEKA---------QLWDevkDRLDAPAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 654 RLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
497-692 |
5.84e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.98 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 497 FQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylHTQVAAV 576
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 577 GQEPLLF-GRSFRENIAYGLTR------------------TPTMEEITAV----------AMESGAHDFIS--GFPQG-Y 624
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAElraleaeleeleaklaepDEDLERLAELqeefealggwEAEARAEEILSglGFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 625 DTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEW-----ASR--TVLLIT 692
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-----------ESIEWleeflKNYpgTVLVVS 206
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
496-674 |
5.89e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.69 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 496 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLYQP--TGGKVLLDGEPLvqydhHYLHTQ 572
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRRL-----TALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVG---QEPLLFGR-SFRENIAYGLTRTPTMEEITAVAM----ESGAHDFISGFPqgydtevgetgNQLSGGQRQAVA 644
Cdd:COG4136 75 QRRIGilfQDDLLFPHlSVGENLAFALPPTIGRAQRRARVEqaleEAGLAGFADRDP-----------ATLSGGQRARVA 143
|
170 180 190
....*....|....*....|....*....|
gi 56717 645 LARALIRKPRLLILDDATSALDAGnqLRVQ 674
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAA--LRAQ 171
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
516-692 |
1.11e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 91.82 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 516 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylHTQVAAVGQEPLLFGR-SFRENIAYG 594
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 595 LT--RTPTMEEITAVA-MESGAH--DFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGN 669
Cdd:PRK11607 116 LKqdKLPKAEIASRVNeMLGLVHmqEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180
....*....|....*....|...
gi 56717 670 QLRVQRLLYESPEWASRTVLLIT 692
Cdd:PRK11607 185 RDRMQLEVVDILERVGVTCVMVT 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
508-711 |
1.18e-19 |
|
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: 88.16 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 508 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL----LDGEPLVQYDHHYLHTQVAAVGQEPLLF 583
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 584 GRSFRENIAYGltrTP-TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDAT 662
Cdd:cd03290 92 NATVEENITFG---SPfNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 56717 663 SALDA--GNQLrVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGS 711
Cdd:cd03290 169 SALDIhlSDHL-MQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
480-727 |
1.31e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 480 SPLSGSLAPLnmkgLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 559
Cdd:PRK13536 31 ASIPGSMSTV----AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 560 P--------------LVQYDHHYLHTQVaavgQEPLL-FGRSFRENIAYGLTRTPTMEEITavAMESGAhdfisgfpqgy 624
Cdd:PRK13536 104 PvpararlararigvVPQFDNLDLEFTV----RENLLvFGRYFGMSTREIEAVIPSLLEFA--RLESKA----------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 625 DTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDA-GNQLRVQRLlyESPEWASRTVLLITQQLSLAERAHH 703
Cdd:PRK13536 167 DARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPhARHLIWERL--RSLLARGKTILLTTHFMEEAERLCD 240
|
250 260
....*....|....*....|....*.
gi 56717 704 ILFLKEG--SVCEQGTHLQLMERGGC 727
Cdd:PRK13536 241 RLCVLEAgrKIAEGRPHALIDEHIGC 266
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
512-667 |
1.35e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.93 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLV-----QYDhhylhtqVAAVGQEPLLFGR- 585
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrsiqQRD-------ICMVFQSYALFPHm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 SFRENIAYGLTrtptM-----EEITAVAMESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILDD 660
Cdd:PRK11432 94 SLGENVGYGLK----MlgvpkEERKQRVKEALELVDLAGFEDRYV-------DQISGGQQQRVALARALILKPKVLLFDE 162
|
....*..
gi 56717 661 ATSALDA 667
Cdd:PRK11432 163 PLSNLDA 169
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
495-700 |
1.47e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.94 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG-----GKVLLDGEPLVQ--YDHH 567
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQVAAVGQEPLLFGRSFRENIAYGLTRT---PTMEEITAVamESGAHDfiSGFPQGYDTEVGETGNQLSGGQRQAVA 644
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrPKLEIDDIV--ESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER 700
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
193-470 |
1.68e-19 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 89.49 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 193 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHG----EVFRAVLHQETGFF 268
Cdd:cd18563 15 GLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITAdlrrDLYEHLQRLSLSFF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 269 LKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 348
Cdd:cd18563 95 DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 349 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKealayVTEVWTM--SVSGMLLKVG---ILYLGG 423
Cdd:cd18563 175 WRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR-----AEKLWATffPLLTFLTSLGtliVWYFGG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 56717 424 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18563 250 RQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
511-716 |
2.46e-19 |
|
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: 86.45 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGEPLvqyDHHYLHTQVAAVGQEPLLFGR-SF 587
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 588 RENIAYgltrtptmeeitAVAMESgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALDA 667
Cdd:cd03213 100 RETLMF------------AAKLRG-----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 56717 668 GNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEGSVCEQG 716
Cdd:cd03213 145 SSALQVMSLLRRLAD-TGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
494-716 |
4.44e-19 |
|
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: 87.45 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQnlyqptggkvLLDGeplvqyDHHylhtqv 573
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKST---LLS----------LITG------DLP------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEPLLFGRSF--------RENIAY-------GLTRTPTMEEITAvameSGAHDFIsGFPQGYDTE----------- 627
Cdd:COG1119 55 PTYGNDVRLFGERRggedvwelRKRIGLvspalqlRFPRDETVLDVVL----SGFFDSI-GLYREPTDEqrerarellel 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 628 ------VGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAER 700
Cdd:COG1119 130 lglahlADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPG 209
|
250
....*....|....*.
gi 56717 701 AHHILFLKEGSVCEQG 716
Cdd:COG1119 210 ITHVLLLKDGRVVAAG 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
515-719 |
7.75e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.97 E-value: 7.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 515 GLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFG----- 584
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIARMGvvrtfQHVRLFRemtvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 --------RSFRENIAYGLTRTPTMEEITAVAMESGAH--DFIsGFpqgydTEVG--ETGNqLSGGQRQAVALARALIRK 652
Cdd:PRK11300 99 enllvaqhQQLKTGLFSGLLKTPAFRRAESEALDRAATwlERV-GL-----LEHAnrQAGN-LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 653 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLA-ERAHHILflkegsVCEQGTHL 719
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIY------VVNQGTPL 233
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
489-666 |
1.01e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 86.68 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKfqdvSFaYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH 567
Cdd:COG1101 2 LELKNLSK----TF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQVAAVGQEPLLfGRSFR----EN--IAY------GLTRTPTMEEITAVamesgaHDFISGFPQGY----DTEVGet 631
Cdd:COG1101 77 KRAKYIGRVFQDPMM-GTAPSmtieENlaLAYrrgkrrGLRRGLTKKRRELF------RELLATLGLGLenrlDTKVG-- 147
|
170 180 190
....*....|....*....|....*....|....*
gi 56717 632 gnQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
511-723 |
1.06e-18 |
|
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: 85.67 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFGR 585
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH----KRARLGigylpQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 -SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 664
Cdd:cd03218 90 lTVEENILAVLEIRGLSKKEREEKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 665 LDAGNQLRVQRLLYESPEWAsrTVLLIT-----QQLSLAERAhHILFlkEGSVCEQGTHLQLME 723
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRG--IGVLITdhnvrETLSITDRA-YIIY--EGKVLAEGTPEEIAA 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
500-717 |
1.14e-18 |
|
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: 90.13 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 500 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKS-TVAALLQNLYQP---TGGKVLLDGEPLVQYDHHYLHT---- 571
Cdd:COG4172 14 VAFGQGGGT-VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPL-----LF--GRSFRENIA--YGLTRTPTMEEITAVAMESG---AHDFISGFPqgydtevgetgNQLSGGQ 639
Cdd:COG4172 93 RIAMIFQEPMtslnpLHtiGKQIAEVLRlhRGLSGAAARARALELLERVGipdPERRLDAYP-----------HQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
494-717 |
1.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 86.58 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH-HYLHTQ 572
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEP--LLFGRSFRENIAYG-----LTRTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVAL 645
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 646 ARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
512-717 |
1.30e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ------PTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGR 585
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 -SFRENIAYGLTRTPTME--EITAVAMESGAHdfISGFPQGYDtEVGETGNQLSGGQRQAVALARALIRKPRLLILDDAT 662
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEkrEIKKIVEECLRK--VGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 663 SALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
516-725 |
1.39e-18 |
|
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: 87.86 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 516 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH-YLHTQVAAVG---QEPLLFGR-SFREN 590
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGyvfQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 591 IAYGLTRT------PTMEEITAVAmesgahdfisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 664
Cdd:TIGR02142 96 LRYGMKRArpserrISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 665 LDagNQLRVQRLLY-ESPEWASRT-VLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERG 725
Cdd:TIGR02142 162 LD--DPRKYEILPYlERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
509-717 |
1.78e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.83 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHYLHT---QVAAVGQEPLLFGR 585
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHArdrKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 -SFRENIAYGLTRTPTMEEITAVAMESGAHDFI-----SGFPQGYDTevgetgnQLSGGQRQAVALARALIRKPRLLILD 659
Cdd:PRK10851 89 mTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 660 DATSALDAgnQLRVQ-----RLLYESPEWASrtVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK10851 162 EPFGALDA--QVRKElrrwlRQLHEELKFTS--VFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
500-692 |
2.46e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 2.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 500 VSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDhhylhTQVAAVGQ- 578
Cdd:PRK11248 7 LYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EPLLFGRSFRENIAYGLT-RTPTMEEITAVAMESGAHDFISGFPQGYDTevgetgnQLSGGQRQAVALARALIRKPRLLI 657
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*
gi 56717 658 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT 692
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
219-478 |
2.54e-18 |
|
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: 86.74 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 219 NMW--LMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFF--LKNPTGSITSRVTEDTSNVCESISDK 294
Cdd:cd18578 52 NFWalMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 295 LNLFL-----------------WYLGrgLCLLAFM--IWGSFYLtvvtllslpllfllprrLGKVYQSLAVKVQESLAKS 355
Cdd:cd18578 132 LGLILqaivtlvagliiafvygWKLA--LVGLATVplLLLAGYL-----------------RMRLLSGFEEKNKKAYEES 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 356 TQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALayvtevWTMSVSG------MLLKVGILYLGGQLVVRG 429
Cdd:cd18578 193 SKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL------ISGLGFGlsqsltFFAYALAFWYGGRLVANG 266
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 56717 430 AVSSGN-LVSFVLyqLQFT-RAVEVLLSIYPSMQKSVGASEKIFEYLDRTP 478
Cdd:cd18578 267 EYTFEQfFIVFMA--LIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
494-717 |
2.94e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 2.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAY-PNHPNV-QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLV-----QYDH 566
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVsstskQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 567 HYLHTQVAAVGQEP--LLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFpqGYDTEVGETGN-QLSGGQRQAV 643
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFG----PQNFGIPKEKAEKIAAEKLEMV--GLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGT 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
495-717 |
2.96e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.78 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNH-PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT-- 571
Cdd:PRK11153 2 IELKNISKVFPQGgRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 -QVAAVGQE-PLLFGRSFRENIAYGLT--RTPTmEEITAVAME-------SGAHDFisgFPQgydtevgetgnQLSGGQR 640
Cdd:PRK11153 82 rQIGMIFQHfNLLSSRTVFDNVALPLElaGTPK-AEIKARVTEllelvglSDKADR---YPA-----------QLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 641 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
491-717 |
5.02e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYP-------------------NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQ 548
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 549 PTGGKVLLDGEplvqydhhylhtqVAAvgqePLLFGRSF------RENI-----AYGLTRtptmEEITAVAmesgahDFI 617
Cdd:COG1134 78 PTSGRVEVNGR-------------VSA----LLELGAGFhpeltgRENIylngrLLGLSR----KEIDEKF------DEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 618 SGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQ 693
Cdd:COG1134 131 VEF-----AELGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSH 204
|
250 260
....*....|....*....|....*
gi 56717 694 QLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:COG1134 205 SMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
494-722 |
5.23e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.86 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPnvqvlqgLTFTLY--PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHylHT 571
Cdd:PRK10771 1 MLKLTDITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHT--TT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 Q-----VAAVGQEPLLFGR-SFRENIAYGLTrtPTM-------EEITAVAMESGAHDFISGFPqgydtevgetgNQLSGG 638
Cdd:PRK10771 67 PpsrrpVSMLFQENNLFSHlTVAQNIGLGLN--PGLklnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK10771 134 QRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGP 213
|
....*
gi 56717 718 HLQLM 722
Cdd:PRK10771 214 TDELL 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
512-716 |
5.44e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.65 E-value: 5.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGR-SFREN 590
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 591 IAYGltRTPTM----------EEITAVAMESGAHDFISGfpQGYDTevgetgnqLSGGQRQAVALARALIRKPRLLILDD 660
Cdd:PRK10253 102 VARG--RYPHQplftrwrkedEEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 661 ATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
193-470 |
6.16e-18 |
|
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: 85.13 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 193 EMAIPFFTGRITDWILQDKTAPsfARNMWLMCILTIASTVLEFAGDGIYNITMGH-----MHS-RVhgEVFRAVLHQETG 266
Cdd:cd18544 15 ELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKlgqriIYDlRR--DLFSHIQRLPLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 267 FFLKNPTGSITSRVTEDTsnvcESISDKLNLFLWYLGRGLCLLAFMIWGSFYL---------------TVVTLlslpllf 331
Cdd:cd18544 91 FFDRTPVGRLVTRVTNDT----EALNELFTSGLVTLIGDLLLLIGILIAMFLLnwrlalisllvlpllLLATY------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 332 llprrlgkVYQSLAVKVQ----ESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWT 406
Cdd:cd18544 160 --------LFRKKSRKAYrevrEKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPL 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 407 MSVSGMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18544 231 VELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
509-722 |
7.30e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQV---LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTGGKVLLDGEPLVQYDHH-------YLHTQVAAVGQ 578
Cdd:COG4138 5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EPLLfgrsfrENIAYGLTRTPTMEEITAVaMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR------- 651
Cdd:COG4138 84 MPVF------QYLALHQPAGASSEAVEQL-LAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 722
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRhADRVWLLKQGKLVASGETAEVM 221
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
513-700 |
1.07e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 82.90 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 513 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydhhylhtqvaavgQEP------------ 580
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----------------TEPgpdrmvvfqnys 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 581 LLFGRSFRENIAYGLTRT-PTM----------EEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVALARAL 649
Cdd:TIGR01184 65 LLPWLTVRENIALAVDRVlPDLskserraiveEHIALVGLTEAADKRPG---------------QLSGGMKQRVAIARAL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 56717 650 IRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT----QQLSLAER 700
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVThdvdEALLLSDR 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
491-700 |
1.22e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQ--------PTGGKVLLDGEPLV 562
Cdd:PRK14239 2 TEPILQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 563 --QYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTME-EITAVAMES---GAHDFISGFPQGYDTEVGetgnqLS 636
Cdd:PRK14239 76 spRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDkQVLDEAVEKslkGASIWDEVKDRLHDSALG-----LS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 637 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER 700
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASR 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
499-726 |
1.41e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.52 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 499 DVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvQYDHH---YLHTQVAA 575
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 VGQEP--LLFGRSFRENIAYGLTRTPTME-EITAVAMESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALARALIRK 652
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEaEITRRVDEALTLVDAQHFRH-------QPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 653 PRLLILDDATSALDAGNQLR----VQRLLYEspewaSRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG------THLQL 721
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQmiaiIRRIVAQ-----GNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEA 229
|
....*
gi 56717 722 MERGG 726
Cdd:PRK13638 230 MEQAG 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
494-721 |
1.56e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.30 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPNV-QVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQNLYQP----TGGKVLLDGEPLVQYDHH 567
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLH----TQVAAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEEITAVAMESG---AHDFISGFPqgydtevget 631
Cdd:PRK15134 85 TLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYP---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 632 gNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 710
Cdd:PRK15134 155 -HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|.
gi 56717 711 SVCEQGTHLQL 721
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
494-717 |
1.67e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.36 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHH---YLH 570
Cdd:PRK13636 5 ILKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-IDYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQEP--LLFGRSFRENIAYGLT--RTPTMEEITAV--AMESGAHDFISGFPQgydtevgetgNQLSGGQRQAVA 644
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGAVnlKLPEDEVRKRVdnALKRTGIEHLKDKPT----------HCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGT 717
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGN 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
509-677 |
2.12e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.46 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH----HYLHTQVAAvgqEPLLfg 584
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLGHRNAM---KPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 rSFRENIA-----YGLTRTPTMEEITAVAMESGAHdfisgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPRLLILD 659
Cdd:PRK13539 89 -TVAENLEfwaafLGGEELDIAAALEAVGLAPLAH-----LPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170
....*....|....*...
gi 56717 660 DATSALDAGNQLRVQRLL 677
Cdd:PRK13539 153 EPTAALDAAAVALFAELI 170
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
489-665 |
2.71e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-HH 567
Cdd:COG3845 6 LELRGITK----RF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQVAAVGQEPLLFGR-SFRENIAYGLTRTPTM--------EEITAVAMEsgahdfiSGFPQGYDTEVGetgnQLSGG 638
Cdd:COG3845 77 AIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGrldrkaarARIRELSER-------YGLDVDPDAKVE----DLSVG 145
|
170 180
....*....|....*....|....*..
gi 56717 639 QRQAVALARALIRKPRLLILDDATSAL 665
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL 172
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
497-711 |
3.40e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 85.63 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 497 FQDVSFAypnHPNVQVL-QGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQPTGGKVLL-DGEplvqydhhylht 571
Cdd:COG4178 365 LEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKST---LLRaiaGLWPYGSGRIARpAGA------------ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFGRSFRENIAY-GLTRTPTMEEITAVAMESGAHDFISGFpqgyDTEVgETGNQLSGGQRQAVALARALI 650
Cdd:COG4178 427 RVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERL----DEEA-DWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 651 RKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGS 711
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
495-722 |
4.05e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 81.67 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 574
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGR-SFRENIAYGltRTP------TMEEITAVA-------MESGAHDFIsgfpqgydtevgetgNQLSGGQR 640
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFG--RFPyskgrlTAEDREIIDeaiayldLEDLADRYL---------------DELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 641 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHL 719
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPE 221
|
...
gi 56717 720 QLM 722
Cdd:COG4604 222 EII 224
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
248-441 |
4.54e-17 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 82.59 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 248 MHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDT----SNVCESISDKLNLFLWYLGRGLCLlaFMIwgSFYLTVVT 323
Cdd:cd18574 73 VAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRSVTQTVGCVVSL--YLI--SPKLTLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 324 LLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeaLAYVTE 403
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK--LGLGIG 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 56717 404 VWTM----SVSGMLLkvGILYLGGQLVVRGAVSSGNLVSFVL 441
Cdd:cd18574 227 IFQGlsnlALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
523-717 |
5.08e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.93 E-value: 5.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 523 GKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH----TQVAAVGQE-PLLFGRSFRENIAYGLT- 596
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTVLDNTAFGMEl 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 597 --------RTPTMEEITAVAMESGAHdfisGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 668
Cdd:PRK10070 134 aginaeerREKALDALRQVGLENYAH----SYP-----------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 56717 669 NQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGT 248
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
512-699 |
8.63e-17 |
|
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: 79.46 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 590
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 591 IAY--GLTRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 668
Cdd:cd03231 94 LRFwhADHSDEQVEEALARVGLNGFEDRPV--------------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|.
gi 56717 669 NQLRVQRLLYESPEWASRTVLLITQQLSLAE 699
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
493-716 |
1.03e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 79.88 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 493 GLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQ 572
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAA-----VGQEPLLFGrsfRENI-----AYGLTRtptmEEITAVAmesgahDFISGFpqgydTEVGETGNQ----LSGG 638
Cdd:cd03220 85 VSSllglgGGFNPELTG---RENIylngrLLGLSR----KEIDEKI------DEIIEF-----SELGDFIDLpvktYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
509-737 |
1.08e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVLLDGEPLV----------------QY------ 564
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILelspderaragiflafQYpveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 565 --DHHYLHTQVAAVGQEPLLFgRSFRENIAygltrtptmEEITAVAMesgAHDFIsgfpqgyDTEVGETgnqLSGGQRQA 642
Cdd:COG0396 92 vsVSNFLRTALNARRGEELSA-REFLKLLK---------EKMKELGL---DEDFL-------DRYVNEG---FSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 643 VALARALIRKPRLLILD--------DATSALDAG-NQLRvqrllyeSPEwasRTVLLITQQLSLAE--RAHHILFLKEGS 711
Cdd:COG0396 149 NEILQMLLLEPKLAILDetdsgldiDALRIVAEGvNKLR-------SPD---RGILIITHYQRILDyiKPDFVHVLVDGR 218
|
250 260
....*....|....*....|....*....
gi 56717 712 VCEQGTH---LQLMERGgcYRSMVEALAA 737
Cdd:COG0396 219 IVKSGGKelaLELEEEG--YDWLKEEAAA 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
495-705 |
1.09e-16 |
|
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: 77.96 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVlldgeplvqydHHYLHTQVA 574
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQEPLLFGRSFRENIAYgltrtPTMEEitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPR 654
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYEspewASRTVLLITQQLSLAERAHHIL 705
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHRPSLWKFHDRVL 158
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
495-717 |
1.58e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.59 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHP--NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQY--DHHYLH 570
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 T--QVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFIS--GFPQGYdteVGETGNQLSGGQRQAVA 644
Cdd:PRK13646 83 VrkRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMdlGFSRDV---MSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTS 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
510-679 |
2.21e-16 |
|
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: 79.02 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLldgeplvqYDHHYLHTQVAAVGQEPLLFGRsfRE 589
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDGGWVDLAQASPREILALR--RR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 590 NIAY------GLTRTPTMEeitaVAMESGAHdfisgfpQGYDTEV-----GETGNQL--------------SGGQRQAVA 644
Cdd:COG4778 94 TIGYvsqflrVIPRVSALD----VVAEPLLE-------RGVDREEararaRELLARLnlperlwdlppatfSGGEQQRVN 162
|
170 180 190
....*....|....*....|....*....|....*
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 679
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
491-712 |
2.91e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.85 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPN-HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 569
Cdd:PRK10535 1 MTALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 htqvAAVGQEPllFGRSFREniaYGLTRTPTME---EITAV-------AMESGAHDFISGFpqGYDTEVGETGNQLSGGQ 639
Cdd:PRK10535 81 ----AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSV 712
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
195-470 |
2.93e-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: 80.14 E-value: 2.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDWILQDKTAPS------FARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRV----HGEVFRAVLHQE 264
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGGGgvdfsgLLRILLLLLGLYLLSALFSY----LQNRLMARVSQRTvydlRKDLFEKLQRLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 265 TGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCL----LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 340
Cdd:cd18547 93 LSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLI----SSILTivgtLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 341 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGIL 419
Cdd:cd18547 169 SQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY-VLVA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 56717 420 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18547 248 VVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
501-700 |
3.00e-16 |
|
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: 78.91 E-value: 3.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 501 SFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE-PLVQYDHHyLHTQVAAVGQE 579
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKF-LRRIGVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 580 PLLF-----GRSFRENIA-YGLTR---TPTMEEITAvAMESGAHdfisgfpqgYDTEVgetgNQLSGGQRQAVALARALI 650
Cdd:cd03267 104 TQLWwdlpvIDSFYLLAAiYDLPParfKKRLDELSE-LLDLEEL---------LDTPV----RQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 56717 651 RKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL----SLAER 700
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMkdieALARR 223
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
493-712 |
3.07e-16 |
|
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: 79.51 E-value: 3.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 493 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLYqpTGGKVLLDGeplVQYDHHYLHT 571
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDG---VSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVG---QEPLLFGRSFRENI-AYGLTRTptmEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALAR 647
Cdd:cd03289 75 WRKAFGvipQKVFIFSGTFRKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 648 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 712
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
491-717 |
3.62e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHPNVQ---VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH 567
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 Y-LHTQVAAVGQEP--LLFGRSFRENIAYG---LTRTPtmEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSG 637
Cdd:PRK13633 81 WdIRNKAGMVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRERVDESlkkvGMYEYRRHAP-----------HLLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 638 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
513-717 |
3.76e-16 |
|
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: 78.18 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 513 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYLHTQVAAVGQEPLLFGR-SFRENI 591
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 A-----YGLTRTPTMEEITAVAmesgahDFIsgfpqgydtEVGETGNQL----SGGQRQAVALARALIRKPRLLILDDAT 662
Cdd:cd03265 95 YiharlYGVPGAERRERIDELL------DFV---------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 663 SALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGT 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
508-667 |
4.86e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.50 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 508 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDH--HYLHTQVAAVGQE----PL 581
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-MRFASttAALAAGVAIIYQElhlvPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 582 LfgrSFRENI-------AYGLTRTPTMEEITAVAMESGAHDFISGFPQGYdtevgetgnqLSGGQRQAVALARALIRKPR 654
Cdd:PRK11288 94 M---TVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----------LSIGQRQMVEIAKALARNAR 160
|
170
....*....|...
gi 56717 655 LLILDDATSALDA 667
Cdd:PRK11288 161 VIAFDEPTSSLSA 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
512-667 |
5.15e-16 |
|
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: 77.01 E-value: 5.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 590
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 591 I----AYGLTRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:TIGR01189 94 LhfwaAIHGGAQRTIEDALAAVGLTGFEDLPA--------------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
.
gi 56717 667 A 667
Cdd:TIGR01189 160 K 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
511-716 |
7.52e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE----------PLVQYDHHYLH---TQVAAVG 577
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgQLKVADKNQLRllrTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QEPLLFGR-SFRENI------AYGLTRTPTMEEITAVAMESGahdfISGFPQGydtevgETGNQLSGGQRQAVALARALI 650
Cdd:PRK10619 99 QHFNLWSHmTVLENVmeapiqVLGLSKQEARERAVKYLAKVG----IDERAQG------KYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 651 RKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:PRK10619 169 MEPEVLLFDEPTSALDpelVGEVLRIMQQLAEE----GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
495-692 |
7.87e-16 |
|
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: 74.79 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtqva 574
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 avgqepllfgrsfRENIAYgltrtptmeeitavamesgahdfisgFPqgydtevgetgnQLSGGQRQAVALARALIRKPR 654
Cdd:cd03221 62 -------------TVKIGY--------------------------FE------------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*...
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPewasRTVLLIT 692
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVS 124
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
512-721 |
8.29e-16 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 78.36 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRSFRENI 591
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGLT----RTPTMeeITAVAMESGahdfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDa 667
Cdd:cd03291 119 IFGVSydeyRYKSV--VKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 668 gnqLRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 721
Cdd:cd03291 192 ---VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
512-712 |
1.01e-15 |
|
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: 81.88 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLyqPTGGKVLLDGeplVQYDHHYLHTQVAAVG---QEPLLFGRSF 587
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLlSALLRLL--STEGEIQIDG---VSWNSVTLQTWRKAFGvipQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 588 RENIaygltrTP----TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 663
Cdd:TIGR01271 1309 RKNL------DPyeqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 56717 664 ALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 712
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
495-676 |
1.08e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG------EPlVQYDhhy 568
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelEP-ADRD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 lhtqVAAVGQEPLLFGR-SFRENIAYGLT--RTPTmEEI------TAVAMESGAhdFISGFPQgydtevgetgnQLSGGQ 639
Cdd:PRK11650 78 ----IAMVFQNYALYPHmSVRENMAYGLKirGMPK-AEIeervaeAARILELEP--LLDRKPR-----------ELSGGQ 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 56717 640 RQAVALARALIRKPRLLILDDATSALDAgnQLRVQ-RL 676
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDA--KLRVQmRL 175
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
512-721 |
1.57e-15 |
|
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: 81.11 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRSFRENI 591
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGLTRTPTmeEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDagnqL 671
Cdd:TIGR01271 508 IFGLSYDEY--RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----V 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 56717 672 RVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 721
Cdd:TIGR01271 582 VTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
500-718 |
1.67e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 500 VSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvQYDHHY---------LH 570
Cdd:PRK11124 8 INCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKtpsdkaireLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQE----PLLfgrSFRENI------AYGLTRTPTMEEitavAMESGAH----DFISGFPQgydtevgetgnQLS 636
Cdd:PRK11124 82 RNVGMVFQQynlwPHL---TVQQNLieapcrVLGLSKDQALAR----AEKLLERlrlkPYADRFPL-----------HLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 637 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQ 715
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
...
gi 56717 716 GTH 718
Cdd:PRK11124 223 GDA 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
494-700 |
2.36e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 76.74 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPNVQvlqGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ--PTG---GKVLLDGEPLvqYDHHY 568
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNL--YAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 ----LHTQVAAVGQEPLLFGRSFRENIAYG---LTRTPTMEEITAVAMESGAHdfisgfpqgYDtEVG----ETGNQLSG 637
Cdd:PRK14243 85 dpveVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAAL---------WD-EVKdklkQSGLSLSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 638 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER 700
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAAR 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
489-667 |
2.47e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEPLVQyd 565
Cdd:PRK13549 6 LEMKNITK----TF-----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 566 HHYLHTQ---VAAVGQEPLLF-GRSFRENIAYGltrtptmEEITA------VAMESGAHDFISGFPQGYD--TEVGETGn 633
Cdd:PRK13549 74 SNIRDTEragIAIIHQELALVkELSVLENIFLG-------NEITPggimdyDAMYLRAQKLLAQLKLDINpaTPVGNLG- 145
|
170 180 190
....*....|....*....|....*....|....
gi 56717 634 qlsGGQRQAVALARALIRKPRLLILDDATSALDA 667
Cdd:PRK13549 146 ---LGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
510-716 |
2.85e-15 |
|
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: 75.77 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKST----VAALLQNLYQpTGGKVLLDGEPLvqyDHHYLHTQVAAVGQ-EPLLFG 584
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR---KPDQFQKCVAYVRQdDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 RSFRENIAYGLT-RTPT---------MEEIT---AVAMESGAHDFISGfpqgydtevgetgnqLSGGQRQAVALARALIR 651
Cdd:cd03234 96 LTVRETLTYTAIlRLPRkssdairkkRVEDVllrDLALTRIGGNLVKG---------------ISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLL-ITQQLS-LAERAHHILFLKEGSVCEQG 716
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILtIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
221-468 |
3.13e-15 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 77.32 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 221 WLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLW 300
Cdd:cd18558 63 YYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 301 YLGR-GLCLLAFMIWGsFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEA 379
Cdd:cd18558 143 NIATfGTGFIIGFIRG-WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 380 QKFRQKLEEMKPLNKKEAlayVTEVWTMSVSGMLLKVG---ILYLGGQLVVRGAVSSGNLVSFVLYQLQFT-RAVEVLLS 455
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKA---ITFNISMGAAFLLIYASyalAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAfSAGQQVPS 298
|
250
....*....|...
gi 56717 456 IYPSMQKSVGASE 468
Cdd:cd18558 299 IEAFANARGAAYH 311
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
494-666 |
3.80e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.95 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLVQ-Y---DHHYL 569
Cdd:COG0488 315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgYfdqHQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTqvaavgqepllfGRSFRENIAYGLtrtPTMEEITAVAMesgAHDFisGFPqGYD--TEVGEtgnqLSGGQRQAVALAR 647
Cdd:COG0488 391 DP------------DKTVLDELRDGA---PGGTEQEVRGY---LGRF--LFS-GDDafKPVGV----LSGGEKARLALAK 445
|
170
....*....|....*....
gi 56717 648 ALIRKPRLLILDDATSALD 666
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLD 464
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
193-462 |
5.47e-15 |
|
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: 76.33 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 193 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFagdgiYNITMGH-----MHSRVHGEVFRAVLHQETGF 267
Cdd:cd18549 18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNY-----FVTYWGHvmgarIETDMRRDLFEHLQKLSFSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 268 FLKNPTGSITSRVTEDTSNVCE------------------------SISDKLNLFLwylgrgLCLLAFMIWGSFYLTvvt 323
Cdd:cd18549 93 FDNNKTGQLMSRITNDLFDISElahhgpedlfisiitiigsfiillTINVPLTLIV------FALLPLMIIFTIYFN--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 324 llslpllfllprrlGKVYQSLAvKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKpLNKKEAlaYVT 402
Cdd:cd18549 164 --------------KKMKKAFR-RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFL-ESKKKA--YKA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 403 EVWTMSVSGM---LLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQK 462
Cdd:cd18549 225 MAYFFSGMNFftnLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
491-697 |
5.47e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.54 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 570
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAvgqePLLFGRSFRenIAYGLTRT---PTMEEITAvamesgAHdfISGFPQgydtevgetgNQLSGGQRQAVALAR 647
Cdd:PRK09544 78 LDTTL----PLTVNRFLR--LRPGTKKEdilPALKRVQA------GH--LIDAPM----------QKLSGGETQRVLLAR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 56717 648 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL 697
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
512-740 |
5.63e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 5.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTV----AALLQNLYQPTG----GKVLLDGEPLVQYDHHYLHTQVAAVGQ--EPl 581
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 582 LFGRSFRENIAYGltRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARAL---------IRK 652
Cdd:PRK13547 95 AFAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 653 PRLLILDDATSALDAGNQLR----VQRLlyeSPEWaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERG-- 725
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRlldtVRRL---ARDW-NLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPAhi 248
|
250
....*....|....*.
gi 56717 726 -GCYRSMVEALAAPSD 740
Cdd:PRK13547 249 aRCYGFAVRLVDAGDG 264
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
495-717 |
7.16e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.83 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAY-PNHPNVQ-VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLV-----QYDHH 567
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVItagkkNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPT---MEEITAVAMESGAHDFIsgfpqGYDTEVGETGN-QLSGGQRQ 641
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFG----PMnfgVSEEDAKQKAREMIELV-----GLPEELLARSPfELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 642 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
510-715 |
9.52e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVGQEPLLF-GRSFr 588
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE----ARAKLRAKHVGFvFQSF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 589 eniayglTRTPTM---EEITAVAMESGAHDFISG------FPQ-GYDTEVGETGNQLSGGQRQAVALARALIRKPRLLIL 658
Cdd:PRK10584 98 -------MLIPTLnalENVELPALLRGESSRQSRngakalLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 659 DDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQ 715
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
512-712 |
1.08e-14 |
|
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: 72.85 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhylhtqvaavgqepllfGRSFRENI 591
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT---------------------RRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGltrtptmeeITAVAMESGAHDFISGFPqgydteVGE---TGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 668
Cdd:cd03215 74 RAG---------IAYVPEDRKREGLVLDLS------VAEniaLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 56717 669 NQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSV 712
Cdd:cd03215 139 AKAEIYRLIRELAD-AGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
509-716 |
1.33e-14 |
|
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: 72.94 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPl 581
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE----ERARLGiflafQYP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 582 lfgrsfreniaygltrtptmEEITAVAMEsgahDFISgfpqgydtEVGETgnqLSGGQRQAVALARALIRKPRLLILDDA 661
Cdd:cd03217 87 --------------------PEIPGVKNA----DFLR--------YVNEG---FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 662 TSALDAGNqLR-----VQRLLYEspewaSRTVLLITQQLSLAE--RAHHILFLKEGSVCEQG 716
Cdd:cd03217 132 DSGLDIDA-LRlvaevINKLREE-----GKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
194-470 |
1.95e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 74.44 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAgDGIYNITMGH--MHS-RVhgEVFRAVLHQETGFFLK 270
Cdd:cd18550 16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVV-QTYLSARIGQgvMYDlRV--QLYAHLQRMSLAFFTR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 271 NPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQE 350
Cdd:cd18550 93 TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 351 SLAKSTQVALEALSA--MPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVR 428
Cdd:cd18550 173 KLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 56717 429 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18550 253 GGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
515-679 |
2.62e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.74 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 515 GLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT---QVAAVGQEPL--LFGR-SFR 588
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsDIQMIFQDPLasLNPRmTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 589 ENIAYGL-------TRTPTMEEITAVAMESG-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDD 660
Cdd:PRK15079 119 EIIAEPLrtyhpklSRQEVKDRVKAMMLKVGlLPNLINRYP-----------HEFSGGQCQRIGIARALILEPKLIICDE 187
|
170
....*....|....*....
gi 56717 661 ATSALDAGNQLRVQRLLYE 679
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQ 206
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
523-737 |
3.17e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.13 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 523 GKVTALVGPNGSGKSTvaaLLQNL---YQPTGGKVLLDgeplvqydhhylhTQVAAVGQEPLLFGRSFRENIAYgLTRTP 599
Cdd:PTZ00243 686 GKLTVVLGATGSGKST---LLQSLlsqFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNILF-FDEED 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 600 TMEEITAVAMESGAHDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 679
Cdd:PTZ00243 749 AARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFL 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 680 SpEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMErggcyRSMVEALAA 737
Cdd:PTZ00243 828 G-ALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-----TSLYATLAA 879
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
495-717 |
3.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.63 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPNVQ--VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL----VQYDHHY 568
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtP-----TMEEITAVAMESGAHDFISgfpqgyDTEVGETGNQLSGGQRQ 641
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 642 AVALARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
495-717 |
5.10e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 73.16 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAY-PNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLV--QYDHHYLH 570
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVGQEP--LLFGRSFRENIAYGLTRTP-TMEEI---TAVAMEsgahdfISGFPqgYDTEVGETGNQLSGGQRQAVA 644
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGlSEEEIenrVKRAMN------IVGLD--YEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
194-470 |
6.66e-14 |
|
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: 72.89 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKTAPSfarnMWLMCILTIASTVLEFAGDGIYNITMGHMHSRV-HG---EVFRAVLHQETGFFL 269
Cdd:cd18545 17 LAGPYLIKIAIDEYIPNGDLSG----LLIIALLFLALNLVNWVASRLRIYLMAKVGQRIlYDlrqDLFSHLQKLSFSFFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KNPTGSITSRVTEDTSNVCE--------SISDKLNLFlwylgrglCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVY 341
Cdd:cd18545 93 SRPVGKILSRVINDVNSLSDllsnglinLIPDLLTLV--------GIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 342 QSLAVKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeALAYVTEVW-TMSVSGMLLKVGIL 419
Cdd:cd18545 165 RKAWQRVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWpLVELISALGTALVY 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 56717 420 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18545 243 WYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
514-707 |
1.53e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.22 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 514 QGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYlHTQVAAVGQ----EPLLfgrSFRE 589
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHqpgiKTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 590 NIAYGLT-RTPTMEEITAVAMEsgahdfisgfpqgydtEVGETG------NQLSGGQRQAVALARALIRKPRLLILDDAT 662
Cdd:PRK13538 94 NLRFYQRlHGPGDDEALWEALA----------------QVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 56717 663 SALDAGNQLRVQRLLYESpewASR--TVLLIT-QQLSLAERAHHILFL 707
Cdd:PRK13538 158 TAIDKQGVARLEALLAQH---AEQggMVILTThQDLPVASDKVRKLRL 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
491-665 |
1.80e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylH 570
Cdd:PRK10762 1 MQALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 TQVAAVG---QEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFIS--GFPQGYDTEVGEtgnqLSGGQRQAVA 644
Cdd:PRK10762 76 SQEAGIGiihQELNLIPQlTIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180
....*....|....*....|.
gi 56717 645 LARALIRKPRLLILDDATSAL 665
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDAL 172
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
491-702 |
2.01e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.68 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-HHYL 569
Cdd:PRK11614 2 EKVMLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQEPLLFGR-SFRENIAYG---LTRTPTMEEITAVamesgaHDFisgFPQGYDTEVGETGNqLSGGQRQAVAL 645
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMGgffAERDQFQERIKWV------YEL---FPRLHERRIQRAGT-MSGGEQQMLAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 646 ARALIRKPRLLILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLI----TQQLSLAERAH 702
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLapiiiqqifDTIEQLREQGM----------TIFLVeqnaNQALKLADRGY 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
490-665 |
2.28e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplVQYDH--H 567
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKldH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 YLHTQ--VAAVGQEPLLFGR-SFRENIAYGltRTPT-------------MEEITAVAMesgahdFISGFPQGYDTEVGEt 631
Cdd:PRK09700 75 KLAAQlgIGIIYQELSVIDElTVLENLYIG--RHLTkkvcgvniidwreMRVRAAMML------LRVGLKVDLDEKVAN- 145
|
170 180 190
....*....|....*....|....*....|....
gi 56717 632 gnqLSGGQRQAVALARALIRKPRLLILDDATSAL 665
Cdd:PRK09700 146 ---LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
495-717 |
2.51e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.68 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGEPLVQYDHHYLHT 571
Cdd:PRK09473 15 VKDLRVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 ----QVAAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEE----ITAVAMESgAHDFISGFPqgydtevgetgNQ 634
Cdd:PRK09473 94 lraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEEsvrmLDAVKMPE-ARKRMKMYP-----------HE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 635 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVC 713
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
|
....
gi 56717 714 EQGT 717
Cdd:PRK09473 242 EYGN 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
489-667 |
2.59e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.94 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKfqdvSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEPLVQyd 565
Cdd:TIGR02633 2 LEMKGIVK----TFG-----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 566 HHYLHTQ---VAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFpQGYDTEVGETGNQLSGGQRQ 641
Cdd:TIGR02633 70 SNIRDTEragIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQ 148
|
170 180
....*....|....*....|....*.
gi 56717 642 AVALARALIRKPRLLILDDATSALDA 667
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTE 174
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
495-710 |
3.39e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAY-PNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY---- 568
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 569 LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFpqGYDTEVGETGN-QLSGGQRQAVAL 645
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 646 ARALIRKPRLLILDDATSALDAGNQLRVQRLLYESpEWASRTVLLITQQL-SLAERAHHILFLKEG 710
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
521-721 |
3.71e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.51 E-value: 3.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 521 YPGK-VTALVGPNGSGKSTVAALLQNLYQPTGG-----KVLLDGEPLVQY-DHHYLHTQVAAVGQEPLLFGRSFRENIAY 593
Cdd:PRK14271 44 FPARaVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 594 GLT----------RTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATS 663
Cdd:PRK14271 124 GVRahklvprkefRGVAQARLTEVGLWDAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 664 ALDAGNQLRVQRLLYespEWASR-TVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQL 721
Cdd:PRK14271 193 ALDPTTTEKIEEFIR---SLADRlTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
508-717 |
3.93e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 508 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNlYQPTG----GKVLLDGEPL-----------VQYDHHYLHTQ 572
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPIdakemraisayVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAavgQEPLLFGRSFR--ENIAYGLTRTPTMEEITAVAMESGAHdfisgfpqgydTEVGETGNQ--LSGGQRQAVALARA 648
Cdd:TIGR00955 115 TV---REHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCAN-----------TRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 649 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 717
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGS 250
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
511-659 |
5.20e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.29 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFGR 585
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH----KRARLGigylpQEASIFRK 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 586 -SFRENIAYGL-TRTPTMEEITAvAMESGAHDF-IsgfpqgydTEVGET-GNQLSGGQRQAVALARALIRKPRLLILD 659
Cdd:COG1137 93 lTVEDNILAVLeLRKLSKKEREE-RLEELLEEFgI--------THLRKSkAYSLSGGERRRVEIARALATNPKFILLD 161
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
522-693 |
1.43e-12 |
|
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: 65.86 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 522 PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL-LDGEPLVQYDHHYLHtqvaavgqepllfgrsfreniaygltrtpt 600
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 601 meeitavamesgahdfisgfpqgyDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ-----R 675
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelR 106
|
170
....*....|....*...
gi 56717 676 LLYESPEWASRTVLLITQ 693
Cdd:smart00382 107 LLLLLKSEKNLTVILTTN 124
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
497-714 |
2.56e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.00 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 497 FQDVSFAYPNhPNVQVlQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAV 576
Cdd:PRK10522 325 LRNVTFAYQD-NGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 577 GQEPLLFGRsfreniayglTRTPTMEEITAVAMESGAHdfISGFPQGYDTEVGETGN-QLSGGQRQAVALARALIRKPRL 655
Cdd:PRK10522 403 FTDFHLFDQ----------LLGPEGKPANPALVEKWLE--RLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 656 LILDDAtsALDAGNQLR---VQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSVCE 714
Cdd:PRK10522 471 LLLDEW--AADQDPHFRrefYQVLLPLLQE-MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
511-723 |
2.62e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 67.56 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ-----PTGGKVLLDGEPLVQYDHHYLHT--QVAAVGQEPLLF 583
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIEVrrEVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 584 GR-SFRENIAYGL------TRTPTMEEITAVAMESGA-----HDFISGFPqgydtevgetgNQLSGGQRQAVALARALIR 651
Cdd:PRK14267 98 PHlTIYDNVAIGVklnglvKSKKELDERVEWALKKAAlwdevKDRLNDYP-----------SNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 723
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
515-716 |
3.10e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.42 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 515 GLTFTLYPGKVTALVGPNGSGKS-TVAALLQNL---YQPTGGKVLLDGEPLVQYDHHYLHtqVAAVGQEPllfgRS-F-- 587
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRK--IATIMQNP----RSaFnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 588 --------RENI-AYGLTRTPT--MEEITAVAMESgAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLL 656
Cdd:PRK10418 95 lhtmhthaRETClALGKPADDAtlTAALEAVGLEN-AARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 657 ILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 716
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
510-695 |
3.47e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.45 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV-LLDGEPLVQ-----YDHHYLHTQ-VAAVGQEPLL 582
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDmtkpgPDGRGRAKRyIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 583 FG-RSFRENiaygLTRTPTMEEITAVAMESGAHDFIS-GFPQGYDTEVGET-GNQLSGGQRQAVALARALIRKPRLLILD 659
Cdd:TIGR03269 377 YPhRTVLDN----LTEAIGLELPDELARMKAVITLKMvGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190
....*....|....*....|....*....|....*.
gi 56717 660 DATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL 695
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
499-697 |
4.19e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 499 DVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHHYLHTQVAAVGQ 578
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-IKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 E----PLLfgrSFRENIAYGLTRTPTMEEITAVAMESGAHDFISgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPR 654
Cdd:PRK13540 82 RsginPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 56717 655 LLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL 697
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPL 190
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
513-716 |
4.34e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.87 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 513 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL---DGEPLVQYD------HHYLHTQVAAVGQEP--- 580
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYAlseaerRRLLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 581 LLFGRSFRENIA----------YGLTRTPTMEEITAVAMESgahDFISGFPQGYdtevgetgnqlSGGQRQAVALARALI 650
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYGDIRATAGDWLERVEIDA---ARIDDLPTTF-----------SGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 651 RKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAeR--AHHILFLKEGSVCEQG 716
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVA-RllAHRLLVMKQGRVVESG 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
634-717 |
4.35e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.84 E-value: 4.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 634 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSV 712
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQV 232
|
....*
gi 56717 713 CEQGT 717
Cdd:PRK11022 233 VETGK 237
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
418-561 |
5.58e-12 |
|
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: 69.06 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 418 ILYLGGQLvvrGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIfEYLDRTPCSPLSGSLAPLNMKGLVKF 497
Cdd:COG4615 250 ILFLLPAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKI-EELELALAAAEPAAADAAAPPAPADF 325
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 498 Q-----DVSFAYPN--HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL 561
Cdd:COG4615 326 QtlelrGVTYRYPGedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
498-692 |
9.32e-12 |
|
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: 68.04 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSFAYPnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYdhhylhtqvaaVG 577
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGY-----------LP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QEPLL-FGRSFRENIAYGLTRTP-TMEEITAVAME------------------------SGAHDFISGF---------PQ 622
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKdALDRFNEISAKyaepdadfdklaaeqaelqeiidaADAWDLDSQLeiamdalrcPP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 623 GyDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEWASR-------TVLLIT 692
Cdd:TIGR03719 155 W-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-----------ESVAWLERhlqeypgTVVAVT 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
508-717 |
9.49e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 508 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY--LHTQ------------V 573
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVieLSEQsaaqmrhvrgadM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEEITAVAME---SGAHDFISGFPqgydtevgetgNQLSGGQRQ 641
Cdd:PRK10261 107 AMIFQEPMTslnpvftVGEQIAESIRLhqGASREEAMVEAKRMLDQvriPEAQTILSRYP-----------HQLSGGMRQ 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 642 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 717
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGS 252
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
469-738 |
1.05e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.65 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 469 KIFEYLDRTPcsPLSGSLaplnmKGLVKfqdvsfayPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ 548
Cdd:COG4586 9 KTYRVYEKEP--GLKGAL-----KGLFR--------REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 549 PTGGKVLLDGepLVQYDH--HYLHtQVAAV-GQE-------PLLfgRSFRENIA-YGLTRT---PTMEEITAVaMEsgah 614
Cdd:COG4586 74 PTSGEVRVLG--YVPFKRrkEFAR-RIGVVfGQRsqlwwdlPAI--DSFRLLKAiYRIPDAeykKRLDELVEL-LD---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 615 dfISGFpqgYDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQ 694
Cdd:COG4586 144 --LGEL---LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 56717 695 LS----LAERahhILFLKEGSVCEQGTHLQLMERGGCYRSMVEALAAP 738
Cdd:COG4586 215 MDdieaLCDR---VIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEP 259
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
512-712 |
1.51e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhyLHTQVAAVGQ-----------EP 580
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDAIRAgiayvpedrkgEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 581 LLFGRSFRENIA---------YGLTRTPTMEEITAvamesgahDFISGF---PQGYDTEVGetgnQLSGGQRQAVALARA 648
Cdd:COG1129 341 LVLDLSIRENITlasldrlsrGGLLDRRRERALAE--------EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 649 LIRKPRLLILDDATSALDAGNQLRVQRLLYESpewASR--TVLLITQQLS-LAERAHHILFLKEGSV 712
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIREL---AAEgkAVIVISSELPeLLGLSDRILVMREGRI 472
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
491-731 |
1.79e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY---QPTGGKVLLDG-----EPLV 562
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQH---QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtvqrEGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 563 QYDHHYLHTQVAAVGQEPLLFGR-SFRENIAYG-LTRTP----------------TMEEITAVAMESGAHDFISgfpqgy 624
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRlSVLENVLIGaLGSTPfwrtcfswftreqkqrALQALTRVGMVHFAHQRVS------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 625 dtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHH 703
Cdd:PRK09984 152 ---------TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCER 222
|
250 260 270
....*....|....*....|....*....|
gi 56717 704 ILFLKEGSVCEQGTHLQL-MER-GGCYRSM 731
Cdd:PRK09984 223 IVALRQGHVFYDGSSQQFdNERfDHLYRSI 252
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
194-470 |
1.90e-11 |
|
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: 65.54 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRVHGEV----FRAVLHQETGFFL 269
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSY----IRSYLLLKLSQKLDIRLilgyFKHLLKLPLSFFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 270 KNPTGSITSRVTeDTSNVCESISDK-----LNLFLwylgrGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSL 344
Cdd:cd18570 95 TRKTGEIISRFN-DANKIREAISSTtislfLDLLM-----VIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 345 AVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA-LAYVTEVWTMSVSGmLLKVGILYLGG 423
Cdd:cd18570 169 NREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGkLSNLQSSIKGLISL-IGSLLILWIGS 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 56717 424 QLVVRGAVSSGNLVSFvlYQLQ--FTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18570 248 YLVIKGQLSLGQLIAF--NALLgyFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
498-692 |
2.32e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSFAYPnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK-VLLDGeplvqydhhylhtqvAAV 576
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG---------------IKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 577 G---QEPLL-FGRSFRENIAYG-------LTR---------TPtMEEITAVAMESG----------AHDFIS-------- 618
Cdd:PRK11819 73 GylpQEPQLdPEKTVRENVEEGvaevkaaLDRfneiyaayaEP-DADFDALAAEQGelqeiidaadAWDLDSqleiamda 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 619 -GFPQGyDTEVGetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEWASR-------TVLL 690
Cdd:PRK11819 152 lRCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-----------ESVAWLEQflhdypgTVVA 215
|
..
gi 56717 691 IT 692
Cdd:PRK11819 216 VT 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
509-722 |
2.86e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQV---LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTGGKVLLDGEPLVQYDHH-------YLHTQVAAVGQ 578
Cdd:PRK03695 5 DVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarhraYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EPLlfgrsFRENIAYGLTRTPTMEEITAVamesgaHDFISGFpqGYDTEVGETGNQLSGGQRQAVALARALIR-----KP 653
Cdd:PRK03695 84 MPV-----FQYLTLHQPDKTRTEAVASAL------NEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 654 --RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGTHLQLM 722
Cdd:PRK03695 151 agQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
633-724 |
3.45e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 633 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGS 711
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLeSISQWADTITVLYCGQ 236
|
90
....*....|...
gi 56717 712 VCEQGTHLQLMER 724
Cdd:COG4170 237 TVESGPTEQILKS 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
510-723 |
4.98e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE---PLVQYDHHYLHTQVAAVGQEP------ 580
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasldp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 581 ----------------LLFGRSFRENIAYGLTRTPTMEEitavamesgaHDFisGFPqgydtevgetgNQLSGGQRQAVA 644
Cdd:PRK10261 417 rqtvgdsimeplrvhgLLPGKAAAARVAWLLERVGLLPE----------HAW--RYP-----------HEFSGGQRQRIC 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 645 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 723
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
490-660 |
6.95e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.63 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 569
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HT---QVAAVGQEPLLF-GRSFRENIAYGL---TRTP-------TMEEITAVAMESGAHDFISgfpqgydtevgetgnQL 635
Cdd:PRK11831 80 YTvrkRMSMLFQSGALFtDMNVFDNVAYPLrehTQLPapllhstVMMKLEAVGLRGAAKLMPS---------------EL 144
|
170 180
....*....|....*....|....*
gi 56717 636 SGGQRQAVALARALIRKPRLLILDD 660
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDE 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
516-721 |
1.17e-10 |
|
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: 65.42 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 516 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHHYLHTQVAAVGQEPLLFGR-SFRENIAYG 594
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD-IETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 595 LTRTPTMEEITAVAMESGAHDfisgfpQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ 674
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 56717 675 RLL--YESpewaSRTVLLITQQLSLAE-RAHHILFLKEGSVCEQGTHLQL 721
Cdd:TIGR01257 1102 DLLlkYRS----GRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
512-710 |
1.36e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG--GKVLLDGEPLV-----------QYDHHYLHTQVaavgQ 578
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTkqilkrtgfvtQDDILYPHLTV----R 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 579 EPLLFGRSFReniaygLTRTPTMEEITAVAmESGAHDFisGFPQGYDTEVGETGNQ-LSGGQRQAVALARALIRKPRLLI 657
Cdd:PLN03211 159 ETLVFCSLLR------LPKSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 56717 658 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEG 710
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEG 283
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
195-470 |
2.05e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 62.55 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMG-HMHSRVHGEVFRAVLHQETGFFLKNPT 273
Cdd:cd18778 17 VPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEqKVVADLRSDLYDKLQRLSLRYFDDRQT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 274 GSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLA 353
Cdd:cd18778 97 GDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 354 KSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKplnkkEALAYVTEVW-----TMSVSGMLLKVGILYLGGQLVVR 428
Cdd:cd18778 177 ELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYR-----KAQLRAMKLWaifhpLMEFLTSLGTVLVLGFGGRLVLA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 56717 429 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18778 252 GELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
519-691 |
3.06e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 61.27 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 519 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHHY------------LHTQVAAVGQEPllfgrS 586
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQYikadyegtvrdlLSSITKDFYTHP-----Y 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 587 FRENIAYGLtrtpTMEEItavamesgahdfisgfpqgYDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:cd03237 95 FKTEIAKPL----QIEQI-------------------LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180
....*....|....*....|....*
gi 56717 667 AGNQLRVQRLLYESPEWASRTVLLI 691
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVV 172
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
501-667 |
4.41e-10 |
|
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: 59.97 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 501 SFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG---GKVLLDGEPLVQYDHHYlHTQVAAVG 577
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QE----PLLfgrsfreniaygltrtpTMEEITAVAMESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARALIRKP 653
Cdd:cd03233 90 EEdvhfPTL-----------------TVRETLDFALRCKGNEFVRGI---------------SGGERKRVSIAEALVSRA 137
|
170
....*....|....
gi 56717 654 RLLILDDATSALDA 667
Cdd:cd03233 138 SVLCWDNSTRGLDS 151
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
511-717 |
5.69e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 5.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE-----PLvqydHHYLHTQVAAVGQEPLLFGR 585
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRGIGYLPQEASIFRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 -SFRENIAYGLTrtpTMEEITAVAMESGAHDFISGFPQGYDTEvgETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 664
Cdd:PRK10895 93 lSVYDNLMAVLQ---IRDDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 665 LDAGNQLRVQRLLYESPEwaSRTVLLIT-----QQLSLAERAHhilFLKEGSVCEQGT 717
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRD--SGLGVLITdhnvrETLAVCERAY---IVSQGHLIAHGT 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
495-716 |
6.03e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 61.26 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAY----PNHpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV---LLDGEPLVQYDHH 567
Cdd:PRK13651 3 IKVKNIVKIFnkklPTE--LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 Y---------------------LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFIS--GFPQ 622
Cdd:PRK13651 81 EkvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 623 GYdteVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERA 701
Cdd:PRK13651 157 SY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLdNVLEWT 232
|
250
....*....|....*
gi 56717 702 HHILFLKEGSVCEQG 716
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
510-717 |
6.17e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL---------DGEPLVQY-------DHHYLHTQV 573
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNpyskkikNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQEP--LLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFPQGYD-TEVGETGnqLSGGQRQAVALARALI 650
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 651 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 717
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
489-665 |
6.23e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.11 E-value: 6.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEP----- 560
Cdd:NF040905 2 LEMRGITK----TF-----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 561 LVQYDHH---YLHTQVAAVgqePLLfgrSFRENI-------AYGL-----TRTPTMEEITAVamesgahdfisGFPQGYD 625
Cdd:NF040905 72 IRDSEALgivIIHQELALI---PYL---SIAENIflgneraKRGVidwneTNRRARELLAKV-----------GLDESPD 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 56717 626 TEVGETGNqlsgGQRQAVALARALIRKPRLLILDDATSAL 665
Cdd:NF040905 135 TLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
495-666 |
1.04e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLvqydhhylhtQVA 574
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGQ--EPLLFGRSFRENIAYGLtrtpTMEEITAVAMESGAhdFISGFP-QGYDTE--VGetgnQLSGGQRQAVALARAL 649
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGL----DIIKLGKREIPSRA--YVGRFNfKGSDQQkkVG----QLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 56717 650 IRKPRLLILDDATSALD 666
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
494-666 |
1.38e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ-YDHHylHTQ 572
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvFSQH--HVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 573 VAAVGQEPLLFgrsfreniaygltrtptMEEITAVAMESGAHDFISGFpqgydtevGETGN-------QLSGGQRQAVAL 645
Cdd:PLN03073 584 GLDLSSNPLLY-----------------MMRCFPGVPEQKLRAHLGSF--------GVTGNlalqpmyTLSGGQKSRVAF 638
|
170 180
....*....|....*....|.
gi 56717 646 ARALIRKPRLLILDDATSALD 666
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLD 659
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
419-708 |
2.05e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 60.92 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 419 LYLGGQLVVRGAVSSGNLVSFV--LYQLQ-FTRAVEVLLSIYPSMQK------SVGASEKIFEYLDRTPCSPLSGSLapL 489
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLMLAGrdMTRLAgFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV--E 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYdhhyl 569
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY----- 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 htqvaaVGQEPLLFGRSFRENIAYGLT---------RTPTMEEItavaMESGAHDFISGFPQGYDTeVGETGNQLSGGQR 640
Cdd:TIGR00954 520 ------VPQRPYMTLGTLRDQIIYPDSsedmkrrglSDKDLEQI----LDNVQLTHILEREGGWSA-VQDWMDVLSGGEK 588
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 641 QAVALARALIRKPRLLILDDATSALdagnQLRVQRLLYESPEWASRTVLLITQQLSLAEraHHILFLK 708
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWK--YHEYLLY 650
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
498-700 |
2.13e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSfaYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-HHYLHTQVAAV 576
Cdd:COG3845 261 ENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 577 GQEPLLFG----RSFRENIAYGLTRTPTMEE---ITAVAMESGAHDFISGF---PQGYDTEVGetgnQLSGGQRQAVALA 646
Cdd:COG3845 339 PEDRLGRGlvpdMSVAENLILGRYRRPPFSRggfLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILA 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 56717 647 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL----SLAER 700
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLdeilALSDR 471
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
517-697 |
5.74e-09 |
|
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: 57.38 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 517 TFTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKvlLDGEP-------------LVQYDHHYLHTQVAAVg 577
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefrgseLQNYFTKLLEGDVKVI- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QEPL---LFGRSFRENIAYGLTRTPtmeeitavamESGAHDFIS---GFPQGYDTEVgetgNQLSGGQRQAVALARALIR 651
Cdd:cd03236 91 VKPQyvdLIPKAVKGKVGELLKKKD----------ERGKLDELVdqlELRHVLDRNI----DQLSGGELQRVAIAAALAR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSL 697
Cdd:cd03236 157 DADFYFFDEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAV 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
517-668 |
5.81e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 517 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLV-QYDHHYLHTQVAAVGQEP----LLFGRSFRENI 591
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRkrdgLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 --------AYGLTRTPTMEEITAVAmesgahDFISGF----PqGYDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILD 659
Cdd:PRK10762 352 sltalryfSRAGGSLKHADEQQAVS------DFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420
|
....*....
gi 56717 660 DATSALDAG 668
Cdd:PRK10762 421 EPTRGVDVG 429
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
508-665 |
9.95e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.20 E-value: 9.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 508 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQY--DHHYLHTQVAAVGQE-PLLFG 584
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE-IDFksSKEALENGISMVHQElNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 585 RSFRENIAYGltRTPTMEEItaVAMESGAHDFISGFPQ-GYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 663
Cdd:PRK10982 88 RSVMDNMWLG--RYPTKGMF--VDQDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
..
gi 56717 664 AL 665
Cdd:PRK10982 164 SL 165
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
510-696 |
1.08e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.97 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKST-VAALLQNLYQ---PTGGKVLLDGEPLVQYDHHY-----------LHTQVA 574
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 575 AVGqEPLLFGRSFR--ENIAYGLTRTPTMEEITAVAMEsgahdfISGFPQGYDTEVG-ETGNQLSGGQRQAVALARALIR 651
Cdd:TIGR00956 154 TVG-ETLDFAARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 56717 652 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS 696
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCS 271
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
510-724 |
1.16e-08 |
|
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: 58.28 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 510 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVL----------------LDGEPLVQYDHHYLHT 571
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLLFgRSFRENIAYGLTRT--------------PTMEEITAVAMES--GAHDFISGFPQGYdtEVGETGNQL 635
Cdd:TIGR03269 93 EVDFWNLSDKLR-RRIRKRIAIMLQRTfalygddtvldnvlEALEEIGYEGKEAvgRAVDLIEMVQLSH--RITHIARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 636 SGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEGSVC 713
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVK-ASGISMVLTSHWPevIEDLSDKAIWLENGEIK 248
|
250
....*....|.
gi 56717 714 EQGTHLQLMER 724
Cdd:TIGR03269 249 EEGTPDEVVAV 259
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
512-692 |
1.75e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 55.73 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY--QPTGGKVLLDGEPLVQydhhylhtqvaavgQEPLLfgrsfrE 589
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------EASLI------D 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 590 NIAYGLTRTPTMEEITAVAMeSGAHDFISGFPqgydtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGN 669
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGL-SDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|...
gi 56717 670 QLRVQRLLYESPEWASRTVLLIT 692
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVAT 194
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
195-439 |
2.08e-08 |
|
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: 56.41 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRVH----GEVFRAVLHQETGFFLK 270
Cdd:cd18568 20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSA----VRQYLLDYFANRIDlsllSDFYKHLLSLPLSFFAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 271 NPTGSITSRVTED-------TSNVCESISDKLNLFLwYLGrglcllaFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQS 343
Cdd:cd18568 96 RKVGDIITRFQENqkirrflTRSALTTILDLLMVFI-YLG-------LMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 344 LAVKVQESLAKSTQVALEALSAMPTVRSFANEegeaQKFRQKLEE--MKPLN---KKEALAYVTEVwTMSVSGMLLKVGI 418
Cdd:cd18568 168 NSREIFQANAEQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNtrfRGQKLSIVLQL-ISSLINHLGTIAV 242
|
250 260
....*....|....*....|.
gi 56717 419 LYLGGQLVVRGAVSSGNLVSF 439
Cdd:cd18568 243 LWYGAYLVISGQLTIGQLVAF 263
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
511-710 |
2.33e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQPTGGKVLLDGEPLV-----------------QYDhhyLHTQV 573
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVngrpldssfqrsigyvqQQD---LHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVgQEPLLFGRSFREniAYGLTRTPTMEEITAV----AMESGAhdfisgfpqgyDTEVGETGNQLSGGQRQAVALARAL 649
Cdd:TIGR00956 851 STV-RESLRFSAYLRQ--PKSVSKSEKMEYVEEVikllEMESYA-----------DAVVGVPGEGLNVEQRKRLTIGVEL 916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 56717 650 IRKPRLLI-LDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEG 710
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
511-666 |
2.51e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.57 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGEPLV----------------QY-------- 564
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLelspedragegifmafQYpveipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 565 DHHYLHTQVAAV----GQEPLlfGR-SFRENIAygltrtptmEEITAVAMesgahdfisgfPQGYDTEVGETGnqLSGGQ 639
Cdd:PRK09580 95 NQFFLQTALNAVrsyrGQEPL--DRfDFQDLME---------EKIALLKM-----------PEDLLTRSVNVG--FSGGE 150
|
170 180
....*....|....*....|....*..
gi 56717 640 RQAVALARALIRKPRLLILDDATSALD 666
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
495-721 |
3.24e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.19 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG------EP-------L 561
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvPPaergvgmV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 562 VQYDHHYLHTQVAavgqepllfgrsfrENIAYGL-----------TRTPTMEEITAVAmesgaHdFISGFPQGydtevge 630
Cdd:PRK11000 81 FQSYALYPHLSVA--------------ENMSFGLklagakkeeinQRVNQVAEVLQLA-----H-LLDRKPKA------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 631 tgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGnqLRVQ----------RLlyespewaSRTVLLITQ-QLSLAE 699
Cdd:PRK11000 134 ----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA--LRVQmrieisrlhkRL--------GRTMIYVTHdQVEAMT 199
|
250 260
....*....|....*....|..
gi 56717 700 RAHHILFLKEGSVCEQGTHLQL 721
Cdd:PRK11000 200 LADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
511-710 |
3.74e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.17 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 511 QVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQPT-----GGKVLLDGEPLVQY--------DHHYLHTQVAAVg 577
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDKNfqrstgyvEQQDVHSPNLTV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 578 QEPLLFGRSFREniaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLI 657
Cdd:cd03232 97 REALRFSALLRG---------------------------------------------LSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 56717 658 LDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEG 710
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
195-470 |
3.76e-08 |
|
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: 55.57 E-value: 3.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDwilqDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVH----GEVFRAVLHQETGFFLK 270
Cdd:cd18543 17 AIPLLTRRAID----GPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEhdlrTDLFAHLQRLDGAFHDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 271 NPTGSITSRVTEDTSnvceSISDKLNLFLWYLGRGLCL---LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVK 347
Cdd:cd18543 93 WQSGQLLSRATSDLS----LVQRFLAFGPFLLGNLLTLvvgLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 348 VQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMkplnkkealaYVTEV----------WTMSVSGMLLKVG 417
Cdd:cd18543 169 AQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRL----------RATRLraarlrarfwPLLEALPELGLAA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 56717 418 ILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18543 239 VLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
347-445 |
4.09e-08 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 55.48 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 347 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGILYLGGQL 425
Cdd:cd18548 169 KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKaGRLMALLNPLMMLIMNLAI-VAILWFGGHL 247
|
90 100
....*....|....*....|
gi 56717 426 VVRGAVSSGNLVSFVLYQLQ 445
Cdd:cd18548 248 INAGSLQVGDLVAFINYLMQ 267
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
513-716 |
9.64e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 513 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLhtqVAAVGQE-------PLL--- 582
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLved 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 583 ---FGRSFReniaYGLTRTPTMEE---ITAVAMESGAHDFisgfpqgYDTEVGEtgnqLSGGQRQAVALARALIRKPRLL 656
Cdd:PRK15056 100 vvmMGRYGH----MGWLRRAKKRDrqiVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 657 ILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERAHHILFLKeGSVCEQG 716
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLgSVTEFCDYTVMVK-GTVLASG 223
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
512-666 |
1.05e-07 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 53.42 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGEPLV----------------QY--------D 565
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLelepderaraglflafQYpeeipgvsN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 566 HHYLHTQVAAV----GQEPL---LFGRSFRENIAygltrtptmeeitAVAM-ESGAHDFIS-GFpqgydtevgetgnqlS 636
Cdd:TIGR01978 95 LEFLRSALNARrsarGEEPLdllDFEKLLKEKLA-------------LLDMdEEFLNRSVNeGF---------------S 146
|
170 180 190
....*....|....*....|....*....|
gi 56717 637 GGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:TIGR01978 147 GGEKKRNEILQMALLEPKLAILDEIDSGLD 176
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
519-675 |
1.10e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.20 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 519 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPLVQYDHHYLHTQVAAVGQEpLL------FGRSF-RENI 591
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDYDGTVED-LLrsitddLGSSYyKSEI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 592 AYGLtrtpTMEEItavamesgahdfisgfpqgYDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQL 671
Cdd:PRK13409 438 IKPL----QLERL-------------------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
....
gi 56717 672 RVQR 675
Cdd:PRK13409 491 AVAK 494
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
489-721 |
1.45e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 489 LNMKGLVKFQDVSFAYPNHP--NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ--- 563
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 564 --YDHHYLHTQVAAVGQEP--LLFGRSFRENIAYG-LTRTPTMEEITAVAMEsgAHDFISgFPQGYdteVGETGNQLSGG 638
Cdd:PRK13645 81 kiKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGENKQEAYKKVPE--LLKLVQ-LPEDY---VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 639 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 717
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
....
gi 56717 718 HLQL 721
Cdd:PRK13645 235 PFEI 238
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
525-666 |
2.14e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.72 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 525 VTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqyDHH---YLHTQVAAVG---QEPLLFGR-SFRENIAYGLTR 597
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEkgiCLPPEKRRIGyvfQDARLFPHyKVRGNLRYGMAK 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 598 TPTMEEITAVAMESGAHdFISGFPQGydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:PRK11144 104 SMVAQFDKIVALLGIEP-LLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
495-666 |
3.11e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpnvQVL-QGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLvqydhhylhtQV 573
Cdd:PRK11819 325 IEAENLSKSFGD----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 574 AAVGQepllfgrsFRENIAYGLTrtpTMEEItavameSGAHDFIS---------------GFpQGYDTE--VGetgnQLS 636
Cdd:PRK11819 390 AYVDQ--------SRDALDPNKT---VWEEI------SGGLDIIKvgnreipsrayvgrfNF-KGGDQQkkVG----VLS 447
|
170 180 190
....*....|....*....|....*....|
gi 56717 637 GGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
506-710 |
4.04e-07 |
|
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: 50.44 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 506 NHPNVQVLQGLTFTlyPGKVTALVGPNGSGKSTVAallqnlyqptggkvlldgeplvqydhhylhTQVAAVgqeplLFGR 585
Cdd:cd03227 6 RFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTIL------------------------------DAIGLA-----LGGA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 SFRENIAYGLTRTptmEEITAVAMEsgahdFISGFPQgydtevgetgnqLSGGQRQAVALARALI---RKPR-LLILDDA 661
Cdd:cd03227 49 QSATRRRSGVKAG---CIVAAVSAE-----LIFTRLQ------------LSGGEKELSALALILAlasLKPRpLYILDEI 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 56717 662 TSALDAGNQLRVQRLLYE-SPEwaSRTVLLITQQLSLAERA---HHILFLKEG 710
Cdd:cd03227 109 DRGLDPRDGQALAEAILEhLVK--GAQVIVITHLPELAELAdklIHIKKVITG 159
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
505-695 |
4.77e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 505 PNHPN--VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVgqepll 582
Cdd:PRK13546 30 PKHKNktFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 583 fgrsfrENIAY-----GLTRtptmEEITAVAMEsgahdfISGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKP 653
Cdd:PRK13546 104 ------ENIEFkmlcmGFKR----KEIKAMTPK------IIEF-----SELGEFIYQpvkkYSSGMRAKLGFSINITVNP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 56717 654 RLLILDDatsALDAGNQLRVQRLL---YESPEwASRTVLLITQQL 695
Cdd:PRK13546 163 DILVIDE---ALSVGDQTFAQKCLdkiYEFKE-QNKTIFFVSHNL 203
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
205-473 |
4.82e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 52.12 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 205 DWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSR----VHGEVFRAVLHQETGFFLKNPTGSITSRV 280
Cdd:cd18580 23 DWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRasrrLHDKLLRSVLRAPMSFFDTTPSGRILNRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 281 TEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTllslPLLFLLPRRLGKVYQSLA--VKVQESLAKS--- 355
Cdd:cd18580 103 SKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL----PPLLVVYYLLQRYYLRTSrqLRRLESESRSply 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 356 TQVaLEALSAMPTVRSFANEEGEAQKFRQKLEE-MKPLNkkeaLAYVTEVW-----TMSVSGMLLKVGILylggqLVVRG 429
Cdd:cd18580 179 SHF-SETLSGLSTIRAFGWQERFIEENLRLLDAsQRAFY----LLLAVQRWlglrlDLLGALLALVVALL-----AVLLR 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 56717 430 AVSSGNLVSFVLYQ-LQFTRAVEVLLSIYPSMQKSVGASEKIFEY 473
Cdd:cd18580 249 SSISAGLVGLALTYaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
203-470 |
7.29e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 51.74 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 203 ITDWILQDKTAPSFA--------RNM---WLMCILTIASTVLEFAGDGIYNITMG----HMHSRVHGEVFRAVLHQETGF 267
Cdd:cd18564 25 VIDDVLGDKPLPGLLglapllgpDPLallLLAAAALVGIALLRGLASYAGTYLTAlvgqRVVLDLRRDLFAHLQRLSLSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 268 FLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVK 347
Cdd:cd18564 105 HDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASRE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 348 VQESLAKSTQVALEALSAMPTVRSFANEEGEAQKF----RQKLEE-MKPLNKKEALAYVTEVwTMSVSGMLlkvgILYLG 422
Cdd:cd18564 185 QRRREGALASVAQESLSAIRVVQAFGREEHEERRFarenRKSLRAgLRAARLQALLSPVVDV-LVAVGTAL----VLWFG 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 56717 423 GQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18564 260 AWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
498-666 |
7.29e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 498 QDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPL-VQY-DHHYlhtqvAA 575
Cdd:PRK11147 323 ENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLeVAYfDQHR-----AE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 576 VGQEpllfgRSFRENIAYGltrtptMEEITAVAMESGAHDFISGF---PQGYDTEVgetgNQLSGGQRQAVALARALIRK 652
Cdd:PRK11147 394 LDPE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKP 458
|
170
....*....|....
gi 56717 653 PRLLILDDATSALD 666
Cdd:PRK11147 459 SNLLILDEPTNDLD 472
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
509-565 |
8.30e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 8.30e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQN--LYQPTGGKVLLDGEPLVQYD 565
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE 77
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
519-677 |
2.03e-06 |
|
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: 50.94 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 519 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPLVQYDHHYLHTQVAAVGQEPLlfgrsfRENIAYGLTRT 598
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFL------RSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 599 PTMEEITavamesgahdfisgFPQG----YDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ 674
Cdd:COG1245 434 YYKTEII--------------KPLGleklLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
...
gi 56717 675 RLL 677
Cdd:COG1245 496 KAI 498
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
523-720 |
2.43e-06 |
|
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: 48.34 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 523 GKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDgeplvqydhhylhtqvaavgqepllfgrsfRENIAYGltrtptme 602
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------------------------GITPVYK-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 603 eitavamesgahdfisgfPQGYDtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPE 682
Cdd:cd03222 67 ------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 56717 683 WASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQ 720
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQ 157
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
500-722 |
2.60e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.19 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 500 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVA----ALLQNLYQPTGGKVLLDGEPLVQYD----HHYLHT 571
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLLRLSprerRKLVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 572 QVAAVGQEPLL-------FGRSFRENIA-----------YGLTRTPTMEEITAVAMESgAHDFISGFPQgydtevgetgn 633
Cdd:PRK15093 90 NVSMIFQEPQScldpserVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD-HKDAMRSFPY----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 634 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSV 712
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADKINVLYCGQT 237
|
250
....*....|
gi 56717 713 CEQGTHLQLM 722
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
195-461 |
3.27e-06 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 49.42 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNitmgHMHSRVHGE----VFRAVLHQETGFFLK 270
Cdd:cd18588 20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFS----HTTNRIDAElgarLFRHLLRLPLSYFES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 271 NPTGSITSRVTEdtsnvCESISDklnlFLwyLGRGLCL----------LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 340
Cdd:cd18588 96 RQVGDTVARVRE-----LESIRQ----FL--TGSALTLvldlvfsvvfLAVMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 341 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEegeaQKFRQKLEEMkplnkkeaLA-YVTEV--------WTMSVSG 411
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVE----PQFQRRWEEL--------LArYVKASfktanlsnLASQIVQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 56717 412 MLLK---VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQ 461
Cdd:cd18588 233 LIQKlttLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQ 285
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
221-447 |
4.01e-06 |
|
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: 49.49 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 221 WLMCILTIASTVLEFAGDGIYNITMGH-----MHS-RVhgEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDK 294
Cdd:cd18565 54 WLLGGLTVAAFLLESLFQYLSGVLWRRfaqrvQHDlRT--DTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 295 LNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAK-STQvaLE-ALSAMPTVRSF 372
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNAR--LEnNLSGIAVIKAF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 373 ANEEGEAQKFRQKLEEMKPLNK---KEALAYVTEVWTMSVSGMLLkvgILYLGGQLVVRGAV------SSGNLVSFVLYQ 443
Cdd:cd18565 210 TAEDFERERVADASEEYRDANWraiRLRAAFFPVIRLVAGAGFVA---TFVVGGYWVLDGPPlftgtlTVGTLVTFLFYT 286
|
....
gi 56717 444 LQFT 447
Cdd:cd18565 287 QRLL 290
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
512-666 |
5.79e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 5.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylHTQVAAVGQE-PLLF------- 583
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQEtPALPqpaleyv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 584 ---GRSFRE-----------NIAYGL-TRTPTMEEITAVAMESGAHDFIS--GFPQgydTEVGETGNQLSGGQRQAVALA 646
Cdd:PRK10636 85 idgDREYRQleaqlhdanerNDGHAIaTIHGKLDAIDAWTIRSRAASLLHglGFSN---EQLERPVSDFSGGWRMRLNLA 161
|
170 180
....*....|....*....|
gi 56717 647 RALIRKPRLLILDDATSALD 666
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
517-712 |
9.34e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 517 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhyLHTQVAAV-----------GQEPLLFGR 585
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 SFRENIAygltrtptmeeITAVAMESGAHDFISGfpqGYDTEVGET-----------GNQ----LSGGQRQAVALARALI 650
Cdd:PRK11288 347 SVADNIN-----------ISARRHHLRAGCLINN---RWEAENADRfirslniktpsREQlimnLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 651 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL----SLAERahhILFLKEGSV 712
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLpevlGVADR---IVVMREGRI 474
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
601-666 |
1.01e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 601 MEEITAVAMESGAHDFISGFPQGYDTEVGETgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQVKAT-KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
635-713 |
1.19e-05 |
|
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: 48.67 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 635 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYespEWASRTVLLITQQLSLAE---RAHHILFLKEGS 711
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLIN---QLAQEGVAIIVVSSELAEvlgLSDRVLVIGEGK 480
|
..
gi 56717 712 VC 713
Cdd:TIGR02633 481 LK 482
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
226-388 |
1.24e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 47.85 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 226 LTIASTVLEFAGdGIYNITMGHMHSRV-HGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgr 304
Cdd:cd18606 44 LGVLQAIFLFLF-GLLLAYLGIRASKRlHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFL----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 305 glcLLAFMIWGSFYLTVVT----LLSLPLLFLLPRRLGKVYQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFanee 376
Cdd:cd18606 118 ---YTLSSIIGTFILIIIYlpwfAIALPPLLVLYYFIANYYRASSreLKRLESILRSFVYANfsESLSGLSTIRAY---- 190
|
170
....*....|..
gi 56717 377 GEAQKFRQKLEE 388
Cdd:cd18606 191 GAQDRFIKKNEK 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
494-666 |
1.53e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 494 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLyqptGGKVLLD---------------- 557
Cdd:PRK11147 3 LISIHGAWLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKST---LMKIL----NGEVLLDdgriiyeqdlivarlq 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 558 ----------------------GEPLVQYdHHYLHTqvaaVGQEPllfgrsfRENIaygLTRTPTMEEITAVA----MES 611
Cdd:PRK11147 73 qdpprnvegtvydfvaegieeqAEYLKRY-HDISHL----VETDP-------SEKN---LNELAKLQEQLDHHnlwqLEN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 56717 612 GAHDFISGFPQGYDTEVGEtgnqLSGG-QRQAvALARALIRKPRLLILDDATSALD 666
Cdd:PRK11147 138 RINEVLAQLGLDPDAALSS----LSGGwLRKA-ALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
194-461 |
1.78e-05 |
|
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: 47.20 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 194 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 273
Cdd:cd18782 19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 274 GSITSRVTEdtsnvcesiSDKLNLFLwyLGRGLCL----------LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQS 343
Cdd:cd18782 99 GELSTRISE---------LDTIRGFL--TGTALTTlldvlfsviyIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 344 LAVKVQESLAKSTQVALEALSAMPTVRSFANEEgeaqKFRQKLEEmkplnkkEALAYVTEVWTMSVSGMLL--------- 414
Cdd:cd18782 168 QIRRRAEASAKTQSYLVESLTGIQTVKAQNAEL----KARWRWQN-------RYARSLGEGFKLTVLGTTSgslsqflnk 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 56717 415 --KVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQ 461
Cdd:cd18782 237 lsSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQ 285
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
516-668 |
4.73e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.58 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 516 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqydhhylhtqvaavgqepLLFGRSFRENIAYGL 595
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK---------------------EINALSTAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 596 TRTPTMEEITAVAMESG--------AHDFISGFPQ-GYDTEVGET-----------GNQ----LSGGQRQAVALARALIR 651
Cdd:PRK15439 341 VYLPEDRQSSGLYLDAPlawnvcalTHNRRGFWIKpARENAVLERyrralnikfnhAEQaartLSGGNQQKVLIAKCLEA 420
|
170
....*....|....*..
gi 56717 652 KPRLLILDDATSALDAG 668
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVS 437
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
518-679 |
6.54e-05 |
|
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: 46.32 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 518 FTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPlvQYD---HHYLHTQVaavgQEPLlfgrsfr 588
Cdd:COG1245 88 FRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEP--SWDevlKRFRGTEL----QDYF------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 589 ENIAYGltrtptmeEITaVAMESGAHDFIsgfPQGYDTEVG-------ETG-------------------NQLSGGQRQA 642
Cdd:COG1245 153 KKLANG--------EIK-VAHKPQYVDLI---PKVFKGTVRellekvdERGkldelaeklglenildrdiSELSGGELQR 220
|
170 180 190
....*....|....*....|....*....|....*..
gi 56717 643 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 679
Cdd:COG1245 221 VAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
488-677 |
6.80e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.84 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 488 PLNMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHh 567
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEP---VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 568 ylHTQVAAVGQEPLLFGR-SFRENIAY--GLT-RTPTMEEITAVAmesgahdfISGFPQGYDTEVgetgNQLSGGQRQAV 643
Cdd:PRK13543 81 --SRFMAYLGHLPGLKADlSTLENLHFlcGLHgRRAKQMPGSALA--------IVGLAGYEDTLV----RQLSAGQKKRL 146
|
170 180 190
....*....|....*....|....*....|....
gi 56717 644 ALARALIRKPRLLILDDATSALDAGNQLRVQRLL 677
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
483-726 |
8.62e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 483 SGSLAPLNMKGLVKfqdvsfaypNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvAALLQNLYQPTGGKvlldgEP-- 560
Cdd:NF000106 8 NGARNAVEVRGLVK---------HFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR-----RPwr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 561 LVQYDHHYLHTQVAAVGQEPLLFGR----SFRENIaYGLTRTPTMEEITAVAMesgAHDFISGFpqGYDTEVGETGNQLS 636
Cdd:NF000106 73 F*TWCANRRALRRTIG*HRPVR*GRresfSGRENL-YMIGR*LDLSRKDARAR---ADELLERF--SLTEAAGRAAAKYS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 637 GGQRQAVALARALIRKPRLLILDDATSALDAgnqlRVQRLLYESPEWASR---TVLLITQQLSLAER-AHHILFLKEGSV 712
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDP----RTRNEVWDEVRSMVRdgaTVLLTTQYMEEAEQlAHELTVIDRGRV 222
|
250
....*....|....
gi 56717 713 CEQGTHLQLMERGG 726
Cdd:NF000106 223 IADGKVDELKTKVG 236
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
509-677 |
9.43e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG-------EPLVQYDHHYLHTQVAAVGQEPL 581
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 582 LFGRSFRENIaygltrtptmEEITAVAMESGAHDFISgfpqgydtevgETGNQLSGGQRQAVALARALIRKPRLLILDDA 661
Cdd:PRK13541 92 KFWSEIYNSA----------ETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
170
....*....|....*.
gi 56717 662 TSALDAGNQLRVQRLL 677
Cdd:PRK13541 151 ETNLSKENRDLLNNLI 166
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
512-677 |
9.46e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 512 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqnlyqpTGGkvlldgeplvqydhhylHTQvaAVGQEPLLFGR------ 585
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGD-----------------HPQ--GYSNDLTLFGRrrgsge 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 586 ---SFRENIAYgLTRTPTME-----EITAVAMeSGAHDFISGFPQ----------------GYDTEVGETGNQ-LSGGQR 640
Cdd:PRK10938 330 tiwDIKKHIGY-VSSSLHLDyrvstSVRNVIL-SGFFDSIGIYQAvsdrqqklaqqwldilGIDKRTADAPFHsLSWGQQ 407
|
170 180 190
....*....|....*....|....*....|....*..
gi 56717 641 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLL 677
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
267-470 |
9.93e-05 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 45.10 E-value: 9.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 267 FFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAV 346
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 347 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLE--EMKPLNKKEALAY-VTEVWTMSVSGMLLKVGIlylGG 423
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGhfLTRALKHTRWNAKtFSAVNTITDLAPLLVIGF---AA 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 56717 424 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18554 253 YLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
197-464 |
1.27e-04 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 44.52 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 197 PFFTGRITDwILQDKTAPSFARNMW---LMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 273
Cdd:cd18560 16 PLFLGRAVN-ALTLAKVKDLESAVTlilLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 274 GSITSRVTEDTsnvcESISDKLNLFLWYLGR-----GLCLLAFMIWGSFYLTVVTLLSLPllfllprrlgkVYQSLAVKV 348
Cdd:cd18560 95 GEVVRIMDRGT----ESANTLLSYLVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSVL-----------LYGVFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 349 QESLAK-----------STQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVG 417
Cdd:cd18560 160 TEWRTKfrraankkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 56717 418 ILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSV 464
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
361-470 |
1.65e-04 |
|
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: 44.40 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 361 EALSAMPTVRSFANEEGEAQKFRQkleemkpLNKKEALAYVTEVWTMSV-------SGMLLKVGILYLGGQLVVRGAVSS 433
Cdd:cd18546 183 ETLAGIRVVQAFRRERRNAERFAE-------LSDDYRDARLRAQRLVAIyfpgvelLGNLATAAVLLVGAWRVAAGTLTV 255
|
90 100 110
....*....|....*....|....*....|....*..
gi 56717 434 GNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18546 256 GVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
518-691 |
2.21e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 518 FTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPlvQYDH---HYLHTQvaavgqeplLFgrSFR 588
Cdd:PRK13409 88 FKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEP--SWDEvlkRFRGTE---------LQ--NYF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 589 ENIAYGltrtptmeEITAVamesgaH-----DFIsgfPQGYDTEVG-------ETG-------------------NQLSG 637
Cdd:PRK13409 153 KKLYNG--------EIKVV------HkpqyvDLI---PKVFKGKVRellkkvdERGkldevverlglenildrdiSELSG 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 56717 638 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLI 691
Cdd:PRK13409 216 GELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVV 267
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
634-668 |
3.56e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 3.56e-04
10 20 30
....*....|....*....|....*....|....*
gi 56717 634 QLSGGQRQAVALARALIRKPRLLILDDATSALDAG 668
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
360-450 |
5.01e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 42.83 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 360 LEALSAMPTVRSFANEEGEAQKFRQKLEEMkpLNKKEALAYVTeVWTMSVSGMLL---KVGILYLGGQLVVRGAVSSGNL 436
Cdd:cd18567 184 LETIRGIQTIKLFGREAEREARWLNLLVDA--INADIRLQRLQ-ILFSAANGLLFgleNILVIYLGALLVLDGEFTVGML 260
|
90
....*....|....
gi 56717 437 VSFVLYQLQFTRAV 450
Cdd:cd18567 261 FAFLAYKDQFSSRA 274
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
495-727 |
5.41e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 495 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqnlyqpTGGKVLLDGEPLV----QYDHHYLh 570
Cdd:NF033858 2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AGARKIQQGRVEVlggdMADARHR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 571 tqvAAVGQE----PLLFGR------SFRENIA-----YGLTRTPTMEEITAVAMESGAHDFISGfPQGydtevgetgnQL 635
Cdd:NF033858 72 ---RAVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAAERRRRIDELLRATGLAPFADR-PAG----------KL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 636 SGGQRQAVALARALIRKPRLLILDDATSALD--AGNQ-------LRVQRllyespewASRTVLLITQQLSLAERAHHILF 706
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRRQfwelidrIRAER--------PGMSVLVATAYMEEAERFDWLVA 209
|
250 260
....*....|....*....|.
gi 56717 707 LKEGSVCEQGTHLQLMERGGC 727
Cdd:NF033858 210 MDAGRVLATGTPAELLARTGA 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
530-666 |
6.36e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 530 GPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqyDHHYLHT--QVAAVGQEPLLFGR-SFRENIA-----YGLTRTPTM 601
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATrrRVGYMSQAFSLYGElTVRQNLElharlFHLPAAEIA 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56717 602 EEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 666
Cdd:NF033858 376 ARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
267-470 |
6.71e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 42.47 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 267 FFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAV 346
Cdd:cd18540 92 YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 347 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEAL---AYVTEVWTMSVSGMLLkvgILYLGG 423
Cdd:cd18540 172 KVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARlsaLFLPIVLFLGSIATAL---VLWYGG 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 56717 424 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18540 249 ILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
491-696 |
1.26e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 491 MKGLVKFQDVSFAYP--NHPNVQV---------------LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 553
Cdd:PRK13545 1 MNYKVKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 554 VLLDGEPLVQYDHHYLHTQVAAVgqepllfgrsfrENIAY-GLTRTPTMEEITAVAmesgahdfisgfPQGYD-TEVGET 631
Cdd:PRK13545 81 VDIKGSAALIAISSGLNGQLTGI------------ENIELkGLMMGLTKEKIKEII------------PEIIEfADIGKF 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56717 632 GNQ----LSGGQRQAVALARALIRKPRLLILDDatsALDAGNQLRVQRLLYESPEWAS--RTVLLITQQLS 696
Cdd:PRK13545 137 IYQpvktYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNEFKEqgKTIFFISHSLS 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
490-680 |
1.60e-03 |
|
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: 42.31 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 490 NMKGLVKFQDVSFAYPNHPNVQVlQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYL 569
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 570 HTQVAAVGQ----EPLLFGRsfrENI-AYGLTRTPTMEEITAVAMESgahdfISGFpqGYDTEVGETGNQLSGGQRQAVA 644
Cdd:TIGR01257 2011 HQNMGYCPQfdaiDDLLTGR---EHLyLYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLS 2080
|
170 180 190
....*....|....*....|....*....|....*.
gi 56717 645 LARALIRKPRLLILDDATSALDAgnqlRVQRLLYES 680
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDP----QARRMLWNT 2112
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
623-679 |
2.55e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 2.55e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 56717 623 GYDTEVGetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 679
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE 436
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
524-556 |
3.63e-03 |
|
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.
Pssm-ID: 459814 [Multi-domain] Cd Length: 193 Bit Score: 39.06 E-value: 3.63e-03
10 20 30
....*....|....*....|....*....|...
gi 56717 524 KVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL 556
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLL 33
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
503-538 |
5.08e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 39.36 E-value: 5.08e-03
10 20 30
....*....|....*....|....*....|....*..
gi 56717 503 AYPNH-PNVQVLQGLTFTlypGKVTALVGPNGSGKST 538
Cdd:COG3910 19 AYPFNlPAVRNLEGLEFH---PPVTFFVGENGSGKST 52
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
509-547 |
6.00e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 6.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 56717 509 NVQVLQGLTFTLYPGkVTALVGPNGSGKST-VAALLQNLY 547
Cdd:pfam13476 5 NFRSFRDQTIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
251-387 |
6.00e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 39.44 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 251 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTllslPLL 330
Cdd:cd18605 76 RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLL----LPL 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 56717 331 FLLPRRLGKVYQSLA--VKVQESLAKS---TQVAlEALSAMPTVRSFANEEGEAQKFRQKLE 387
Cdd:cd18605 152 AFIYYRIQRYYRATSreLKRLNSVNLSplyTHFS-ETLKGLVTIRAFRKQERFLKEYLEKLE 212
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-537 |
6.39e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 6.39e-03
10 20
....*....|....*....|.
gi 56717 517 TFTLYPGkVTALVGPNGSGKS 537
Cdd:COG1196 19 TIPFEPG-ITAIVGPNGSGKS 38
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
195-470 |
6.40e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 39.42 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 195 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAgDGIYNITMG-HMHSRVHGEVFRAVLHQETGFFLKNPT 273
Cdd:cd18555 20 LIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFL-RGYIIIKLQtKLDKSLMSDFFEHLLKLPYSFFENRSS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 274 GSITSRVTED-------TSNVCESISDKLNLFLwylgrglcLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLav 346
Cdd:cd18555 99 GDLLFRANSNvyirqilSNQVISLIIDLLLLVI--------YLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKL-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56717 347 kVQESLAKSTQVA---LEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA--LAYVTevwTMSVS-GMLLKVGILY 420
Cdd:cd18555 169 -NQEEIVAQTKVQsylTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKErlSNILN---SISSSiQFIAPLLILW 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 56717 421 LGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 470
Cdd:cd18555 245 IGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
518-539 |
6.51e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 6.51e-03
10 20
....*....|....*....|..
gi 56717 518 FTLYPGKVTALVGPNGSGKSTV 539
Cdd:COG4637 16 LELPLGPLTVLIGANGSGKSNL 37
|
|
| |
