|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-717 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 1021.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 2 AAHAWPTAALLLLLVDWLLLRPVLPGIFSLLVP-EVPLLRVWAVGLSRWAILGLGVRGVLGVTAGarGWLAALQPLVAAL 80
Cdd:TIGR00958 1 AALAYLLPWFSLLLVDWALLRDLLQGIFGLLLPfEKGLYVLWLEGTLRLGVLWLGALGILLNKAG--GLLAAVKPLVAAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 81 GLALPGLASFRKLSAWGALREGDNAGLLHWNsrldAFVLSYVAALPAAALWHKLGGFWAP-----SGHKGAGDMLCRMLG 155
Cdd:TIGR00958 79 CLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETADLLFRLLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 156 FLDSKKGRLHLVLVLLILSCLGEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHS 235
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 315
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 316 FLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVS 395
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 396 GMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLN 475
Cdd:TIGR00958 395 GMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLH 555
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALI 635
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 636 RKPRLLILDDATSALDAgnqlRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 715
Cdd:TIGR00958 634 RKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
..
gi 158262052 716 MV 717
Cdd:TIGR00958 710 LV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
178-719 |
2.00e-141 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 426.89 E-value: 2.00e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNP 257
Cdd:COG1132 37 ELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 258 TGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESL 337
Cdd:COG1132 117 TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEAL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 338 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAVS 417
Cdd:COG1132 197 AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 418 SGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP-CSPLSGSLAPLNMKGLVKFQDVSFAYPnhPNVQ 496
Cdd:COG1132 277 VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeIPDPPGAVPLPPVRGEIEFENVSFSYP--GDRP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI 576
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGLtRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQL 656
Cdd:COG1132 435 RYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 657 RVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:COG1132 514 LIQEALER--LMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRL 574
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
177-455 |
4.84e-135 |
|
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: 399.54 E-value: 4.84e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 256
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 257 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 336
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 337 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 158262052 417 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
469-697 |
2.32e-120 |
|
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: 359.48 E-value: 2.32e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 469 GSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQ 548
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 549 YDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 628
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
179-718 |
1.87e-110 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 350.67 E-value: 1.87e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKTAPSfarnMWLMCILTVASTALEFAGDGIYNITMGHMHSRV----HGEVFRAVLHQETGFFL 254
Cdd:COG2274 173 LATPLFTQVVIDRVLPNQDLST----LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIdlrlSSRFFRHLLRLPLSFFE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTeDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:COG2274 249 SRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREES 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGILYLGGQLVVR 413
Cdd:COG2274 328 EASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKlRRLSNLLSTLSGLLQQLAT-VALLWLGAYLVID 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 414 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP-CSPLSGSLAPLNMKGLVKFQDVSFAYPNH 492
Cdd:COG2274 407 GQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 493 pNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSF 572
Cdd:COG2274 487 -SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTI 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 573 RENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:COG2274 566 RENITLGDP-DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 653 GNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 718
Cdd:COG2274 645 ETEAIILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
480-719 |
1.80e-95 |
|
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: 295.60 E-value: 1.80e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGRSFRENIAYGLTRtPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
241-718 |
7.83e-93 |
|
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: 300.46 E-value: 7.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 241 VFRAVLHQETGFFLKNPTGSITSRVTEDT----SNVCESISDKLNLFLWYLGRglclLAFMIWGSFYLTVVTLLSLPLLF 316
Cdd:TIGR02204 97 VFAHLISLSPSFFDKNRSGEVVSRLTTDTtllqSVIGSSLSMALRNALMCIGG----LIMMFITSPKLTSLVLLAVPLVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 317 LLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK--EALAYVTE-VWTMS 393
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQriRTRALLTAiVIVLV 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 394 VSGMllkVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP--CSPLSGSL 471
Cdd:TIGR02204 253 FGAI---VGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 472 APLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDH 551
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 552 HYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTpTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALA 631
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIA 488
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 632 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:TIGR02204 489 RAILKDAPILLLDEATSALDAESEQLVQQALETL--MKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG 566
|
....*..
gi 158262052 712 CYRSMVE 718
Cdd:TIGR02204 567 LYARLAR 573
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
239-713 |
9.50e-89 |
|
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: 289.31 E-value: 9.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 239 GEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLL 318
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 319 PRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKF-----RQKLEEMKPLNKKEALAYVTEVWTMS 393
Cdd:TIGR02203 171 MRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFdavsnRNRRLAMKMTSAGSISSPITQLIASL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 394 VSGMLLkvgilYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPcSPLSGSLAP 473
Cdd:TIGR02203 251 ALAVVL-----FIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP-EKDTGTRAI 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHY 553
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 LHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARA 633
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCY 713
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
177-455 |
5.06e-80 |
|
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: 257.09 E-value: 5.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 256
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 257 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 336
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 337 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 158262052 417 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18572 251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
345-711 |
3.67e-77 |
|
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: 258.53 E-value: 3.67e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 345 LEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKPLnkKEAL--AYVTEVWTM-SVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:COG4988 201 LDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtMKVL--RVAFlsSAVLEFFASlSIALVAVYIGFRLLGGSLTLFAAL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 417 ssgnlvsFVLYqLqftrAVEVLLSI-------YPSMQkSVGASEKIFEYLDRTPCSPLSGSL-APLNMKGLVKFQDVSFA 488
Cdd:COG4988 279 -------FVLL-L----APEFFLPLrdlgsfyHARAN-GIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFS 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 489 YPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLF 568
Cdd:COG4988 346 YPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLF 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 569 GRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:COG4988 424 AGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 649 ALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
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 ... |
177-455 |
5.56e-75 |
|
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: 243.76 E-value: 5.56e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTAleFAG--DGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 254
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSV--AAGirGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:cd18784 89 TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:cd18784 169 DSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 158262052 415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18784 249 QISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
353-716 |
5.72e-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: 253.59 E-value: 5.72e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 353 TVRSFANEEGEAQKFRQKLEEmkplnkKEALAyvTEVWTmsvSGMLLKVG-----------ILYLGGQLVVRGAVSSGNL 421
Cdd:COG5265 230 TVKYFGNEAREARRYDEALAR------YERAA--VKSQT---SLALLNFGqaliialgltaMMLMAAQGVVAGTMTVGDF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 422 VSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLNMK-GLVKFQDVSFAYpnHPNVQVLQG 500
Cdd:COG5265 299 VLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGgGEVRFENVSFGY--DPERPILKG 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGl 580
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG- 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 581 tRtP--TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRV 658
Cdd:COG5265 456 -R-PdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 659 QRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:COG5265 534 QAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
203-716 |
1.85e-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: 1.85e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 203 RNMWLMCILTVASTAL---EFAGDGIYNITMGHMHSRVHGEV----FRAVLHQETGFFLKNPTGSITSRVTEdTSNVCES 275
Cdd:TIGR01846 173 RGLSTLSVLALAMLAVaifEPALGGLRTYLFAHLTSRIDVELgarlYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNF 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 276 ISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVR 355
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 356 SFANEEGEAQKFRQKLEemkplnkkealAYVTEVWTMSVSGMLLKVGI-----------LYLGGQLVVRGAVSSGNLVSF 424
Cdd:TIGR01846 332 ATATEPQFQNRWDRQLA-----------AYVAASFRVTNLGNIAGQAIeliqkltfailLWFGAHLVIGGALSPGQLVAF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 425 VLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDrTPCSPLSGSLAPL-NMKGLVKFQDVSFAY-PNHPnvQVLQGLT 502
Cdd:TIGR01846 401 NMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALpELRGAITFENIRFRYaPDSP--EVLSNLN 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 503 FTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTR 582
Cdd:TIGR01846 478 LDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 583 TPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLL 662
Cdd:TIGR01846 558 AP-FEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNM 636
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 158262052 663 YESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:TIGR01846 637 REIC--RGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
480-716 |
3.38e-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: 239.83 E-value: 3.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
478-711 |
9.52e-74 |
|
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: 238.28 E-value: 9.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 478 GLVKFQDVSFAY-PNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHT 556
Cdd:cd03254 1 GEIEFENVNFSYdEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIR 636
Cdd:cd03254 78 MIGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
480-716 |
2.36e-73 |
|
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: 237.51 E-value: 2.36e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
332-718 |
1.28e-69 |
|
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: 238.13 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA-LAYVTEVWTMSVSGMLLkVGILYLGGQL 410
Cdd:COG4987 186 RLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLArLSALAQALLQLAAGLAV-VAVLWLAAPL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 411 VVRGAVSSGNLVSFVLyqlqFTRAV-EVLLSIYPSMQ---KSVGASEKIFEYLDRTPCSPLSGSLAPLNMKGLVKFQDVS 486
Cdd:COG4987 265 VAAGALSGPLLALLVL----AALALfEALAPLPAAAQhlgRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVS 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 487 FAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPL 566
Cdd:COG4987 341 FRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPH 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 567 LFGRSFRENIAygLTR-TPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:COG4987 420 LFDTTLRENLR--LARpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDE 497
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 646 ATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 718
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 ... |
480-718 |
1.35e-69 |
|
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: 227.75 E-value: 1.35e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQV 558
Cdd:cd03252 1 ITFEHVRFRYkPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEPLLFGRSFRENIAygLTRT-PTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 637
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIA--LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMV 717
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
.
gi 158262052 718 E 718
Cdd:cd03252 235 Q 235
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
227-713 |
1.77e-69 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 238.38 E-value: 1.77e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 227 NITMgHMHSRVhgevFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTV 306
Cdd:PRK11176 95 KVVM-TMRRRL----FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 307 VTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYV 386
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 387 TEVWTMSVSGMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPcSP 466
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ-EK 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 467 LSGSLAPLNMKGLVKFQDVSFAYP--NHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 544
Cdd:PRK11176 329 DEGKRVIERAKGDIEFRNVTFTYPgkEVP---ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 545 LLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQ 624
Cdd:PRK11176 406 DLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHL 704
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHA 563
|
....*....
gi 158262052 705 QLMERGGCY 713
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 ... |
177-455 |
3.75e-67 |
|
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: 222.82 E-value: 3.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 256
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 257 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 336
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 337 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 158262052 417 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
480-695 |
4.28e-65 |
|
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: 213.01 E-value: 4.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPR 639
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
344-711 |
1.50e-62 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 219.45 E-value: 1.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 344 ALEALSAMPTVRSFANEEGEAQKFRQKLEEMkplnkkeaLAYVTEV--WTMSVSGM------LLKVGILYLGGQLVVRGA 415
Cdd:PRK13657 198 VSDAIGNVSVVQSYNRIEAETQALRDIADNL--------LAAQMPVlsWWALASVLnraastITMLAILVLGAALVQKGQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 416 VSSGNLVSFV-LYQLQFTRaVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPL-NMKGLVKFQDVSFAYPNHP 493
Cdd:PRK13657 270 LRVGEVVAFVgFATLLIGR-LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLgRVKGAVEFDDVSFSYDNSR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 nvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFR 573
Cdd:PRK13657 349 --QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 574 ENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK13657 427 DNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 654 NQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:PRK13657 506 TEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
252-719 |
8.90e-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: 208.83 E-value: 8.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 252 FFLKNPTGSITSRVTeDTSNVCESI-SDKLNLFL--WYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRrlgKVYQS 328
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFK---RTFNK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 329 LAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMkpLNKkeALAYV-TEVWTM---SVSGMLLKVGIL 404
Cdd:TIGR01193 322 LNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDY--LNK--SFKYQkADQGQQaikAVTKLILNVVIL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFE-YLDRTPCSPLSGSLAPLNMKGLVKFQ 483
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINKKKRTELNNLNGDIVIN 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 484 DVSFAYPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQ 563
Cdd:TIGR01193 478 DVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 EPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLIL 643
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 644 DDATSALDAgnqLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:TIGR01193 636 DESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
478-701 |
9.37e-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: 195.50 E-value: 9.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 478 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQ 557
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPLLFGRSFRENIAYGLTRTpTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 637
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLA-DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQG 701
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
177-435 |
1.18e-54 |
|
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: 189.01 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMC--ILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 254
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPDGDPETQALNVYSLAllLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 158262052 415 AVSSGNLVSFVLYQLQFTRAV 435
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
397-697 |
2.59e-53 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 193.43 E-value: 2.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 397 MLLKVGILYLGGQLVVRGAVSSGNLV--SFVLyqlqfTRA---VEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSL 471
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAMIaaSILM-----GRAlapIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPL 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 472 -APlnmKGLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYD 550
Cdd:COG4618 325 pRP---KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 551 HHYLHTQVAAVGQEPLLFGRSFRENIAygltR--TPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 628
Cdd:COG4618 401 REELGRHIGYLPQDVELFDGTIAENIA----RfgDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRI 476
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 629 ALARALIRKPRLLILDDATSALD-AGNQLRVQRLLyespEWASR--TVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDdEGEAALAAAIR----ALKARgaTVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
401-719 |
7.77e-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: 192.41 E-value: 7.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 401 VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPL-NMKGL 479
Cdd:TIGR01192 255 MCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELpNVKGA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:TIGR01192 335 VEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGRSFRENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:TIGR01192 413 TVFQDAGLFNRSIRENIRLGRE-GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAP 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
240-724 |
8.41e-53 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 192.63 E-value: 8.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 240 EVFRAVLHQETGFFLKNPTGSITSRVTEDTsnvcESISDklnLFLWYLG---RGLCLLAFMIWGSFYLTVVTLLSLPLLF 316
Cdd:PRK10790 103 DVMDAALRQPLSAFDTQPVGQLISRVTNDT----EVIRD---LYVTVVAtvlRSAALIGAMLVAMFSLDWRMALVAIMIF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 317 LLPRRLGKVYQSLAV----KVQESLAKSTQVALEALSAMPTVrsfaneegeaQKFRQKLEEMKPLNKKEALAYVTEVWTM 392
Cdd:PRK10790 176 PAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVI----------QQFRQQARFGERMGEASRSHYMARMQTL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 393 SVSGMLLK-----------VGILYLGGqLVVRGAVSSGNLVSFVLYqlqFTRAVEVL--LSIYPSM-QKSVGASEKIFEY 458
Cdd:PRK10790 246 RLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISY---LGRLNEPLieLTTQQSMlQQAVVAGERVFEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 459 LDRtPCSPLSGSLAPLNmKGLVKFQDVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 538
Cdd:PRK10790 322 MDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 539 VLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGltRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGN 618
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGN 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVC 698
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQAV 553
|
490 500 510
....*....|....*....|....*....|..
gi 158262052 699 EQGTHLQLMERGGCYRSMV------EALAAPS 724
Cdd:PRK10790 554 EQGTHQQLLAAQGRYWQMYqlqlagEELAASV 585
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
177-455 |
2.16e-49 |
|
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: 174.83 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTAleFAG--DGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 254
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSL--SAGlrGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:cd18590 89 KTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:cd18590 169 DSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 158262052 415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18590 249 HLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
397-702 |
5.22e-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: 177.93 E-value: 5.22e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 397 MLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAplNM 476
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLP--EP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 477 KGLVKFQDVSFAYPNhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHT 556
Cdd:TIGR01842 314 EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLLFGRSFRENIAYgLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIR 636
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 637 KPRLLILDDATSALD-AGNQLRVQRLLyeSPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDeEGEQALANAIK--ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
407-716 |
6.71e-48 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 178.37 E-value: 6.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 407 GGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSpLSGSLAPLNMKGLVKFQDVS 486
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEGRGELDVNIRQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 487 FAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPL 566
Cdd:PRK10789 321 FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 567 LFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDA 646
Cdd:PRK10789 400 LFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 647 TSALDAGNQlrvQRLLYESPEW-ASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:PRK10789 479 LSAVDGRTE---HQILHNLRQWgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
449-692 |
1.46e-47 |
|
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: 176.32 E-value: 1.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 449 VGASEKIFEYLDRT--PCSPLSGSLAPLNMKglVKFQDVSFAYPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAA 526
Cdd:TIGR02857 291 VAAAEALFAVLDAAprPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 527 LLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFP 606
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 607 QGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERA 686
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523
|
....*.
gi 158262052 687 HHILFL 692
Cdd:TIGR02857 524 DRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
478-702 |
1.78e-45 |
|
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: 161.89 E-value: 1.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 478 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQ 557
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPLLFGRSFRENIAygltrtP----TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARA 633
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLItqqlslaerAHH---------ILFLKEGSVCEQGT 702
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTI---------AHRldtiidsdrILVLDKGRVVEFDS 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
479-702 |
9.80e-44 |
|
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: 158.28 E-value: 9.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQV 558
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEPLL-FGRSFRENIAYGltRTPTM----------EEITAVAMES-GAHDFIsgfpqgyDTEVgetgNQLSGGQRQ 626
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALG--RYPHLglfgrpsaedREAVEEALERtGLEHLA-------DRPV----DELSGGERQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
498-648 |
1.84e-43 |
|
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: 153.57 E-value: 1.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGR-SFRENI 576
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 577 AYGLtrtpTMEEITAVAMESGAHDFISGFPQGY--DTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:pfam00005 81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
480-702 |
7.09e-43 |
|
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: 154.80 E-value: 7.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPL--LFGRSFRENIAYGLTRT----PTMEEITAVAMES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 632
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLglprEEIRERVEEALELvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
442-716 |
2.61e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 162.32 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 442 YPSMQKSVGASEKIFEYLDrTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGK 521
Cdd:PRK11174 311 YHAKAQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 522 ST-VAALLQNL-YQptgGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGltrTPTM--EEITAVAMESG 597
Cdd:PRK11174 390 TSlLNALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG---NPDAsdEQLQQALENAW 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 598 AHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLIT 677
Cdd:PRK11174 464 VSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVT 541
|
250 260 270
....*....|....*....|....*....|....*....
gi 158262052 678 QQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:PRK11174 542 HQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
395-680 |
1.32e-41 |
|
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: 159.45 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 395 SGMLLKVGILYLGGQLVVRGAVSSGN-----LVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLD-----RTPC 464
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRlapvtLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDaagpvAEGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 465 SPLSGSLAPlnMKGLVKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 544
Cdd:TIGR02868 322 APAAGAVGL--GKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 545 LLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQ 624
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGE 476
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQL 680
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
362-720 |
1.89e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 159.61 E-value: 1.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 362 GEAQKFRQKLE--EMKPLNKKEALAYVTEVWT---MSVSGMLLkVGILYLGGQLVvRGAVSSGNLVS-FVLYQLQftrAV 435
Cdd:PRK11160 217 GAEDRYRQQLEqtEQQWLAAQRRQANLTGLSQalmILANGLTV-VLMLWLAAGGV-GGNAQPGALIAlFVFAALA---AF 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 436 EVLLSIYPSMQ---KSVGASEKIFEYLDRTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTA 512
Cdd:PRK11160 292 EALMPVAGAFQhlgQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 513 LVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTrTPTMEEITAV 592
Cdd:PRK11160 371 LLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEV 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 593 AMESGAHDFISGfPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPewASRT 672
Cdd:PRK11160 450 LQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKT 526
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 158262052 673 VLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEAL 720
Cdd:PRK11160 527 VLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
479-701 |
3.87e-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: 149.96 E-value: 3.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH---YL 554
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTQVAAVGQEPLL-------FGRSFRE--NIAYGLTRTPTMEEITAVAMESG--AHDFISGFPqgydtevgetgNQLSGG 623
Cdd:cd03257 81 RKEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVglPEEVLNRYP-----------HELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
480-696 |
1.29e-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: 147.62 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYP--NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLyQPTGGKVlldgellvqydhhYLHT 556
Cdd:cd03250 1 ISVEDASFTWDsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLLFGRSFRENIAYGLTRTPTMEE--ITAVAMESgahDfISGFPQGYDTEVGETGNQLSGGQRQAVALARAL 634
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGKPFDEERYEkvIKACALEP---D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 635 IRKPRLLILDDATSALDAgnqlRVQRLLYES---PEWA-SRTVLLITQQLSLAERAHHILFLKEGS 696
Cdd:cd03250 143 YSDADIYLLDDPLSAVDA----HVGRHIFENcilGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
481-695 |
4.80e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.11 E-value: 4.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAA 560
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 VGQEPLLFGRSFRENIAYGLT---RTPTMEEITAvAMESgahdFisGFPQGY-DTEVGEtgnqLSGGQRQAVALARALIR 636
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQlreRKFDRERALE-LLER----L--GLPPDIlDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 695
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
475-718 |
1.54e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 157.50 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY------------QPTG------ 536
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 537 ------------------------------------GKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGl 580
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG- 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 581 TRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQR 660
Cdd:PTZ00265 1320 KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 661 LLYESPEWASRTVLLITQQLSLAERAHHILFL----KEGS-VCEQGTHLQLME-RGGCYRSMVE 718
Cdd:PTZ00265 1400 TIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
179-455 |
9.42e-39 |
|
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: 145.35 E-value: 9.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKT-APSFARNMW-----LMCILTVASTA-------LEFAGDGIYNitmghmhsRVHGEVFRAV 245
Cdd:cd18573 13 MSVPFAIGKLIDVASKESGdIEIFGLSLKtfalaLLGVFVVGAAAnfgrvylLRIAGERIVA--------RLRKRLFKSI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 246 LHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 325
Cdd:cd18573 85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 326 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILY 405
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 158262052 406 LGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
480-709 |
1.20e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 143.28 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQyDHHYLHTQVA 559
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGR-SFRENI-----AYGLTRTPTMEEI----TAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 629
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIdellELFGLTDAADRKVG---------------TLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
.
gi 158262052 709 R 709
Cdd:COG1131 221 R 221
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
476-709 |
1.43e-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: 150.44 E-value: 1.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG---GKVLLDGELLVQYDHH 552
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLHTQVAAVGQEPL--LFGRSFRENIAYGL-TRTPTMEEITAVAMES----GAHDFISGFPQgydtevgetgnQLSGGQR 625
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALeNLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGTHL 704
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPE 228
|
....*
gi 158262052 705 QLMER 709
Cdd:COG1123 229 EILAA 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
479-702 |
1.92e-38 |
|
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: 143.02 E-value: 1.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQ 557
Cdd:COG1124 1 MLEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPLL-------FGRSFREniAYGLTRTPTMEEITAVAMES-G-AHDFISGFPqgydtevgetgNQLSGGQRQAV 628
Cdd:COG1124 81 VQMVFQDPYAslhprhtVDRILAE--PLRIHGLPDREERIAELLEQvGlPPSFLDRYP-----------HQLSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
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 ... |
480-685 |
9.24e-38 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 140.30 E-value: 9.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPN-HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQydhhyLHTQV 558
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEPLLFG-RSFRENIAYGLT-RTPTMEEITAVAMES----GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 632
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElQGVPKAEARERAEELlelvGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS----LAER 685
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeavfLADR 201
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
450-702 |
1.61e-37 |
|
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: 147.36 E-value: 1.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 450 GASEKIFEYLDRTPCSPLSGSLAPLNMKG------LVKFQDVSFAYPNHPN--VQVLQGLTFTLYPGKVTALVGPNGSGK 521
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAaaaaepLLEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 522 STVAALLQNLYQPTGGKVLLDGELLVQYDH---HYLHTQVAAVGQEPL--LFGR-SFRENIAYGLT--RTPTMEEITAVA 593
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNPRmTVGDIIAEPLRlhGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 594 MES----G-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEW 668
Cdd:COG1123 385 AELlervGlPPDLADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRE 453
|
250 260 270
....*....|....*....|....*....|....*
gi 158262052 669 ASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1123 454 LGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
240-692 |
1.86e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 150.95 E-value: 1.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 240 EVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDK-----------LNLFLWYLGRGlCLLAFMIWGSFYLTVVT 308
Cdd:PTZ00265 135 EFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKfitiftyasafLGLYIWSLFKN-ARLTLCITCVFPLIYIC 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 309 LLSLPLLFLLPRRLGKVYQSLAVKVQEslakstqvalEALSAMPTVRSFANEEGEAQKFrqKLEEmKPLNKKEALAYVTE 388
Cdd:PTZ00265 214 GVICNKKVKINKKTSLLYNNNTMSIIE----------EALVGIRTVVSYCGEKTILKKF--NLSE-KLYSKYILKANFME 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 389 VWTMS-VSGMLL---KVGILYlGGQLVVRGAVSS--------GNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIF 456
Cdd:PTZ00265 281 SLHIGmINGFILasyAFGFWY-GTRIIISDLSNQqpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 457 EYLDRTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG 536
Cdd:PTZ00265 360 EIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 537 GKVLL-DGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTME---------------------------- 587
Cdd:PTZ00265 440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakca 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 588 ----------------------------EITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:PTZ00265 520 gdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFL 692
Cdd:PTZ00265 600 ILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
483-701 |
2.06e-37 |
|
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: 137.95 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVG 562
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 563 QepllfgrsfreniaygltrtptmeeitavAMES-GAHDFIsgfPQGYDTevgetgnqLSGGQRQAVALARALIRKPRLL 641
Cdd:cd03214 80 Q-----------------------------ALELlGLAHLA---DRPFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 642 ILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
232-719 |
4.46e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 149.74 E-value: 4.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 232 HMHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLF---LWYLgrglcLLAFMIWGSfyLTVVT 308
Cdd:PLN03232 980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqLWQL-----LSTFALIGT--VSTIS 1052
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 309 LLSLPLLFLLPRRLGKVYQSLAVKVQ--ESLAKSTQVAL--EALSAMPTVRSFaneegeaqkfrQKLEEMKPLNKKEALA 384
Cdd:PLN03232 1053 LWAIMPLLILFYAAYLYYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY-----------KAYDRMAKINGKSMDN 1121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 385 YVTEVWTMSVSGMLLKVGILYLGGQLV-------VRGAVSSGNLVSF-------VLYQLQFTRAVEVLLSIYPSMQKSVG 450
Cdd:PLN03232 1122 NIRFTLANTSSNRWLTIRLETLGGVMIwltatfaVLRNGNAENQAGFastmgllLSYTLNITTLLSGVLRQASKAENSLN 1201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 451 ASEKIFEYLD------------RTPCS-PLSGSlaplnmkglVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGP 516
Cdd:PLN03232 1202 SVERVGNYIDlpseataiiennRPVSGwPSRGS---------IKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGR 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 517 NGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIaygltrTPTMEEITAVAMES 596
Cdd:PLN03232 1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDADLWEA 1344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 597 --GAH--DFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRT 672
Cdd:PLN03232 1345 leRAHikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCT 1422
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 158262052 673 VLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMER-GGCYRSMVEA 719
Cdd:PLN03232 1423 MLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRdTSAFFRMVHS 1470
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
483-697 |
5.14e-37 |
|
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: 136.58 E-value: 5.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVG 562
Cdd:cd03246 4 ENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 563 QEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLI 642
Cdd:cd03246 83 QDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 643 LDDATSALDAGNQLRVQRLLyESPEWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
479-711 |
5.48e-37 |
|
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: 138.84 E-value: 5.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLhTQV 558
Cdd:COG4555 1 MIEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRK 637
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYespEWAS--RTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERGG 711
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 ... |
481-695 |
6.41e-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: 137.60 E-value: 6.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAA 560
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 VGQEP--LLFGRSFRENIAYGL----TRTPTMEEITAVAMEsgahdfisgfpqgydtEVGETG------NQLSGGQRQAV 628
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLenlgLPEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEG 695
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
480-695 |
1.29e-36 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 136.85 E-value: 1.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYP-NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDH----HYL 554
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTQVAAVGQEP-LLFGRSFRENIAYGL----TRTPTMEE-----ITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQ 624
Cdd:cd03255 81 RRHIGFVFQSFnLLPDLTALENVELPLllagVPKKERREraeelLERVGLGDRLNHYPS---------------ELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
476-677 |
4.12e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 4.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQydhhyL 554
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTQVAAVGQEPLLFG-RSFRENIAYGL-TRTPTMEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAV 628
Cdd:COG1116 79 GPDRGVVFQEPALLPwLTVLDNVALGLeLRGVPKAERRERARELlelvGLAGFEDAYP-----------HQLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASR--TVLLIT 677
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLR--LWQETgkTVLFVT 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
481-695 |
5.19e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 133.14 E-value: 5.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAA 560
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 VGQepllfgrsfreniaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRL 640
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 641 LILDDATSALDAGNQLRVQRLLYESPEWAsRTVLLITQQLSLAERA-HHILFLKEG 695
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
480-701 |
9.38e-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: 134.62 E-value: 9.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY-----QPTGGKVLLDGELL--VQYDHH 552
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLHTQVAAVGQEPLLFGRSFRENIAYGLT-----RTPTMEEITAVAMESGahdfisgfpqGYDTEVGE--TGNQLSGGQR 625
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKA----------ALWDEVKDrlHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
236-716 |
9.12e-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: 142.78 E-value: 9.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 315
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLY 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 316 FLLPRRLgkVYQSLAVKVQESLAKSTQVAL--EALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVtevwtms 393
Cdd:TIGR00957 1119 FFVQRFY--VASSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSI------- 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 394 VSGMLLKVGILYLGGQLVV---------RGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPC 464
Cdd:TIGR00957 1186 VANRWLAVRLECVGNCIVLfaalfavisRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 465 SP--LSGSLAPLNM--KGLVKFQDVSFAYpnHPNVQ-VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV 539
Cdd:TIGR00957 1266 APwqIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 540 LLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI----AYGltrtptmEEITAVAME-SGAHDFISGFPQGYDTEVG 614
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYS-------DEEVWWALElAHLKTFVSALPDKLDHECA 1416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 615 ETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyeSPEWASRTVLLITQQLSLAERAHHILFLKE 694
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDYTRVIVLDK 1494
|
490 500
....*....|....*....|..
gi 158262052 695 GSVCEQGTHLQLMERGGCYRSM 716
Cdd:TIGR00957 1495 GEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
482-701 |
1.54e-34 |
|
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: 129.74 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 482 FQDVSFAYPnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHyLHTQVAAV 561
Cdd:cd03247 3 INNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 562 GQEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetGNQLSGGQRQAVALARALIRKPRLL 641
Cdd:cd03247 81 NQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 642 ILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQG 701
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
178-455 |
6.03e-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: 131.52 E-value: 6.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNP 257
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 258 TGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESL 337
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 338 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKealAYVTEVWTMSVSGMLLKVG---ILYLGGQLVVRG 414
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR---AARLSALFSPLIGLLTALGtalVLLYGGYLVLQG 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 158262052 415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd07346 252 SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
179-455 |
6.16e-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: 131.60 E-value: 6.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKTAPSFARN-------MWLMCILTVASTA-------LEFAGDGIYnitmghmhSRVHGEVFRA 244
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEALralnqavLILLGVVLIGSIAtflrswlFTLAGERVV--------ARLRKRLFSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 245 VLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGK 324
Cdd:cd18780 85 IIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 325 VYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGIL 404
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18780 245 WYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
476-695 |
2.01e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.24 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKST---VAALLQnlyQPTGGKVLLDGELLVQYDH 551
Cdd:COG1136 1 MSPLLELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLD---RPTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 552 hylhTQVAA--------VGQEPLLFGR-SFRENIAY-----GLTRTPTMEEITAVAMESGAHDFISGFPqgydtevgetg 617
Cdd:COG1136 78 ----RELARlrrrhigfVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRP----------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 618 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
480-695 |
2.01e-32 |
|
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: 123.45 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHY--LHTQ 557
Cdd:cd03229 1 LELKNVSKRYGQK---TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPLLF-GRSFRENIAYGLtrtptmeeitavamesgahdfisgfpqgydtevgetgnqlSGGQRQAVALARALIR 636
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALGL----------------------------------------SGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 695
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
475-699 |
2.99e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 125.20 E-value: 2.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKST-VAALLqNLYQPTGGKVLLDGELLVQYDHHy 553
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 lhtqVAAVGQEpLLFGRSF----RENIAYGLT------RTPTMEEITAV--AMES-GAHDFIsgfpqgyDTEVGEtgnqL 620
Cdd:COG1121 77 ----IGYVPQR-AEVDWDFpitvRDVVLMGRYgrrglfRRPSRADREAVdeALERvGLEDLA-------DRPIGE----L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 621 SGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYespEWAS--RTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR---ELRRegKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
..
gi 158262052 698 CE 699
Cdd:COG1121 218 AH 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
480-697 |
4.67e-32 |
|
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: 122.51 E-value: 4.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHtQVA 559
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGR-SFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnQLSGGQRQAVALARALIRKP 638
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 639 RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
480-701 |
1.42e-31 |
|
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: 122.24 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylHTQVA 559
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLF-GRSFRENIAYGLT-RTPTMEEITAVAMESGAHDFISGFPQGYDTEvgetgnqLSGGQRQAVALARALIRK 637
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKlRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
480-702 |
2.86e-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: 123.31 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHY-LHTQV 558
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEP--LLFGRSFRENIAYGL----TRTPTMEEI-----TAVAMEsgahDFISGFPQgydtevgetgnQLSGGQRQA 627
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLenlgVPREEMRKRvdealKLVGME----DFRDREPH-----------LLSGGQKQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
475-702 |
3.38e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.18 E-value: 3.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYL 554
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTQVAAVGQEP--LLFGRSFRENIAYGL-----TRTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQA 627
Cdd:PRK13632 82 RKKIGIIFQNPdnQFIGATVEDDIAFGLenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
484-697 |
4.96e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.44 E-value: 4.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 484 DVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDhhyLHTQVAAVGQ 563
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 EP--LLFGRSFRENIAYGLTRTPTMEEITAVAMES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPRL 640
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 641 LILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
479-706 |
3.43e-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: 119.22 E-value: 3.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQ 557
Cdd:cd03258 1 MIELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVG----QEPLLFGRSFRENIAYGL--TRTPtMEEITAVAME----SGAHDFISGFPqgydtevgetgNQLSGGQRQA 627
Cdd:cd03258 81 RRRIGmifqHFNLLSSRTVFENVALPLeiAGVP-KAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQL 706
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
236-722 |
1.18e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 126.39 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFL---WYLGRGLCLLAFM----IWGSFYLTVVT 308
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqiFQLLSTFVLIGIVstisLWAIMPLLVLF 1066
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 309 LLSLPLlfllprrlgkvYQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFaneegeaqkfrQKLEEMKPLNKK--EA 382
Cdd:PLN03130 1067 YGAYLY-----------YQSTAreVKRLDSITRSPVYAQfgEALNGLSTIRAY-----------KAYDRMAEINGRsmDN 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 383 LAYVTEVwTMSvSGMLLKVGILYLGG-------QLVVRGAVSSGNLVSF-------VLYQLQFTRAVEVLLSIYPSMQKS 448
Cdd:PLN03130 1125 NIRFTLV-NMS-SNRWLAIRLETLGGlmiwltaSFAVMQNGRAENQAAFastmgllLSYALNITSLLTAVLRLASLAENS 1202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 449 VGASEKIFEYLD------------RTPCS-PLSGSlaplnmkglVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALV 514
Cdd:PLN03130 1203 LNAVERVGTYIDlpseaplviennRPPPGwPSSGS---------IKFEDVVLRYrPELP--PVLHGLSFEISPSEKVGIV 1271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 515 GPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIaygltrTPTMEEITAVAM 594
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLW 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 595 ES--GAH--DFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWAS 670
Cdd:PLN03130 1346 ESleRAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKS 1423
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 158262052 671 RTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL-MERGGCYRSMVEALAA 722
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQSTGA 1476
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
476-702 |
1.51e-29 |
|
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: 117.39 E-value: 1.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLH 555
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVG---QEPLLFGrSF--RENIAYGLTRTPTM--EEITAVAME-------SGAHDFisgFPqgydtevgetgNQLS 621
Cdd:COG1127 79 ELRRRIGmlfQGGALFD-SLtvFENVAFPLREHTDLseAEIRELVLEklelvglPGAADK---MP-----------SELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQ 700
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223
|
..
gi 158262052 701 GT 702
Cdd:COG1127 224 GT 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
475-710 |
1.70e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYL 554
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTQVAAVGQEP--LLFGRSFRENIAYGL-----TRTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQA 627
Cdd:PRK13635 80 RRQVGMVFQNPdnQFVGATVQDDVAFGLenigvPREEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 628 VALARALIRKPRLLILDDATSALD-AGNQ--LRVQRLLYESpewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHL 704
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDpRGRRevLETVRQLKEQ---KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
....*.
gi 158262052 705 QLMERG 710
Cdd:PRK13635 226 EIFKSG 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
479-702 |
3.66e-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: 116.25 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH--YLHT 556
Cdd:COG1126 1 MIEIENLHKSFGDL---EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLLFG-RSFRENIAYGLTRTPTM--EEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVA 629
Cdd:COG1126 78 KVGMVFQQFNLFPhLTVLENVTLAPIKVKKMskAEAEERAMELlervGLADKADAYP-----------AQLSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 630 LARALIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelVGEVLDVMRDLAKE----GMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
483-702 |
3.81e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.10 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQydhhYLHTQ---VA 559
Cdd:COG1118 6 RNISKRFGS---FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLPPRerrVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFgR--SFRENIAYGLT-RTPTMEEITAVAME----SGAHDFISGFPqgydtevgetgNQLSGGQRQAVALAR 632
Cdd:COG1118 79 FVFQHYALF-PhmTVAENIAFGLRvRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 633 ALIRKPRLLILDDATSALDAgnQLRVQ------RLLYESPewasRTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 702
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDA--KVRKElrrwlrRLHDELG----GTTVFVTHDQEEAlELADRVVVMNQGRIEQVGT 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
480-702 |
5.60e-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: 115.68 E-value: 5.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE---LLVQYDHHYLHT 556
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEdisGLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLLFGR-SFRENIAYGLTRTPTM--EEITAVAME-------SGAHDFisgFPqgydtevgetgNQLSGGQRQ 626
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREIVLEkleavglRGAEDL---YP-----------AELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
496-702 |
7.87e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 115.98 E-value: 7.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQE-PLLFGRSFRE 574
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHsSLAFPFTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 575 NIAYGLTRTPTM----EEITAVAME-SGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALI-------RKPRLLI 642
Cdd:COG4559 95 VVALGRAPHGSSaaqdRQIVREALAlVGLAHLAGRSYQ-----------TLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 643 LDDATSALDAGNQLRVQRLLYespEWASR--TVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLAR---QLARRggGVVAVLHDLNLAAQyADRILLLHQGRLVAQGT 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
476-702 |
8.52e-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: 118.28 E-value: 8.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvqydhhylh 555
Cdd:COG3842 2 AMPALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAA----VG---QEPLLFG-RSFRENIAYGLT-RTPTMEEITA--------VAMESGAHDFISgfpqgydtevgetgn 618
Cdd:COG3842 70 TGLPPekrnVGmvfQDYALFPhLTVAENVAFGLRmRGVPKAEIRArvaellelVGLEGLADRYPH--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRVQ------RLLYESPewasRTVLLIT--QQ--LSLAERahh 688
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDA--KLREEmreelrRLQRELG----ITFIYVThdQEeaLALADR--- 205
|
250
....*....|....
gi 158262052 689 ILFLKEGSVCEQGT 702
Cdd:COG3842 206 IAVMNDGRIEQVGT 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
179-455 |
1.39e-28 |
|
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: 116.04 E-value: 1.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 259 GSITSRVTEDTSNVCESISDKLNLFLwylgRGLCLL----AFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:cd18576 93 GELTSRLSNDVTQIQDTLTTTLAEFL----RQILTLiggvVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:cd18576 169 DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 158262052 415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18576 249 ELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
474-652 |
2.61e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.35 E-value: 2.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvqyDHHY 553
Cdd:COG1129 5 LEMRGISK----SF-----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE-----PVRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 LHTQ------VAAVGQEPLLF-GRSFRENIA-------YGLTRTPTMEEITAVAMES-GAHdfISgfPqgyDTEVGEtgn 618
Cdd:COG1129 71 RSPRdaqaagIAIIHQELNLVpNLSVAENIFlgreprrGGLIDWRAMRRRARELLARlGLD--ID--P---DTPVGD--- 140
|
170 180 190
....*....|....*....|....*....|....
gi 158262052 619 qLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:COG1129 141 -LSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
480-699 |
3.35e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 112.84 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLY---QPTGGKVLLDGELLVQYDHH---Y 553
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 LHTQVAAVGQE-PLLFGRSFRENIAY-----GLTRTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQA 627
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspewASR---TVLLITQQLSLAERAHH-ILFLKEGSVCE 699
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE----INRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
480-695 |
4.32e-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: 112.24 E-value: 4.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQ--YDHHYLHTQ 557
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPLLFG-RSFRENIAYGLTRTPTM--EEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVAL 630
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKGMskAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 631 ARALIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLA-ERAHHILFLKEG 695
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
479-689 |
6.16e-28 |
|
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: 111.80 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQPTGGKVLLDGELLVQYDHHYlH 555
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT---LLRilaGLLPPSAGEVLWNGEPIRDAREDY-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEPLLFGR-SFRENIA-----YGLTRTPT--MEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQA 627
Cdd:COG4133 75 RRLAYLGHADGLKPElTVRENLRfwaalYGLRADREaiDEALEAVGLAGLADLPVR---------------QLSAGQKRR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLyesPEWASR--TVLLITQQLSLAERAHHI 689
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELI---AAHLARggAVLLTTHQPLELAAARVL 200
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
481-698 |
1.25e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.09 E-value: 1.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHhylhtQVAA 560
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 VGQEpLLFGRSF----RENIAYGLTRTPTM-------------EEITAVAMESGAHDFISgfpqgydtevgetgnQLSGG 623
Cdd:cd03235 73 VPQR-RSIDRDFpisvRDVVLMGLYGHKGLfrrlskadkakvdEALERVGLSELADRQIG---------------ELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyesPEWAS--RTVLLITQQLSLAER-AHHILFLKEGSVC 698
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL---RELRRegMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
480-709 |
6.45e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.05 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGELLVQYDHHYLHT 556
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEP--LLFGRSFRENIAYGLTRT----PTMEEITA-VAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 629
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRavprPEMIKIVRdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMER 709
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
478-702 |
6.45e-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: 108.65 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 478 GLVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHT 556
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLLFGRSFRENI-AYGLTrtpTMEEITAVamesgahdfisgfpqgydTEVGETGNQLSGGQRQAVALARALI 635
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEY---SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 636 RKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
480-707 |
7.30e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 110.10 E-value: 7.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:PRK11231 3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLL-FGRSFRENIAYGltRTPTM----------EEITAVAMEsgahdfisgfpqgyDTEVGETGNQ----LSGGQ 624
Cdd:PRK11231 80 LLPQHHLTpEGITVRELVAYG--RSPWLslwgrlsaedNARVNQAME--------------QTRINHLADRrltdLSGGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTH 703
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTP 222
|
....
gi 158262052 704 LQLM 707
Cdd:PRK11231 223 EEVM 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
480-707 |
3.55e-26 |
|
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: 107.77 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLF-GRSFRENIAYGLT---------RTPTMEEITAVAMESGahdfisGFPQGYDtevgetgNQLSGGQRQAVA 629
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKllkwpkekiRERADELLALVGLDPA------EFADRYP-------HELSGGQQQRVG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 707
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
496-702 |
5.47e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 107.55 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLL-FGRSFRE 574
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 575 NIAYGLT----RTPTMEEITAVAMESgahdfisgfpqgydTEVGETGN----QLSGGQRQAVALARALIR------KPRL 640
Cdd:PRK13548 96 VVAMGRAphglSRAEDDALVAAALAQ--------------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 641 LILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
480-702 |
5.66e-26 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 107.04 E-value: 5.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQydHHYLHTQVA 559
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFI-----SGFPQGYDtevgetgNQLSGGQRQAVALARA 633
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 702
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
179-455 |
6.69e-26 |
|
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: 108.33 E-value: 6.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFT---GRITD----WILQDKTAPSF----ARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLH 247
Cdd:cd18577 13 AALPLMTivfGDLFDaftdFGSGESSPDEFlddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 248 QETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFmiwgSFY----LTVVTLLSLPLLFLLPRRLG 323
Cdd:cd18577 93 QDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFII----AFIyswkLTLVLLATLPLIAIVGGIMG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 324 KVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGI 403
Cdd:cd18577 169 KLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALA 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 158262052 404 LYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18577 249 FWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
485-709 |
7.33e-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: 108.99 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 485 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGELLVQYDH----HYLHTQ 557
Cdd:COG0444 9 VYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrKIRGRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPL-----LF--GRSFRENIAY--GLTRtptmEEITAVAME-------SGAHDFISGFPqgydtevgetgNQLS 621
Cdd:COG0444 88 IQMIFQDPMtslnpVMtvGDQIAEPLRIhgGLSK----AEARERAIEllervglPDPERRLDRYP-----------HELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQ 700
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVvAEIADRVAVMYAGRIVEE 232
|
....*....
gi 158262052 701 GTHLQLMER 709
Cdd:COG0444 233 GPVEELFEN 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
481-697 |
1.07e-25 |
|
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: 106.50 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHT---Q 557
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPLLFGR-SFRENIAYG-LTRTPTM---------EEI-------TAVAMESGAHDFISgfpqgydtevgetgnQ 619
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGrLGRRSTWrslfglfpkEEKqralaalERVGLLDKAYQRAD---------------Q 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
476-706 |
1.45e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLH 555
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEP--LLFGRSFRENIAYGLT-----RTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAV 628
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 706
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
507-701 |
1.62e-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: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 507 PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH-YLHTQVAAVG---QEPLLFGR-SFRENIAYGLT 581
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGlvfQQYALFPHlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 582 RTPTMEEITAVAMESGAHDfISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRL 661
Cdd:cd03297 102 RKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 158262052 662 LYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
495-708 |
1.71e-25 |
|
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: 105.21 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvqyDHHYLHTQVAA----VGQEPLLFGR 570
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPPHERARAgigyVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 -SFRENI---AYGLTR---TPTMEEITAVamesgahdfisgFP---QGYDTEVGetgnQLSGGQRQAVALARALIRKPRL 640
Cdd:cd03224 90 lTVEENLllgAYARRRakrKARLERVYEL------------FPrlkERRKQLAG----TLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 641 LILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLITQQLSLA-ERAHHILFLKEGSVCEQGTHLQLME 708
Cdd:cd03224 154 LLLDEPSEGLapkiveeifEAIRELRDEGV----------TILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
502-708 |
3.61e-25 |
|
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: 105.42 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 502 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYL----HTQVAAVGQEPLLF-GRSFRENI 576
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGL-TRTPTMEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:cd03294 124 AFGLeVQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 652 AGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
479-702 |
6.55e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.83 E-value: 6.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYpNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQV 558
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEP--LLFGRSFRENIAYGLTR----TPTMEEITAVAMES-GAHDFISGFPQGydtevgetgnqLSGGQRQAVALA 631
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLENhavpYDEMHRRVSEALKQvDMLERADYEPNA-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 632 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
180-455 |
1.03e-24 |
|
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: 104.81 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 180 AIPFFTGRITDWILQDKTApsfaRNMWLMCILTVASTALEFAGDGIYNITMGHMHSRV----HGEVFRAVLHQETGFFLK 255
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKDL----EALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVvrdlRNDLFDKLLRLPLSFFDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 256 NPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQE 335
Cdd:cd18552 93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 336 SLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKPLNKKEALAYVTEVwtMSVSGMllkVGILYLGGQL 410
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERlrrlsMKIARARALSSPLMEL--LGAIAI---ALVLWYGGYQ 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 158262052 411 VVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18552 248 VISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
480-709 |
1.31e-24 |
|
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: 103.09 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylHTQVA 559
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGR-SFRENIAYGLTRTPT---------MEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 629
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKKLpkaeikervAEALDLVQLEGYANRKPS---------------QLSGGQQQRVA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 630 LARALIRKPRLLILDDATSALDAgnQLRvQRLLYESPEWASR---TVLLIT--QQ--LSLAERahhILFLKEGSVCEQGT 702
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDL--KLR-KDMQLELKRLQKElgiTFVFVThdQEeaLTMSDR---IAVMNKGKIQQIGT 214
|
....*..
gi 158262052 703 HLQLMER 709
Cdd:cd03300 215 PEEIYEE 221
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
480-706 |
1.57e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.20 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqydhHYLHTQVA 559
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--------YSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQE--------PLLFGRSFRENIAY-----GLTRTPTMEEITAVAMESGAHDFIsgfpqgyDTEVGetgnQLSGGQRQ 626
Cdd:cd03263 72 AARQSlgycpqfdALFDELTVREHLRFyarlkGLPKSEIKEEVELLLRVLGLTDKA-------NKRAR----TLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 627 AVALARALIRKPRLLILDDATSALDAgnqlRVQRLLYESPEWA--SRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTH 703
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDP----ASRRAIWDLILEVrkGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSP 216
|
...
gi 158262052 704 LQL 706
Cdd:cd03263 217 QEL 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
483-708 |
2.42e-24 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 102.94 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVG 562
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 563 QE-PLLFGRSFRENIAYG-------------LTRTPTMEEITAVAMESGAHDFIsgfpqgydtevgetgNQLSGGQRQAV 628
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGrypwhgalgrfgaADREKVEEAISLVGLKPLAHRLV---------------DSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 707
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 158262052 708 E 708
Cdd:PRK10575 237 R 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
474-697 |
2.76e-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: 99.81 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqydhhy 553
Cdd:cd03216 1 LELRGITK----RF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 lhtqvaavgqEPLLFgRSFRENIAYGltrtptmeeITAVamesgaHdfisgfpqgydtevgetgnQLSGGQRQAVALARA 633
Cdd:cd03216 62 ----------KEVSF-ASPRDARRAG---------IAMV------Y-------------------QLSVGERQMVEIARA 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 634 LIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:cd03216 97 LARNARLLILDEPTAALTpaeVERLFKVIRRLRAQ----GVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
481-702 |
4.08e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 101.37 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNHPnvqvlqgLTFTLY--PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvqyDHHYLHTQ- 557
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-----DLTALPPAe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 --VAAVGQEPLLFGR-SFRENIAYGLTrtPTM-------EEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQA 627
Cdd:COG3840 71 rpVSMLFQENNLFPHlTVAQNIGLGLR--PGLkltaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 628 VALARALIRKPRLLILDDATSALDAGnqLRvQRLLYESPEWASR---TVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPA--LR-QEMLDLVDELCRErglTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
495-695 |
6.31e-24 |
|
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: 100.97 E-value: 6.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAA-----VG----QEP 565
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED----ARARlrarhVGfvfqSFQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 566 LLFGRSFRENIAYGL-------TRTPTMEEITAVAMESGAHDFisgfPqgydtevgetgNQLSGGQRQAVALARALIRKP 638
Cdd:COG4181 101 LLPTLTALENVMLPLelagrrdARARARALLERVGLGHRLDHY----P-----------AQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 639 RLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
495-709 |
6.48e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 106.31 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQnLyQPTGGKVLLDGELLVQYDHHYL-----HTQVaaVGQEPllF 568
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPSEGEIRFDGQDLDGLSRRALrplrrRMQV--VFQDP--F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 569 G-----RSFRENIAYGLT------RTPTMEEITAVAMEsgahdfisgfpqgydtEVG---ETGN----QLSGGQRQAVAL 630
Cdd:COG4172 373 GslsprMTVGQIIAEGLRvhgpglSAAERRARVAEALE----------------EVGldpAARHryphEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 631 ARALIRKPRLLILDDATSALDAGNQLRVQRLL----------YespewasrtvLLITQQLSLAER-AHHILFLKEGSVCE 699
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLrdlqrehglaY----------LFISHDLAVVRAlAHRVMVMKDGKVVE 506
|
250
....*....|
gi 158262052 700 QGTHLQLMER 709
Cdd:COG4172 507 QGPTEQVFDA 516
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
459-719 |
1.15e-23 |
|
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: 100.75 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 459 LDRTPCSPLSGslaplnMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 538
Cdd:cd03288 5 ISGSSNSGLVG------LGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 539 VLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRT-PTMEEITAVAMesgAHDFISGFPQGYDTEVGETG 617
Cdd:cd03288 78 IVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTdDRLWEALEIAQ---LKNMVKSLPGGLDAVVTEGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 618 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
250 260
....*....|....*....|...
gi 158262052 698 CEQGTHLQLM-ERGGCYRSMVEA 719
Cdd:cd03288 233 VECDTPENLLaQEDGVFASLVRT 255
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
479-709 |
1.42e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.17 E-value: 1.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeLLV---QYDHHYLH 555
Cdd:PRK09493 1 MIEFKNVSKHFGPT---QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-LKVndpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEPLLFGR-SFRENIAYGLTRT----------PTMEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQ 624
Cdd:PRK09493 77 QEAGMVFQQFYLFPHlTALENVMFGPLRVrgaskeeaekQARELLAKVGLAERAHHYPS---------------ELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDA---GNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQ 700
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPelrHEVLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAED 217
|
....*....
gi 158262052 701 GTHLQLMER 709
Cdd:PRK09493 218 GDPQVLIKN 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
484-702 |
1.45e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 484 DVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvQYDHHYL---HTQVAA 560
Cdd:PRK13639 6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 VGQEP--LLFGRSFRENIAYG-LTRTPTMEEITAVAMESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALARALIRK 637
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFEN-------KPPHHLSGGQKKRVAIAGILAMK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGT 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
346-718 |
2.00e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 106.75 E-value: 2.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 346 EALSAMPTVRSFANEegeaQKFRQKL-----EEMKPLNKKEALAYVTEVWTMSVSGM--LLKVGIL-YLGGQLVVRGAVS 417
Cdd:PLN03130 484 EVLAAMDTVKCYAWE----NSFQSKVqtvrdDELSWFRKAQLLSAFNSFILNSIPVLvtVVSFGVFtLLGGDLTPARAFT 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 418 SGNLVS---FVLYQLQ--FTRAVEVLLSIyPSMQKSVGASEKIFeyldrTPCSPLSGSLAPLNMKglvkfqDVSFAYPNH 492
Cdd:PLN03130 560 SLSLFAvlrFPLFMLPnlITQAVNANVSL-KRLEELLLAEERVL-----LPNPPLEPGLPAISIK------NGYFSWDSK 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 493 PNVQVLQGLTFTLYPGKVTALVGPNGSGK-STVAALLQNLYQPTGGKVLLDGellvqydhhylhtQVAAVGQEPLLFGRS 571
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNAT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 572 FRENIAYGLTRTPTMEEiTAVAMESGAHDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PLN03130 695 VRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 652 AgnqlRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 718
Cdd:PLN03130 773 A----HVGRQVFDKcikDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
476-711 |
3.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 100.19 E-value: 3.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLH 555
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEP--LLFGRSFRENIAYGLTRT----PTMEEITAVAME-SGAHDFISGFPQgydtevgetgnQLSGGQRQAV 628
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKERVNEALElVGMQDFKEREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLME 708
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
...
gi 158262052 709 RGG 711
Cdd:PRK13650 230 RGN 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
495-701 |
5.43e-23 |
|
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: 97.74 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH-----------YLHTQVaavgQ 563
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpeerglYPKMKV----I 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 EPLLFGRSFReniayGLTRTPTMEEITavamesgahDFISGFpqgydtEVGETGN----QLSGGQRQAVALARALIRKPR 639
Cdd:cd03269 89 DQLVYLAQLK-----GLKKEEARRRID---------EWLERL------ELSEYANkrveELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
496-701 |
9.94e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.90 E-value: 9.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGELLVQYDHHY---------LHTQVAAVGQEPL 566
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLsqqkglirqLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 567 LF-GRSFRENIAYG--LTRTPTMEEITAVAMESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLIL 643
Cdd:PRK11264 96 LFpHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 644 DDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG 701
Cdd:PRK11264 169 DEPTSALDpelVGEVLNTIRQLAQE----KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
480-701 |
1.07e-22 |
|
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: 96.52 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVqyDHHYLHTQVA 559
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFG-RSFRENI-----AYGLTRTPTMEEITAVAMESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARA 633
Cdd:cd03268 76 ALIEAPGFYPnLTARENLrllarLLGIRKKRIDEVLDVVGLKDSAKKKVKGF---------------SLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSVCEQG 701
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
180-455 |
1.18e-22 |
|
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: 98.66 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 180 AIPFFTGRITDWILQDKtapSFARNMWLMCILTVASTALEfagdGIYNITMGHMHSRVhgeVFRA-------VLHQETGF 252
Cdd:cd18551 17 AQPLLVKNLIDALSAGG---SSGGLLALLVALFLLQAVLS----ALSSYLLGRTGERV---VLDLrrrlwrrLLRLPVSF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 253 FLKNPTGSITSRVTEDTSNVCESISDKL-NLFLwylgrGLCLL----AFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQ 327
Cdd:cd18551 87 FDRRRSGDLVSRVTNDTTLLRELITSGLpQLVT-----GVLTVvgavVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 328 SLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEAL--AYVTEVWTMSVSGMLLkvGILY 405
Cdd:cd18551 162 KASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKieALIGPLMGLAVQLALL--VVLG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 158262052 406 LGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18551 240 VGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
479-699 |
1.32e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.22 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPN------HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYD-- 550
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 551 -HHYLHTQVAAVGQEPL-------LFGRSFRENIAYGLTRTPTMEEITAVAMESG---AHDFISGFPQgydtevgetgnQ 619
Cdd:PRK10419 83 qRKAFRRDIQMVFQDSIsavnprkTVREIIREPLRHLLSLDKAERLARASEMLRAvdlDDSVLDKRPP-----------Q 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVC 698
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231
|
.
gi 158262052 699 E 699
Cdd:PRK10419 232 E 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
480-659 |
1.35e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.76 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvqydhHYLHTQ-- 557
Cdd:COG3839 4 LELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 -VAAVGQEPLLF-GRSFRENIAYGLT--RTPTmEEItavamesgahdfisgfpqgyDTEVGETG-------------NQL 620
Cdd:COG3839 76 nIAMVFQSYALYpHMTVYENIAFPLKlrKVPK-AEI--------------------DRRVREAAellgledlldrkpKQL 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 158262052 621 SGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRVQ 659
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDA--KLRVE 171
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
255-718 |
1.42e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 103.90 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KN-PTGSITSRVTEDtSNVCESISDKLNlFLWylGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 333
Cdd:PLN03232 393 KNfASGKVTNMITTD-ANALQQIAEQLH-GLW--SAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLT 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 334 QESLA---KSTQVALEALSAMPTVRSFANE---EGEAQKFRQklEEMKPLNKKEALAYVTE--VWTMSVSGMLLKVGI-L 404
Cdd:PLN03232 469 KEGLQwtdKRVGIINEILASMDTVKCYAWEksfESRIQGIRN--EELSWFRKAQLLSAFNSfiLNSIPVVVTLVSFGVfV 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 405 YLGGQLVVRGAVSSGNLVSFVLYQLQFtraVEVLLSIYPSMQKSVGASEKIFEYLDR--TPCSPLSGSLAPLNMKglvkf 482
Cdd:PLN03232 547 LLGGDLTPARAFTSLSLFAVLRSPLNM---LPNLLSQVVNANVSLQRIEELLLSEERilAQNPPLQPGAPAISIK----- 618
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 qDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGK-STVAALLQNLYQPTGGKVLLDGellvqydhhylhtQVAAV 561
Cdd:PLN03232 619 -NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYV 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 562 GQEPLLFGRSFRENIAYGLTRTPTM--EEITAVAMEsgaHDfISGFPqGYD-TEVGETGNQLSGGQRQAVALARALIRKP 638
Cdd:PLN03232 685 PQVSWIFNATVRENILFGSDFESERywRAIDVTALQ---HD-LDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 639 RLLILDDATSALDAgnqlRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 715
Cdd:PLN03232 760 DIYIFDDPLSALDA----HVAHQVFDScmkDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835
|
...
gi 158262052 716 MVE 718
Cdd:PLN03232 836 LME 838
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
480-701 |
1.45e-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: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAY---PNHPNVQVLQGltftlypgKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvqyDHHYLHT 556
Cdd:cd03298 1 VRLDKIRFSYgeqPMHFDLTFAQG--------EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAPP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 Q---VAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALAR 632
Cdd:cd03298 68 AdrpVSMLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
488-692 |
1.60e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 488 AYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYdhhyLHTQVAAVGQEPLl 567
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY----VPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 568 fgrSFRENIAYG------LTRTPTMEEITAV--AMES-GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALIRKP 638
Cdd:NF040873 73 ---TVRDLVAMGrwarrgLWRRLTRDDRAAVddALERvGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158262052 639 RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFL 692
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
477-659 |
1.62e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 100.02 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 477 KGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELL--VQYDHHYL 554
Cdd:PRK09452 12 SPLVELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTqvaaVGQEPLLFGR-SFRENIAYGL--TRTPTmEEITAVAMESGA----HDFISGFPQgydtevgetgnQLSGGQRQA 627
Cdd:PRK09452 89 NT----VFQSYALFPHmTVFENVAFGLrmQKTPA-AEITPRVMEALRmvqlEEFAQRKPH-----------QLSGGQQQR 152
|
170 180 190
....*....|....*....|....*....|..
gi 158262052 628 VALARALIRKPRLLILDDATSALDAgnQLRVQ 659
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDY--KLRKQ 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
480-702 |
2.17e-22 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.00 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYP-NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQV 558
Cdd:COG1135 2 IELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVG----QEPLLFGRSFRENIAY-----GLTRtptmEEITAVAME-------SGAHDFisgFPqgydtevgetgNQLSG 622
Cdd:COG1135 82 RKIGmifqHFNLLSSRTVAENVALpleiaGVPK----AEIRKRVAEllelvglSDKADA---YP-----------SQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspewASR----TVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD----INRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 158262052 698 CEQGT 702
Cdd:COG1135 220 VEQGP 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
480-697 |
2.87e-22 |
|
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: 95.55 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH---YLHT 556
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQE-PLLFGRSFRENIAYGL---------TRTPTMEEITAVAMESGAHDFisgfpqgydtevgetGNQLSGGQRQ 626
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALevtgvppreIRKRVPAALELVGLSHKHRAL---------------PAELSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyESPEWASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
484-701 |
2.90e-22 |
|
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: 95.34 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 484 DVSFAYPNHpnvQVLQGLTFTLYPGkVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQyDHHYLHTQVAAVGQ 563
Cdd:cd03264 5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 EPLLFGR-SFRENIAY-----GLTRTPTMEEITAVAMESGAHDFisgfpqgYDTEVGetgnQLSGGQRQAVALARALIRK 637
Cdd:cd03264 80 EFGVYPNfTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLS-LAERAHHILFLKEGSVCEQG 701
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
495-651 |
3.50e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 98.27 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYL-----HTQV------AA--- 560
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplrrRMQMvfqdpyASlnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 ---VGQ---EPLLfgrsfreniAYGLTRTPTMEEITAVAMES-G-AHDFISGFPqgydtevgetgNQLSGGQRQAVALAR 632
Cdd:COG4608 111 rmtVGDiiaEPLR---------IHGLASKAERRERVAELLELvGlRPEHADRYP-----------HEFSGGQRQRIGIAR 170
|
170
....*....|....*....
gi 158262052 633 ALIRKPRLLILDDATSALD 651
Cdd:COG4608 171 ALALNPKLIVCDEPVSALD 189
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
480-659 |
4.53e-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: 95.01 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylHTQVA 559
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKP 638
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELL------QIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180
....*....|....*....|.
gi 158262052 639 RLLILDDATSALDAgnQLRVQ 659
Cdd:cd03301 150 KVFLMDEPLSNLDA--KLRVQ 168
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
180-455 |
8.36e-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: 96.40 E-value: 8.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTVA---STALEFagdgiYNITMG--HMHSRVHGEVFRAVLHQETGFFL 254
Cdd:cd18575 14 ALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVlalASALRF-----YLVSWLgeRVVADLRKAVFAHLLRLSPSFFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCL----LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLA 330
Cdd:cd18575 89 TTRTGEVLSRLTTDTTLIQTVVGSSLSIAL----RNLLLliggLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 331 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVTEVWTMSVSGMLLK----VGILYL 406
Cdd:cd18575 165 RASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA----AFAAALRRIRARALLTALVIFLVfgaiVFVLWL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 158262052 407 GGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18575 241 GAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
479-702 |
8.61e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 8.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQV 558
Cdd:PRK13652 3 LIETRDLCYSYSG--SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEP--LLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR 636
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGT 702
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRIVAYGT 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
495-702 |
9.67e-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: 94.81 E-value: 9.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAAVG-----QEPLLFG 569
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 R-SFRENIAYGLTRT-----------PTMEEITAVAMEsgAHDFIsGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRK 637
Cdd:cd03219 89 ElTVLENVMVAAQARtgsglllararREEREARERAEE--LLERV-GLADLADRPAGE----LSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
481-677 |
1.53e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.93 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNH-PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELL--------VQYDH 551
Cdd:COG4525 5 TVRHVSVRYPGGgQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrgVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 552 HylhtqvaavgqePLLFGRSFRENIAYGL--------TRTPTMEEITA-VAMESGAHDFISgfpqgydtevgetgnQLSG 622
Cdd:COG4525 85 D------------ALLPWLNVLDNVAFGLrlrgvpkaERRARAEELLAlVGLADFARRRIW---------------QLSG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT 677
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLIT 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
497-702 |
1.71e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQ-----------------YDHHYLHTQVA 559
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaelrnqklgfiYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQ--EPLLFGRSFRENIaygltRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVALARALIRK 637
Cdd:PRK11629 104 ALENvaMPLLIGKKKPAEI-----NSRALEMLAAVGLEHRANHRPS---------------ELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
497-663 |
2.19e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 2.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI 576
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGLT---RTPTMEEITAVAMEsgahdFisGFPqgyDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK10247 102 IFPWQirnQQPDPAIFLDDLER-----F--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170
....*....|
gi 158262052 654 NQLRVQRLLY 663
Cdd:PRK10247 172 NKHNVNEIIH 181
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
495-702 |
3.30e-21 |
|
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: 93.56 E-value: 3.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAAVG-----QEPLLFG 569
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 R-SFRENIA------------YGLTRTP----TMEEITAVAMES----GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAV 628
Cdd:COG0411 93 ElTVLENVLvaaharlgrgllAALLRLPrarrEEREARERAEELlervGLADRA-------DEPAGN----LSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
473-701 |
3.56e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 473 PLNMKGLvkfqDVSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH 552
Cdd:PRK09536 3 MIDVSDL----SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLHTQVAAVGQE-PLLFGRSFRENIAYG----LTRTPTMEEI--TAV--AMESGahdfisGFPQGYDTEVGEtgnqLSGG 623
Cdd:PRK09536 74 AASRRVASVPQDtSLSFEFDVRQVVEMGrtphRSRFDTWTETdrAAVerAMERT------GVAQFADRPVTS----LSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAGNQLR----VQRLLYEspewaSRTVLLITQQLSLAER-AHHILFLKEGSVC 698
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRtlelVRRLVDD-----GKTAVAAIHDLDLAARyCDELVLLADGRVR 218
|
...
gi 158262052 699 EQG 701
Cdd:PRK09536 219 AAG 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
470-701 |
4.88e-21 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.18 E-value: 4.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 470 SLAPLNMKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNL--------YQPTGGKVLL 541
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 542 DGE--LLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGL-----TRTPTMEEI-----TAVAMesgahdfisgfpqgY 609
Cdd:COG1117 76 DGEdiYDPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSELDEIveeslRKAAL--------------W 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 610 DtEV----GETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLIT---QQlsl 682
Cdd:COG1117 142 D-EVkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVThnmQQ--- 215
|
250 260
....*....|....*....|
gi 158262052 683 AER-AHHILFLKEGSVCEQG 701
Cdd:COG1117 216 AARvSDYTAFFYLGELVEFG 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
474-702 |
4.98e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 94.65 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKFQDVS---FAYPNHpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYD 550
Cdd:PRK11308 6 LQAIDLKKHYPVKrglFKPERL--VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 551 HHY---LHTQVAAVGQ-----------------EPLLfgrsfrenIAYGLTRTPTMEEITAVAMESGAHdfisgfPQGYD 610
Cdd:PRK11308 84 PEAqklLRQKIQIVFQnpygslnprkkvgqileEPLL--------INTSLSAAERREKALAMMAKVGLR------PEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 611 tevgETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHI 689
Cdd:PRK11308 150 ----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEV 225
|
250
....*....|...
gi 158262052 690 LFLKEGSVCEQGT 702
Cdd:PRK11308 226 MVMYLGRCVEKGT 238
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
503-709 |
6.47e-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: 95.17 E-value: 6.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 503 FTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDH-HYLHT---QVAAVGQEPLLFG-RSFRENIA 577
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgIFLPPhrrRIGYVFQEARLFPhLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 578 YGLTRTPT------MEEITAVAmesGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:COG4148 100 YGRKRAPRaerrisFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 652 AGnqlRVQRLL-Y-ES-PEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMER 709
Cdd:COG4148 166 LA---RKAEILpYlERlRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
498-725 |
6.76e-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: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 498 LQGLTFTLYPGKVTALVGPNGSGKST-VAALLQNLyQPTGGKVLLDGellvqydhhylhtQVAAVGQEPLLFGRSFRENI 576
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEM-DKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGltrTPTMEEITAVAMESGA--HDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAgn 654
Cdd:TIGR00957 720 LFG---KALNEKYYQQVLEACAllPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-- 793
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 655 qlRVQRLLYES---PE--WASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEALAAPSD 725
Cdd:TIGR00957 794 --HVGKHIFEHvigPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
494-702 |
1.38e-20 |
|
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: 91.20 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAAVG-----QEPLLF 568
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH----RIARLGigyvpEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 569 GR-SFRENI---AYGLTRTP----TMEEITAVamesgahdfisgFPqgydtEVGE----TGNQLSGGQRQAVALARALIR 636
Cdd:COG0410 91 PSlTVEENLllgAYARRDRAevraDLERVYEL------------FP-----RLKErrrqRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 637 KPRLLILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 702
Cdd:COG0410 154 RPKLLLLDEPSLGLapliveeifEIIRRLNREGV----------TILLVEQNARFAlEIADRAYVLERGRIVLEGT 219
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
179-427 |
1.39e-20 |
|
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: 92.86 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDK-TAPSFARNMWLMCILTVASTALEFagdgIYNITMGHMHSRV----HGEVFRAVLHQETGFF 253
Cdd:cd18541 16 LLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRF----LWRYLIFGASRRIeydlRNDLFAHLLTLSPSFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 254 LKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 333
Cdd:cd18541 92 QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 334 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVTeVW-----TMSVSGMLLKVGILYLGG 408
Cdd:cd18541 172 QEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEE----YVEKNLRLAR-VDalffpLIGLLIGLSFLIVLWYGG 246
|
250
....*....|....*....
gi 158262052 409 QLVVRGAVSSGNLVSFVLY 427
Cdd:cd18541 247 RLVIRGTITLGDLVAFNSY 265
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
497-702 |
1.42e-20 |
|
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: 91.24 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQY--DHHylhtQVAAVGQEPLLFGR-SFR 573
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKR----DISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 574 ENIAYGL-TRTPTMEEITAVAMEsgahdfISGFpQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:cd03299 90 KNIAYGLkKRKVDKKEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158262052 653 GNQLRVQRLLYESPEWASRTVLLITQQL----SLAERahhILFLKEGSVCEQGT 702
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFeeawALADK---VAIMLNGKLIQVGK 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
490-701 |
1.46e-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: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 490 PNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqYDhhyLHTQVAAVGQEPLLFG 569
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FD---VVKEPAEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 RSF--------RENIAY-----GLTRTPTMEEITAVAMESGAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALIR 636
Cdd:cd03266 85 DSTglydrltaRENLEYfaglyGLKGDELTARLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 637 KPRLLILDDATSALD--AGNQLR-VQRLLYEspewASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03266 154 DPPVLLLDEPTTGLDvmATRALReFIRQLRA----LGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
496-697 |
2.04e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 91.28 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQY-DHHYLHTQVAAvgqepLLFGRSFRE 574
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEArEDTRLMFQDAR-----LLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 575 NIAYGLT---RTPTMEEITAVAMESGAHDFISGfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK11247 101 NVGLGLKgqwRDAALQALAAVGLADRANEWPAA---------------LSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 158262052 652 AGNQLRVQRLLyESpEWASR--TVLLITQQLS----LAERahhILFLKEGSV 697
Cdd:PRK11247 166 ALTRIEMQDLI-ES-LWQQHgfTVLLVTHDVSeavaMADR---VLLIEEGKI 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
479-695 |
4.33e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.55 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH---YLH 555
Cdd:PRK10908 1 MIRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQE-PLLFGRSFRENIAYGLTRTPTMEE-----ITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 629
Cdd:PRK10908 79 RQIGMIFQDhHLLMDRTVYDNVAIPLIIAGASGDdirrrVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQLSL-AERAHHILFLKEG 695
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLiSRRSYRMLTLSDG 213
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
476-701 |
4.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.95 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLH 555
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEP--LLFGRSFRENIAYG-----LTRTP----TMEEITAVAMESGAHdfisgfpqgydtevgETGNQLSGGQ 624
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEverrVEEALKAVRMWDFRD---------------KPPYHLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG 701
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAaEWADQVIVLKEGRVLAEG 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
482-677 |
5.72e-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: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 482 FQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqydhhylHTQVAAV 561
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 562 GQEPLLF-GRSFRENIAYGLTR------------------TPTMEEITAV----------AMESGAHDFIS--GFPQG-Y 609
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAElraleaeleeleaklaepDEDLERLAELqeefealggwEAEARAEEILSglGFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 610 DTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEW-----ASR--TVLLIT 677
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-----------ESIEWleeflKNYpgTVLVVS 206
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
462-720 |
7.08e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 7.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 462 TPCSPLSGslAPLNMK-GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL 540
Cdd:PTZ00243 1292 EPASPTSA--APHPVQaGSLVFEGVQMRYREGLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 541 LDGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPtmEEITAVAMESGAHDFISGFPQGYDTEVGETGNQL 620
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 621 SGGQRQAVALARALIRKPRLLIL-DDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCE 699
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSA--FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
250 260
....*....|....*....|..
gi 158262052 700 QGTHLQL-MERGGCYRSMVEAL 720
Cdd:PTZ00243 1525 MGSPRELvMNRQSIFHSMVEAL 1546
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
475-650 |
7.89e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqydHHYL 554
Cdd:PRK15439 7 TAPPLLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG-------NPCA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 H-TQVAA-------VGQEPLLF-GRSFRENIAYGLTRTP-TMEEITAVAMESGAHdfisgfpqgYDTEVgeTGNQLSGGQ 624
Cdd:PRK15439 77 RlTPAKAhqlgiylVPQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ---------LDLDS--SAGSLEVAD 145
|
170 180
....*....|....*....|....*.
gi 158262052 625 RQAVALARALIRKPRLLILDDATSAL 650
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASL 171
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
179-455 |
8.93e-20 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 90.18 E-value: 8.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKtapsFARNMWLMCILTVASTALEFAGDGIYNITMG----HMHSRVHGEVFRAVLHQETGFFL 254
Cdd:cd18542 16 LLIPLLIRRIIDSVIGGG----LRELLWLLALLILGVALLRGVFRYLQGYLAEkasqKVAYDLRNDLYDHLQRLSFSFHD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCLLAF----MIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLA 330
Cdd:cd18542 92 KARTGDLMSRCTSDVDTIRRFLAFGLVELV----RAVLLFIGaliiMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 331 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeaLAYVTEVW--TMSVSGMLLKVGILYLGG 408
Cdd:cd18542 168 EEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIK--LAKLLAKYwpLMDFLSGLQIVLVLWVGG 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 158262052 409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18542 246 YLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-701 |
9.87e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.20 E-value: 9.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ-----PTGGKVLLDGELLVQYDHHYLHTQVAAVGQEP-LL 567
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 568 FGRSFRENIAYGL------TRTPTMEEITAVAMESGahdfisgfpQGYD---TEVGETGNQLSGGQRQAVALARALIRKP 638
Cdd:PRK14247 95 PNLSIFENVALGLklnrlvKSKKELQERVRWALEKA---------QLWDevkDRLDAPAGKLSGGQQQRLCIARALAFQP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 639 RLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
481-659 |
1.14e-19 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 87.92 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLYQP--TGGKVLLDGELLvqydhHYLHTQ 557
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRRL-----TALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVG---QEPLLFGR-SFRENIAYGLTRTPTMEEITAVAM----ESGAHDFISGFPqgydtevgetgNQLSGGQRQAVA 629
Cdd:COG4136 75 QRRIGilfQDDLLFPHlSVGENLAFALPPTIGRAQRRARVEqaleEAGLAGFADRDP-----------ATLSGGQRARVA 143
|
170 180 190
....*....|....*....|....*....|
gi 158262052 630 LARALIRKPRLLILDDATSALDAGnqLRVQ 659
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAA--LRAQ 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
496-701 |
1.21e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQNLyqPTGGKVLLDGELLVQYDHHYL---HTQVAAVGQEP--LLFG 569
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 R-SFRENIAYGLT-RTPTM-----EEITAVAMESGAHDFISgfPQGYDTEvgetgnqLSGGQRQAVALARALIRKPRLLI 642
Cdd:PRK15134 378 RlNVLQIIEEGLRvHQPTLsaaqrEQQVIAVMEEVGLDPET--RHRYPAE-------FSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 643 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAeRA--HHILFLKEGSVCEQG 701
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV-RAlcHQVIVLRQGEVVEQG 508
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
178-455 |
1.37e-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: 89.88 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 178 EMAIPFFTGRITDWILQDKTAP-SFARNMWLMCILTVASTALEFAGdGIYNITMGHMHSRVHG----EVFRAVLHQETGF 252
Cdd:cd18563 15 GLVPPYLTKILIDDVLIQLGPGgNTSLLLLLVLGLAGAYVLSALLG-ILRGRLLARLGERITAdlrrDLYEHLQRLSLSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 253 FLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVK 332
Cdd:cd18563 94 FDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 333 VQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKealayVTEVWTM--SVSGMLLKVG---ILYLG 407
Cdd:cd18563 174 QWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR-----AEKLWATffPLLTFLTSLGtliVWYFG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 158262052 408 GQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18563 249 GRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
467-712 |
1.94e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 89.48 E-value: 1.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 467 LSGSLAPLNMKGLVKfqdvsfAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELL 546
Cdd:PRK13537 1 GPMSVAPIDFRNVEK------RYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 547 VQYDHHyLHTQVAAVGQ----EP--------LLFGRSFRENIAYGLTRTPTMEEITavAMESGAhdfisgfpqgyDTEVG 614
Cdd:PRK13537 72 PSRARH-ARQRVGVVPQfdnlDPdftvrenlLVFGRYFGLSAAAARALVPPLLEFA--KLENKA-----------DAKVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 615 EtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRvqRLLYE---SPEWASRTVLLITQQLSLAER-AHHIL 690
Cdd:PRK13537 138 E----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP--QAR--HLMWErlrSLLARGKTILLTTHFMEEAERlCDRLC 209
|
250 260
....*....|....*....|...
gi 158262052 691 FLKEGSVCEQGTHLQLMERG-GC 712
Cdd:PRK13537 210 VIEEGRKIAEGAPHALIESEiGC 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
501-677 |
2.16e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 90.66 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylHTQVAAVGQEPLLFGR-SFRENIAYG 579
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 580 LT--RTPTMEEITAVA-MESGAH--DFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGN 654
Cdd:PRK11607 116 LKqdKLPKAEIASRVNeMLGLVHmqEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
|
170 180
....*....|....*....|...
gi 158262052 655 QLRVQRLLYESPEWASRTVLLIT 677
Cdd:PRK11607 185 RDRMQLEVVDILERVGVTCVMVT 207
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
480-685 |
2.41e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 88.56 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG-----GKVLLDGELLVQ--YDHH 552
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLHTQVAAVGQEPLLFGRSFRENIAYGLTRT---PTMEEITAVamESGAHDfiSGFPQGYDTEVGETGNQLSGGQRQAVA 629
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrPKLEIDDIV--ESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER 685
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
497-652 |
2.58e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.16 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLV-----QYDhhylhtqVAAVGQEPLLFGR- 570
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrsiqQRD-------ICMVFQSYALFPHm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 SFRENIAYGLTrtptM-----EEITAVAMESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK11432 94 SLGENVGYGLK----MlgvpkEERKQRVKEALELVDLAGFEDRYV-------DQISGGQQQRVALARALILKPKVLLFDE 162
|
....*..
gi 158262052 646 ATSALDA 652
Cdd:PRK11432 163 PLSNLDA 169
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
495-723 |
3.10e-19 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 88.31 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEP--------- 565
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 566 --LLFGRSFRENIAygLTRTPTMEEITAVAMESG-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLI 642
Cdd:PRK15112 106 isQILDFPLRLNTD--LEPEQREKQIIETLRQVGlLPDHASYYP-----------HMLAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 643 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGthlqlmerggcyrSMVEALA 721
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERG-------------STADVLA 239
|
..
gi 158262052 722 AP 723
Cdd:PRK15112 240 SP 241
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
501-710 |
3.33e-19 |
|
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: 89.79 E-value: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH-YLHTQVAAVG---QEPLLFGR-SFREN 575
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGyvfQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 576 IAYGLTRT------PTMEEITAVAmesgahdfisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 649
Cdd:TIGR02142 96 LRYGMKRArpserrISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 650 LDagNQLRVQRLLY-ESPEWASRT-VLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERG 710
Cdd:TIGR02142 162 LD--DPRKYEILPYlERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-702 |
3.67e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.63 E-value: 3.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 477 KGLVKfqdvSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvQYDHhylht 556
Cdd:COG4152 5 KGLTK----RFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPED----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 qVAAVG---QEPLLFGR-SFRENIAY-----GLTRtptmeeitAVAMESgAHDFISGFpqgydtEVGETGN----QLSGG 623
Cdd:COG4152 70 -RRRIGylpEERGLYPKmKVGEQLVYlarlkGLSK--------AEAKRR-ADEWLERL------GLGDRANkkveELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
479-701 |
3.89e-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: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQnlyqptggkvLLDGellvqyDHHylhtqv 558
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKST---LLS----------LITG------DLP------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEPLLFGRSF--------RENIAY-------GLTRTPTMEEITAvameSGAHDFIsGFPQGYDTE----------- 612
Cdd:COG1119 55 PTYGNDVRLFGERRggedvwelRKRIGLvspalqlRFPRDETVLDVVL----SGFFDSI-GLYREPTDEqrerarellel 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 613 ------VGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAER 685
Cdd:COG1119 130 lglahlADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPG 209
|
250
....*....|....*.
gi 158262052 686 AHHILFLKEGSVCEQG 701
Cdd:COG1119 210 ITHVLLLKDGRVVAAG 225
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
493-696 |
4.72e-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: 86.62 E-value: 4.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQ----VAAVGQEPLLF 568
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 569 GRSFRENIAYGltrTP-TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:cd03290 92 NATVEENITFG---SPfNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 648 SALDA--GNQLrVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGS 696
Cdd:cd03290 169 SALDIhlSDHL-MQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
479-702 |
6.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.87 E-value: 6.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAY-PNHPNV-QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGELLV-----QYDH 551
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVsstskQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 552 HYLHTQVAAVGQEP--LLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFpqGYDTEVGETGN-QLSGGQRQAV 628
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFG----PQNFGIPKEKAEKIAAEKLEMV--GLADEFWEKSPfELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
465-712 |
8.86e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.35 E-value: 8.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 465 SPLSGSLAPLnmkgLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 544
Cdd:PRK13536 31 ASIPGSMSTV----AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 545 --------------LLVQYDHHYLHTQVaavgQEPLL-FGRSFRENIAYGLTRTPTMEEITavAMESGAhdfisgfpqgy 609
Cdd:PRK13536 104 pvpararlararigVVPQFDNLDLEFTV----RENLLvFGRYFGMSTREIEAVIPSLLEFA--RLESKA----------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 610 DTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDA-GNQLRVQRLlyESPEWASRTVLLITQQLSLAERAHH 688
Cdd:PRK13536 167 DARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPhARHLIWERL--RSLLARGKTILLTTHFMEEAERLCD 240
|
250 260
....*....|....*....|....*.
gi 158262052 689 ILFLKEG--SVCEQGTHLQLMERGGC 712
Cdd:PRK13536 241 RLCVLEAgrKIAEGRPHALIDEHIGC 266
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
494-702 |
1.65e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 87.83 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvqyDHHYLHT---QVAAVGQEPLLFGR 570
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHArdrKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 -SFRENIAYGLTRTPTMEEITAVAMESGAHDFI-----SGFPQGYDTevgetgnQLSGGQRQAVALARALIRKPRLLILD 644
Cdd:PRK10851 89 mTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 645 DATSALDAgnQLRVQ-----RLLYESPEWASrtVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK10851 162 EPFGALDA--QVRKElrrwlRQLHEELKFTS--VFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
497-702 |
1.83e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELL------VQYDHHYLHTQVAAVGQEPLLFGR 570
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdiFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 -SFRENIAYGLTRTPTME--EITAVAMESGAHdfISGFPQGYDtEVGETGNQLSGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEkrEIKKIVEECLRK--VGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 648 SALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
496-708 |
1.87e-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: 84.90 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAAVG-----QEPLLFGR 570
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH----KRARLGigylpQEASIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 -SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 649
Cdd:cd03218 90 lTVEENILAVLEIRGLSKKEREEKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 650 LDAGNQLRVQRLLYESPEWAsrTVLLIT-----QQLSLAERAhHILFlkEGSVCEQGTHLQLME 708
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRG--IGVLITdhnvrETLSITDRA-YIIY--EGKVLAEGTPEEIAA 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
474-651 |
2.01e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKfqdvSFaYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHH 552
Cdd:COG1101 2 LELKNLSK----TF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLHTQVAAVGQEPLLfGRSFR----EN--IAY------GLTRTPTMEEITAVamesgaHDFISGFPQGY----DTEVGet 616
Cdd:COG1101 77 KRAKYIGRVFQDPMM-GTAPSmtieENlaLAYrrgkrrGLRRGLTKKRRELF------RELLATLGLGLenrlDTKVG-- 147
|
170 180 190
....*....|....*....|....*....|....*
gi 158262052 617 gnQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
479-702 |
2.30e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDH-HYLHTQ 557
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEP--LLFGRSFRENIAYG-----LTRTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVAL 630
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 631 ARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
485-702 |
2.86e-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: 88.59 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 485 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKS-TVAALLQNLYQP---TGGKVLLDGELLVQYDHHYLHT---- 556
Cdd:COG4172 14 VAFGQGGGT-VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPL-----LF--GRSFRENIA--YGLTRTPTMEEITAVAMESG---AHDFISGFPqgydtevgetgNQLSGGQ 624
Cdd:COG4172 93 RIAMIFQEPMtslnpLHtiGKQIAEVLRlhRGLSGAAARARALELLERVGipdPERRLDAYP-----------HQLSGGQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
476-702 |
5.03e-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: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYP-------------------NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQ 533
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 534 PTGGKVLLDGEllvqydhhylhtqVAAvgqePLLFGRSF------RENI-----AYGLTRtptmEEITAVAmesgahDFI 602
Cdd:COG1134 78 PTSGRVEVNGR-------------VSA----LLELGAGFhpeltgRENIylngrLLGLSR----KEIDEKF------DEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 603 SGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQ 678
Cdd:COG1134 131 VEF-----AELGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSH 204
|
250 260
....*....|....*....|....*
gi 158262052 679 QLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1134 205 SMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
480-702 |
5.43e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 86.01 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNH-PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHT-- 556
Cdd:PRK11153 2 IELKNISKVFPQGgRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 -QVAAVGQE-PLLFGRSFRENIAYGLT--RTPTmEEITAVAME-------SGAHDFisgFPQgydtevgetgnQLSGGQR 625
Cdd:PRK11153 82 rQIGMIFQHfNLLSSRTVFDNVALPLElaGTPK-AEIKARVTEllelvglSDKADR---YPA-----------QLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
479-707 |
5.87e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 83.48 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPnvqvlqgLTFTLY--PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvqyDHHylHT 556
Cdd:PRK10771 1 MLKLTDITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHT--TT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 Q-----VAAVGQEPLLFGR-SFRENIAYGLTrtPTM-------EEITAVAMESGAHDFISGFPqgydtevgetgNQLSGG 623
Cdd:PRK10771 67 PpsrrpVSMLFQENNLFSHlTVAQNIGLGLN--PGLklnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK10771 134 QRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGP 213
|
....*
gi 158262052 703 HLQLM 707
Cdd:PRK10771 214 TDELL 218
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
497-701 |
6.95e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEPLLFGR-SFREN 575
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 576 IAYGltRTPTM----------EEITAVAMESGAHDFISGfpQGYDTevgetgnqLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK10253 102 VARG--RYPHQplftrwrkedEEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 646 ATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
496-701 |
7.08e-18 |
|
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: 82.21 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGellVQYDHHYLHTQVAAVGQEPLLFGR-SF 572
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 573 RENIAYgltrtptmeeitAVAMESgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:cd03213 100 RETLMF------------AAKLRG-----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 653 GNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEGSVCEQG 701
Cdd:cd03213 145 SSALQVMSLLRRLAD-TGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
500-704 |
8.81e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.50 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 500 GLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAAVG-----QEPLLFG----- 569
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIARMGvvrtfQHVRLFRemtvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 --------RSFRENIAYGLTRTPTMEEITAVAMESGAH--DFIsGFpqgydTEVG--ETGNqLSGGQRQAVALARALIRK 637
Cdd:PRK11300 99 enllvaqhQQLKTGLFSGLLKTPAFRRAESEALDRAATwlERV-GL-----LEHAnrQAGN-LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 638 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLA-ERAHHILflkegsVCEQGTHL 704
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIY------VVNQGTPL 233
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
204-463 |
1.21e-17 |
|
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: 84.43 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 204 NMWLMCILTVAstalefAGDGIYNITMGHMHSRVhGE---------VFRAVLHQETGFF--LKNPTGSITSRVTEDTSNV 272
Cdd:cd18578 52 NFWALMFLVLA------IVAGIAYFLQGYLFGIA-GErltrrlrklAFRAILRQDIAWFddPENSTGALTSRLSTDASDV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 273 CESISDKLNLFL-----------------WYLGrgLCLLAFM--IWGSFYLtvvtllslpllfllprrLGKVYQSLAVKV 333
Cdd:cd18578 125 RGLVGDRLGLILqaivtlvagliiafvygWKLA--LVGLATVplLLLAGYL-----------------RMRLLSGFEEKN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 334 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALayvtevWTMSVSG------MLLKVGILYLG 407
Cdd:cd18578 186 KKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL------ISGLGFGlsqsltFFAYALAFWYG 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 408 GQLVVRGAVSSGN-LVSFVLyqLQFT-RAVEVLLSIYPSMQKSVGASEKIFEYLDRTP 463
Cdd:cd18578 260 GRLVANGEYTFEQfFIVFMA--LIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
498-685 |
1.29e-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: 82.51 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvqydhhylhtQVAAVGQE--------PLLFG 569
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK------------QITEPGPDrmvvfqnySLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 RSFRENIAYGLTRT-PTM----------EEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVALARALIRKP 638
Cdd:TIGR01184 69 LTVRENIALAVDRVlPDLskserraiveEHIALVGLTEAADKRPG---------------QLSGGMKQRVAIARALSIRP 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 639 RLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT----QQLSLAER 685
Cdd:TIGR01184 134 KVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVThdvdEALLLSDR 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
476-685 |
1.52e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.90 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqNLYQPTGGKVLLDGEllVQYDHHYLH 555
Cdd:PRK14239 2 TEPILQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSI-NRMNDLNPEVTITGS--IVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 T----------QVAAVGQEPLLFGRSFRENIAYGLTRTPTME-EITAVAMES---GAHDFISGFPQGYDTEVGetgnqLS 621
Cdd:PRK14239 76 SprtdtvdlrkEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDkQVLDEAVEKslkGASIWDEVKDRLHDSALG-----LS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER 685
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASR 212
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
482-696 |
2.19e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.01 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 482 FQDVSFAypnHPNVQVL-QGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQPTGGKVLL--DGELLVqydhhylh 555
Cdd:COG4178 365 LEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKST---LLRaiaGLWPYGSGRIARpaGARVLF-------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 tqvaaVGQEPLLFGRSFRENIAY-GLTRTPTMEEITAVAMESGAHDFISGFpqgyDTEVgETGNQLSGGQRQAVALARAL 634
Cdd:COG4178 431 -----LPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERL----DEEA-DWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 635 IRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGS 696
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
485-677 |
2.33e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 2.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 485 VSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG--------ELLVQYDHhylht 556
Cdd:PRK11248 7 LYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvegpgaERGVVFQN----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 qvaavgqEPLLFGRSFRENIAYGLT-RTPTMEEITAVAMESGAHDFISGFPQGYDTevgetgnQLSGGQRQAVALARALI 635
Cdd:PRK11248 79 -------EGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158262052 636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT 677
Cdd:PRK11248 145 ANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
479-706 |
2.57e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPNV-QVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQNLYQP----TGGKVLLDGELLVQYDHH 552
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLH----TQVAAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEEITAVAMESG---AHDFISGFPqgydtevget 616
Cdd:PRK15134 85 TLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYP---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 617 gNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 695
Cdd:PRK15134 155 -HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|.
gi 158262052 696 SVCEQGTHLQL 706
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
178-455 |
2.69e-17 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 83.21 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 178 EMAIPFFTGRITDWILQDKTAPsfARNMWLMCILTVASTALEFAGDGIYNITMGH-----MHS-RVhgEVFRAVLHQETG 251
Cdd:cd18544 15 ELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKlgqriIYDlRR--DLFSHIQRLPLS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 252 FFLKNPTGSITSRVTEDTsnvcESISDKLNLFLWYLGRGLCLL----AFMIWGSFYLTVVTLLS----LPLLFLLPRRLG 323
Cdd:cd18544 91 FFDRTPVGRLVTRVTNDT----EALNELFTSGLVTLIGDLLLLigilIAMFLLNWRLALISLLVlpllLLATYLFRKKSR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 324 KVYQslavKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVG 402
Cdd:cd18544 167 KAYR----EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALAL 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 158262052 403 ILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18544 242 VLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
233-426 |
6.23e-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: 81.82 E-value: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 233 MHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDT----SNVCESISDKLNLFLWYLGRGLCLlaFMIwgSFYLTVVT 308
Cdd:cd18574 73 VAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRSVTQTVGCVVSL--YLI--SPKLTLLL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 309 LLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeaLAYVTE 388
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK--LGLGIG 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 158262052 389 VWTM----SVSGMLLkvGILYLGGQLVVRGAVSSGNLVSFVL 426
Cdd:cd18574 227 IFQGlsnlALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
494-707 |
9.04e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 9.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQV---LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTGGKVLLDGELLVQYDHH-------YLHTQVAAVGQ 563
Cdd:COG4138 5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 EPLLfgrsfrENIAYGLTRTPTMEEITAVaMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR------- 636
Cdd:COG4138 84 MPVF------QYLALHQPAGASSEAVEQL-LAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 707
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRhADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
508-702 |
9.43e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 508 GKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLH----TQVAAVGQE-PLLFGRSFRENIAYGLT- 581
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTVLDNTAFGMEl 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 582 --------RTPTMEEITAVAMESGAHdfisGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK10070 134 aginaeerREKALDALRQVGLENYAH----SYP-----------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 158262052 654 NQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGT 248
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
480-690 |
1.03e-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: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVlldgellvqydHHYLHTQVA 559
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGRSFRENIAYgltrtPTMEEitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPR 639
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYEspewASRTVLLITQQLSLAERAHHIL 690
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHRPSLWKFHDRVL 158
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
478-701 |
1.09e-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: 79.50 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 478 GLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqydhhylhtQ 557
Cdd:cd03220 18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAA-----VGQEPLLFGrsfRENI-----AYGLTRtptmEEITAVAmesgahDFISGFpqgydTEVGETGNQ----LSGG 623
Cdd:cd03220 85 VSSllglgGGFNPELTG---RENIylngrLLGLSR----KEIDEKI------DEIIEF-----SELGDFIDLpvktYSSG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
494-722 |
1.25e-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: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVLLDGE----------------LLVQY------ 549
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEdilelspderaragifLAFQYpveipg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 550 --DHHYLHTQVAAVGQEPLLFgRSFRENIAygltrtptmEEITAVAMesgAHDFIsgfpqgyDTEVGETgnqLSGGQRQA 627
Cdd:COG0396 92 vsVSNFLRTALNARRGEELSA-REFLKLLK---------EKMKELGL---DEDFL-------DRYVNEG---FSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 628 VALARALIRKPRLLILD--------DATSALDAG-NQLRvqrllyeSPEwasRTVLLITQQLSLAE--RAHHILFLKEGS 696
Cdd:COG0396 149 NEILQMLLLEPKLAILDetdsgldiDALRIVAEGvNKLR-------SPD---RGILIITHYQRILDyiKPDFVHVLVDGR 218
|
250 260
....*....|....*....|....*....
gi 158262052 697 VCEQGTH---LQLMERGgcYRSMVEALAA 722
Cdd:COG0396 219 IVKSGGKelaLELEEEG--YDWLKEEAAA 245
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
480-702 |
1.33e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 80.98 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHP--NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDgELLVQY---DHHYL 554
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHktkDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HT--QVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFIS--GFPQGYdteVGETGNQLSGGQRQAV 628
Cdd:PRK13646 82 PVrkRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMdlGFSRDV---MSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTS 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
486-685 |
1.33e-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: 79.68 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 486 SFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVGQEP 565
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 566 LLF-----GRSFRENIA-YGLTR---TPTMEEITAvAMESGAHdfisgfpqgYDTEVgetgNQLSGGQRQAVALARALIR 636
Cdd:cd03267 105 QLWwdlpvIDSFYLLAAiYDLPParfKKRLDELSE-LLDLEEL---------LDTPV----RQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL----SLAER 685
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMkdieALARR 223
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
480-707 |
1.41e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.13 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVA 559
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQEPLLFGR-SFRENIAYGltRTP------TMEEITAVA-------MESGAHDFIsgfpqgydtevgetgNQLSGGQR 625
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFG--RFPyskgrlTAEDREIIDeaiayldLEDLADRYL---------------DELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHL 704
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPE 221
|
...
gi 158262052 705 QLM 707
Cdd:COG4604 222 EII 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
495-664 |
1.89e-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: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLldgellvqYDHHYLHTQVAAVGQEPLLFGRsfRE 574
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDGGWVDLAQASPREILALR--RR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 575 NIAY------GLTRTPTMEeitaVAMESGAHdfisgfpQGYDTEV-----GETGNQL--------------SGGQRQAVA 629
Cdd:COG4778 94 TIGYvsqflrVIPRVSALD----VVAEPLLE-------RGVDREEararaRELLARLnlperlwdlppatfSGGEQQRVN 162
|
170 180 190
....*....|....*....|....*....|....*
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 664
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
494-662 |
1.99e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDH----HYLHTQVAAvgqEPLLfg 569
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLGHRNAM---KPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 rSFRENIA-----YGLTRTPTMEEITAVAMESGAHdfisgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPRLLILD 644
Cdd:PRK13539 89 -TVAENLEfwaafLGGEELDIAAALEAVGLAPLAH-----LPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
|
170
....*....|....*...
gi 158262052 645 DATSALDAGNQLRVQRLL 662
Cdd:PRK13539 153 EPTAALDAAAVALFAELI 170
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
484-711 |
2.01e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 80.05 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 484 DVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvQYDHH---YLHTQVAA 560
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 VGQEP--LLFGRSFRENIAYGLTRTPTME-EITAVAMESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALARALIRK 637
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEaEITRRVDEALTLVDAQHFRH-------QPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 638 PRLLILDDATSALDAGNQLR----VQRLLYEspewaSRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG------THLQL 706
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQmiaiIRRIVAQ-----GNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEA 229
|
....*
gi 158262052 707 MERGG 711
Cdd:PRK13638 230 MEQAG 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
478-697 |
2.99e-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: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 478 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLYqpTGGKVLLDGellVQYDHHYLHT 556
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDG---VSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVG---QEPLLFGRSFRENI-AYGLTRTptmEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALAR 632
Cdd:cd03289 75 WRKAFGvipQKVFIFSGTFRKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
496-701 |
3.17e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.24 E-value: 3.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL-----------DGELLVqYDHHYLH---TQVAAV 561
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkDGQLKV-ADKNQLRllrTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 562 GQEPLLFGR-SFRENI------AYGLTRTPTMEEITAVAMESGahdfISGFPQGydtevgETGNQLSGGQRQAVALARAL 634
Cdd:PRK10619 98 FQHFNLWSHmTVLENVmeapiqVLGLSKQEARERAVKYLAKVG----IDERAQG------KYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 635 IRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEE----GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
474-650 |
3.89e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 3.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYD-HH 552
Cdd:COG3845 6 LELRGITK----RF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLHTQVAAVGQEPLLFGR-SFRENIAYGLTRTPTM--------EEITAVAMEsgahdfiSGFPQGYDTEVGetgnQLSGG 623
Cdd:COG3845 77 AIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGrldrkaarARIRELSER-------YGLDVDPDAKVE----DLSVG 145
|
170 180
....*....|....*....|....*..
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSAL 650
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL 172
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
476-682 |
4.04e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLH 555
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAvgqePLLFGRSFRenIAYGLTRT---PTMEEITAvamesgAHdfISGFPQgydtevgetgNQLSGGQRQAVALAR 632
Cdd:PRK09544 78 LDTTL----PLTVNRFLR--LRPGTKKEdilPALKRVQA------GH--LIDAPM----------QKLSGGETQRVLLAR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 158262052 633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL 682
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
476-697 |
4.40e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 82.08 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPN-HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYL 554
Cdd:PRK10535 1 MTALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 htqvAAVGQEPllFGRSFREniaYGLTRTPTME---EITAV-------AMESGAHDFISGFpqGYDTEVGETGNQLSGGQ 624
Cdd:PRK10535 81 ----AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
479-702 |
5.51e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.12 E-value: 5.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGElLVQYDHH---YLH 555
Cdd:PRK13636 5 ILKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEP--LLFGRSFRENIAYGLT--RTPTMEEITAV--AMESGAHDFISGFPQgydtevgetgNQLSGGQRQAVA 629
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGAVnlKLPEDEVRKRVdnALKRTGIEHLKDKPT----------HCLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGT 702
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGN 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
476-702 |
6.11e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.59 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHPNVQ---VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG--------- 543
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 544 -------ELLVQYDHHYLhtqVAAVGQEPLLFGRsfrEN--IAYGLTRTPTMEEITAVAMesgaHDFISGFPqgydtevg 614
Cdd:PRK13633 81 wdirnkaGMVFQNPDNQI---VATIVEEDVAFGP---ENlgIPPEEIRERVDESLKKVGM----YEYRRHAP-------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 615 etgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKE 694
Cdd:PRK13633 143 ---HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDS 219
|
....*...
gi 158262052 695 GSVCEQGT 702
Cdd:PRK13633 220 GKVVMEGT 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
498-702 |
6.86e-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: 77.41 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQyDHHYLHTQVAAVGQEPLLFGR-SFRENI 576
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 A-----YGLTRTPTMEEITAVAmesgahDFIsgfpqgydtEVGETGNQL----SGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:cd03265 95 YiharlYGVPGAERRERIDELL------DFV---------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 648 SALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGT 215
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
180-455 |
7.56e-16 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 78.60 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 180 AIPFFTGRITDWILQDKTAPS------FARNMWLMCILTVASTALEFagdgIYNITMGHMHSRV----HGEVFRAVLHQE 249
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGGGgvdfsgLLRILLLLLGLYLLSALFSY----LQNRLMARVSQRTvydlRKDLFEKLQRLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 250 TGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCL----LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 325
Cdd:cd18547 93 LSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLI----SSILTivgtLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 326 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGIL 404
Cdd:cd18547 169 SQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY-VLVA 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18547 248 VVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
497-706 |
8.21e-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: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqydhhylhtQVAAVGQEPLLFGRSFRENI 576
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGLT----RTPTMeeITAVAMESGahdfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDa 652
Cdd:cd03291 119 IFGVSydeyRYKSV--VKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD- 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 653 gnqLRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 706
Cdd:cd03291 192 ---VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
480-661 |
9.01e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.50 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvqydhhylhTQV- 558
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV---------NELe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 ------AAVGQEPLLFGR-SFRENIAYGLT--RTPTmEEI------TAVAMESGAhdFISGFPQgydtevgetgnQLSGG 623
Cdd:PRK11650 73 padrdiAMVFQNYALYPHmSVRENMAYGLKirGMPK-AEIeervaeAARILELEP--LLDRKPR-----------ELSGG 138
|
170 180 190
....*....|....*....|....*....|....*....
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAgnQLRVQ-RL 661
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLDA--KLRVQmRL 175
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
480-677 |
9.51e-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: 9.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELlvqydhhylhtqva 559
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 avgqepllfgrsfreNIAYgltrtptmeeitavamesgahdfisgFPqgydtevgetgnQLSGGQRQAVALARALIRKPR 639
Cdd:cd03221 64 ---------------KIGY--------------------------FE------------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*...
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPewasRTVLLIT 677
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVS 124
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
497-684 |
9.53e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 76.38 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 575
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 576 IAY--GLTRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:cd03231 94 LRFwhADHSDEQVEEALARVGLNGFEDRPV--------------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|.
gi 158262052 654 NQLRVQRLLYESPEWASRTVLLITQQLSLAE 684
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-697 |
1.08e-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: 81.50 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLyqPTGGKVLLDGellVQYDHHYLHTQVAAVG---QEPLLFGRSF 572
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLlSALLRLL--STEGEIQIDG---VSWNSVTLQTWRKAFGvipQKVFIFSGTF 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 573 RENIaygltrTP----TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:TIGR01271 1309 RKNL------DPyeqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 158262052 649 ALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-706 |
1.67e-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: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellvqydhhylhtQVAAVGQEPLLFGRSFRENI 576
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGLTRTPTmeEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDagnqL 656
Cdd:TIGR01271 508 IFGLSYDEY--RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----V 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 158262052 657 RVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 706
Cdd:TIGR01271 582 VTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
485-703 |
1.79e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 485 VSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvQYDHHY---------LH 555
Cdd:PRK11124 8 INCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKtpsdkaireLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQE----PLLfgrSFRENI------AYGLTRTPTMEEitavAMESGAH----DFISGFPQgydtevgetgnQLS 621
Cdd:PRK11124 82 RNVGMVFQQynlwPHL---TVQQNLieapcrVLGLSKDQALAR----AEKLLERlrlkPYADRFPL-----------HLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQ 700
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
...
gi 158262052 701 GTH 703
Cdd:PRK11124 223 GDA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
479-651 |
3.16e-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: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQY---DHHYLH 555
Cdd:COG0488 315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYfdqHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TqvaavgqepllfGRSFRENIAYGLtrtPTMEEITAVAMesgAHDFisGFPqGYD--TEVGEtgnqLSGGQRQAVALARA 633
Cdd:COG0488 392 P------------DKTVLDELRDGA---PGGTEQEVRGY---LGRF--LFS-GDDafKPVGV----LSGGEKARLALAKL 446
|
170
....*....|....*...
gi 158262052 634 LIRKPRLLILDDATSALD 651
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLD 464
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
479-685 |
3.85e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.97 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPNVQvlqGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ--PTG---GKVLLDGELLvqYDHHY 553
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNL--YAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 ----LHTQVAAVGQEPLLFGRSFRENIAYG---LTRTPTMEEITAVAMESGAHdfisgfpqgYDtEVG----ETGNQLSG 622
Cdd:PRK14243 85 dpveVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAAL---------WD-EVKdklkQSGLSLSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER 685
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAAR 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
497-652 |
4.04e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 74.32 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 575
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 576 I----AYGLTRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:TIGR01189 94 LhfwaAIHGGAQRTIEDALAAVGLTGFEDLPA--------------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
.
gi 158262052 652 A 652
Cdd:TIGR01189 160 K 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
493-652 |
4.24e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEllvqyDHHY------LHTQVAAVGQE-- 564
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----EMRFasttaaLAAGVAIIYQElh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 565 --PLLfgrSFRENI-------AYGLTRTPTMEEITAVAMESGAHDFISGFPQGYdtevgetgnqLSGGQRQAVALARALI 635
Cdd:PRK11288 90 lvPEM---TVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----------LSIGQRQMVEIAKALA 156
|
170
....*....|....*..
gi 158262052 636 RKPRLLILDDATSALDA 652
Cdd:PRK11288 157 RNARVIAFDEPTSSLSA 173
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
480-702 |
4.67e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.21 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAY-PNHPNVQ-VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLV----QYDHHY 553
Cdd:PRK13634 3 ITFQKVEHRYqYKTPFERrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPT---MEEITAVAMESGAHDFIsgfpqGYDTEVGETGN-QLSGGQRQA 627
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFG----PMnfgVSEEDAKQKAREMIELV-----GLPEELLARSPfELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
494-701 |
1.04e-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: 73.33 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVLLDGELLVQYDHHylhtQVAAVG-----QEPl 566
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE----ERARLGiflafQYP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 567 lfgrsfreniaygltrtptmEEITAVAMEsgahDFISgfpqgydtEVGETgnqLSGGQRQAVALARALIRKPRLLILDDA 646
Cdd:cd03217 87 --------------------PEIPGVKNA----DFLR--------YVNEG---FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 647 TSALDAGNqLR-----VQRLLYEspewaSRTVLLITQQLSLAE--RAHHILFLKEGSVCEQG 701
Cdd:cd03217 132 DSGLDIDA-LRlvaevINKLREE-----GKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
480-702 |
1.69e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 74.40 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPNVQ--VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELL----VQYDHHY 553
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtP-----TMEEITAVAMESGAHDFISgfpqgyDTEVGETGNQLSGGQRQ 626
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
178-447 |
1.79e-14 |
|
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: 74.79 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFagdgiYNITMGH-----MHSRVHGEVFRAVLHQETGF 252
Cdd:cd18549 18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNY-----FVTYWGHvmgarIETDMRRDLFEHLQKLSFSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 253 FLKNPTGSITSRVTEDTSNVCE------------------------SISDKLNLFLwylgrgLCLLAFMIWGSFYLTvvt 308
Cdd:cd18549 93 FDNNKTGQLMSRITNDLFDISElahhgpedlfisiitiigsfiillTINVPLTLIV------FALLPLMIIFTIYFN--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 309 llslpllfllprrlGKVYQSLAvKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKpLNKKEAlaYVT 387
Cdd:cd18549 164 --------------KKMKKAFR-RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFL-ESKKKA--YKA 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 388 EVWTMSVSGM---LLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQK 447
Cdd:cd18549 225 MAYFFSGMNFftnLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-455 |
1.79e-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: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAgDGIYNITMGH--MHS-RVhgEVFRAVLHQETGFFLK 255
Cdd:cd18550 16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVV-QTYLSARIGQgvMYDlRV--QLYAHLQRMSLAFFTR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 256 NPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQE 335
Cdd:cd18550 93 TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 336 SLAKSTQVALEALSA--MPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVR 413
Cdd:cd18550 173 KLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 158262052 414 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18550 253 GGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
474-652 |
2.07e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGELLVQyd 550
Cdd:PRK13549 6 LEMKNITK----TF-----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQA-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 551 HHYLHTQ---VAAVGQEPLLF-GRSFRENIAYGltrtptmEEITA------VAMESGAHDFISGFPQGYD--TEVGETGn 618
Cdd:PRK13549 74 SNIRDTEragIAIIHQELALVkELSVLENIFLG-------NEITPggimdyDAMYLRAQKLLAQLKLDINpaTPVGNLG- 145
|
170 180 190
....*....|....*....|....*....|....
gi 158262052 619 qlsGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:PRK13549 146 ---LGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
500-664 |
2.32e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 74.74 E-value: 2.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 500 GLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG-ELLVQYDHHYLHT--QVAAVGQEPL--LFGR-SFR 573
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkDLLGMKDDEWRAVrsDIQMIFQDPLasLNPRmTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 574 ENIAYGL-------TRTPTMEEITAVAMESG-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK15079 119 EIIAEPLrtyhpklSRQEVKDRVKAMMLKVGlLPNLINRYP-----------HEFSGGQCQRIGIARALILEPKLIICDE 187
|
170
....*....|....*....
gi 158262052 646 ATSALDAGNQLRVQRLLYE 664
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQ 206
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
508-722 |
2.73e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 77.13 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 508 GKVTALVGPNGSGKSTvaaLLQNLYqptggkvlldGELLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYgLTRTPTME 587
Cdd:PTZ00243 686 GKLTVVLGATGSGKST---LLQSLL----------SQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILF-FDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 588 EITAVAMESGAHDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESpE 667
Cdd:PTZ00243 752 LADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLG-A 829
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 668 WASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMErggcyRSMVEALAA 722
Cdd:PTZ00243 830 LAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-----TSLYATLAA 879
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
236-453 |
3.07e-14 |
|
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: 74.24 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGR-GLCLLAFMIWGsFYLTVVTLLSLPL 314
Cdd:cd18558 93 KIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATfGTGFIIGFIRG-WKLTLVILAISPV 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 315 LFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEAlayVTEVWTMSV 394
Cdd:cd18558 172 LGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKA---ITFNISMGA 248
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 395 SGMLLKVG---ILYLGGQLVVRGAVSSGNLVSFVLYQLQFT-RAVEVLLSIYPSMQKSVGASE 453
Cdd:cd18558 249 AFLLIYASyalAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAfSAGQQVPSIEAFANARGAAYH 311
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
495-701 |
3.14e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 72.69 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKST----VAALLQNLYQpTGGKVLLDGEllvQYDHHYLHTQVAAVGQ-EPLLFG 569
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQ---PRKPDQFQKCVAYVRQdDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 570 RSFRENIAYGLT-RTPT---------MEEIT---AVAMESGAHDFISGfpqgydtevgetgnqLSGGQRQAVALARALIR 636
Cdd:cd03234 96 LTVRETLTYTAIlRLPRkssdairkkRVEDVllrDLALTRIGGNLVKG---------------ISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLL-ITQQLS-LAERAHHILFLKEGSVCEQG 701
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILtIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
480-702 |
9.06e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.39 E-value: 9.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAY-PNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLV--QYDHHYLH 555
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVGQEP--LLFGRSFRENIAYGLTRTP-TMEEI---TAVAMEsgahdfISGFPqgYDTEVGETGNQLSGGQRQAVA 629
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGlSEEEIenrVKRAMN------IVGLD--YEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGT 228
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
497-725 |
1.33e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.78 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTV----AALLQNLYQPTG----GKVLLDGELLVQYDHHYLHTQVAAVGQ--EPl 566
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 567 LFGRSFRENIAYGltRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARAL---------IRK 637
Cdd:PRK13547 95 AFAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 638 PRLLILDDATSALDAGNQLR----VQRLlyeSPEWaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERG-- 710
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRlldtVRRL---ARDW-NLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPAhi 248
|
250
....*....|....*.
gi 158262052 711 -GCYRSMVEALAAPSD 725
Cdd:PRK13547 249 aRCYGFAVRLVDAGDG 264
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
179-455 |
1.62e-13 |
|
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: 71.73 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKTAPSfarnMWLMCILTVASTALEFAGDGIYNITMGHMHSRV-HG---EVFRAVLHQETGFFL 254
Cdd:cd18545 17 LAGPYLIKIAIDEYIPNGDLSG----LLIIALLFLALNLVNWVASRLRIYLMAKVGQRIlYDlrqDLFSHLQKLSFSFFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTEDTSNVCE--------SISDKLNLFlwylgrglCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVY 326
Cdd:cd18545 93 SRPVGKILSRVINDVNSLSDllsnglinLIPDLLTLV--------GIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 327 QSLAVKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeALAYVTEVW-TMSVSGMLLKVGIL 404
Cdd:cd18545 165 RKAWQRVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWpLVELISALGTALVY 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 158262052 405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18545 243 WYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
497-697 |
1.85e-13 |
|
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: 69.38 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVqydhhylhtqvaavgqepllfGRSFRENI 576
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT---------------------RRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGltrtptmeeITAVAMESGAHDFISGFPqgydteVGE---TGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:cd03215 74 RAG---------IAYVPEDRKREGLVLDLS------VAEniaLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158262052 654 NQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:cd03215 139 AKAEIYRLIRELAD-AGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
495-700 |
2.06e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAAVGQEPLLF-GRSFr 573
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE----ARAKLRAKHVGFvFQSF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 574 eniayglTRTPTM---EEITAVAMESGAHDFISG------FPQ-GYDTEVGETGNQLSGGQRQAVALARALIRKPRLLIL 643
Cdd:PRK10584 98 -------MLIPTLnalENVELPALLRGESSRQSRngakalLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 644 DDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQ 700
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
475-650 |
2.20e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGellVQYDH--H 552
Cdd:PRK09700 1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKldH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 553 YLHTQ--VAAVGQEPLLFGR-SFRENIAYGltRTPT-------------MEEITAVAMesgahdFISGFPQGYDTEVGEt 616
Cdd:PRK09700 75 KLAAQlgIGIIYQELSVIDElTVLENLYIG--RHLTkkvcgvniidwreMRVRAAMML------LRVGLKVDLDEKVAN- 145
|
170 180 190
....*....|....*....|....*....|....
gi 158262052 617 gnqLSGGQRQAVALARALIRKPRLLILDDATSAL 650
Cdd:PRK09700 146 ---LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
476-687 |
3.75e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYD-HHYL 554
Cdd:PRK11614 2 EKVMLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTQVAAVGQEPLLFGR-SFRENIAYG---LTRTPTMEEITAVamesgaHDFisgFPQGYDTEVGETGNqLSGGQRQAVAL 630
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMGgffAERDQFQERIKWV------YEL---FPRLHERRIQRAGT-MSGGEQQMLAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 631 ARALIRKPRLLILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLI----TQQLSLAERAH 687
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLapiiiqqifDTIEQLREQGM----------TIFLVeqnaNQALKLADRGY 208
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
480-702 |
4.17e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.91 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGELLVQYDHHYLHT 556
Cdd:PRK09473 15 VKDLRVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 ----QVAAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEE----ITAVAMESgAHDFISGFPqgydtevgetgNQ 619
Cdd:PRK09473 94 lraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEEsvrmLDAVKMPE-ARKRMKMYP-----------HE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVC 698
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241
|
....
gi 158262052 699 EQGT 702
Cdd:PRK09473 242 EYGN 245
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
480-695 |
4.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 70.63 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAY-PNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHY---- 553
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 554 LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFpqGYDTEVGETGN-QLSGGQRQAVAL 630
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 631 ARALIRKPRLLILDDATSALDAGNQLRVQRLLYESpEWASRTVLLITQQL-SLAERAHHILFLKEG 695
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
506-706 |
6.13e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 69.74 E-value: 6.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 506 YPGK-VTALVGPNGSGKSTVAALLQNLYQPTGG-----KVLLDGELLVQY-DHHYLHTQVAAVGQEPLLFGRSFRENIAY 578
Cdd:PRK14271 44 FPARaVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 579 GLT----------RTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:PRK14271 124 GVRahklvprkefRGVAQARLTEVGLWDAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 649 ALDAGNQLRVQRLLYespEWASR-TVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQL 706
Cdd:PRK14271 193 ALDPTTTEKIEEFIR---SLADRlTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
493-702 |
9.38e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHY--LHTQ------------V 558
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVieLSEQsaaqmrhvrgadM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEEITAVAME---SGAHDFISGFPqgydtevgetgNQLSGGQRQ 626
Cdd:PRK10261 107 AMIFQEPMTslnpvftVGEQIAESIRLhqGASREEAMVEAKRMLDQvriPEAQTILSRYP-----------HQLSGGMRQ 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
476-650 |
1.48e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylH 555
Cdd:PRK10762 1 MQALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 TQVAAVG---QEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFIS--GFPQGYDTEVGEtgnqLSGGQRQAVA 629
Cdd:PRK10762 76 SQEAGIGiihQELNLIPQlTIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180
....*....|....*....|.
gi 158262052 630 LARALIRKPRLLILDDATSAL 650
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDAL 172
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
507-678 |
2.33e-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: 65.09 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 507 PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL-LDGELLVQYDHHYLHtqvaavgqepllfgrsfreniaygltrtpt 585
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 586 meeitavamesgahdfisgfpqgyDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ-----R 660
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelR 106
|
170
....*....|....*...
gi 158262052 661 LLYESPEWASRTVLLITQ 678
Cdd:smart00382 107 LLLLLKSEKNLTVILTTN 124
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
498-701 |
2.48e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.64 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL---DGELLVQYD------HHYLHTQVAAVGQEP--- 565
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYAlseaerRRLLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 566 LLFGRSFRENIA----------YGLTRTPTMEEITAVAMESgahDFISGFPQGYdtevgetgnqlSGGQRQAVALARALI 635
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYGDIRATAGDWLERVEIDA---ARIDDLPTTF-----------SGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAeR--AHHILFLKEGSVCEQG 701
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVA-RllAHRLLVMKQGRVVESG 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
499-692 |
2.73e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 66.37 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 499 QGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYlHTQVAAVGQ----EPLLfgrSFRE 574
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHqpgiKTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 575 NIAYGLT-RTPTMEEITAVAMEsgahdfisgfpqgydtEVGETG------NQLSGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:PRK13538 94 NLRFYQRlHGPGDDEALWEALA----------------QVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158262052 648 SALDAGNQLRVQRLLYESpewASR--TVLLIT-QQLSLAERAHHILFL 692
Cdd:PRK13538 158 TAIDKQGVARLEALLAQH---AEQggMVILTThQDLPVASDKVRKLRL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
483-677 |
2.97e-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: 69.58 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSFAYPnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYdhhylhtqvaaVG 562
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGY-----------LP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 563 QEPLL-FGRSFRENIAYGLTRTP-TMEEITAVAME------------------------SGAHDFISGF---------PQ 607
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKdALDRFNEISAKyaepdadfdklaaeqaelqeiidaADAWDLDSQLeiamdalrcPP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 608 GyDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEWASR-------TVLLIT 677
Cdd:TIGR03719 155 W-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-----------ESVAWLERhlqeypgTVVAVT 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
496-644 |
3.25e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.98 E-value: 3.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHylhtQVAAVG-----QEPLLFGR 570
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH----KRARLGigylpQEASIFRK 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 571 -SFRENIAYGL-TRTPTMEEITAvAMESGAHDF-IsgfpqgydTEVGET-GNQLSGGQRQAVALARALIRKPRLLILD 644
Cdd:COG1137 93 lTVEDNILAVLeLRKLSKKEREE-RLEELLEEFgI--------THLRKSkAYSLSGGERRRVEIARALATNPKFILLD 161
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
619-702 |
4.23e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 67.84 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSV 697
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQV 232
|
....*
gi 158262052 698 CEQGT 702
Cdd:PRK11022 233 VETGK 237
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-708 |
4.27e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.79 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ-----PTGGKVLLDGELLVQYDHHYLHT--QVAAVGQEPLLF 568
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIEVrrEVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 569 GR-SFRENIAYGL------TRTPTMEEITAVAMESGA-----HDFISGFPqgydtevgetgNQLSGGQRQAVALARALIR 636
Cdd:PRK14267 98 PHlTIYDNVAIGVklnglvKSKKELDERVEWALKKAAlwdevKDRLNDYP-----------SNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158262052 637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
474-652 |
4.97e-12 |
|
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: 68.70 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKfqdvSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGELLVQyd 550
Cdd:TIGR02633 2 LEMKGIVK----TFG-----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 551 HHYLHTQ---VAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFpQGYDTEVGETGNQLSGGQRQ 626
Cdd:TIGR02633 70 SNIRDTEragIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQ 148
|
170 180
....*....|....*....|....*.
gi 158262052 627 AVALARALIRKPRLLILDDATSALDA 652
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTE 174
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
493-702 |
5.84e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNlYQPTG----GKVLLDGELL-----------VQYDHHYLHTQ 557
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPIdakemraisayVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAavgQEPLLFGRSFR--ENIAYGLTRTPTMEEITAVAMESGAHdfisgfpqgydTEVGETGNQ--LSGGQRQAVALARA 633
Cdd:TIGR00955 115 TV---REHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCAN-----------TRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGS 250
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
454-723 |
6.00e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 454 KIFEYLDRTPcsPLSGSLaplnmKGLVKfqdvsfayPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ 533
Cdd:COG4586 9 KTYRVYEKEP--GLKGAL-----KGLFR--------REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 534 PTGGKVLLDGELLVQYDHHYLHtQVAAV-GQE-------PLLfgRSFRENIA-YGLTRT---PTMEEITAVaMEsgahdf 601
Cdd:COG4586 74 PTSGEVRVLGYVPFKRRKEFAR-RIGVVfGQRsqlwwdlPAI--DSFRLLKAiYRIPDAeykKRLDELVEL-LD------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 602 ISGFpqgYDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS 681
Cdd:COG4586 144 LGEL---LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMD 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 158262052 682 ----LAERahhILFLKEGSVCEQGTHLQLMERGGCYRSMVEALAAP 723
Cdd:COG4586 217 dieaLCDR---VIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEP 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
495-680 |
6.02e-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: 68.68 E-value: 6.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV-LLDGELLVQ-----YDHHYLHTQ-VAAVGQEPLL 567
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDmtkpgPDGRGRAKRyIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 568 FG-RSFRENiaygLTRTPTMEEITAVAMESGAHDFIS-GFPQGYDTEVGET-GNQLSGGQRQAVALARALIRKPRLLILD 644
Cdd:TIGR03269 377 YPhRTVLDN----LTEAIGLELPDELARMKAVITLKMvGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190
....*....|....*....|....*....|....*.
gi 158262052 645 DATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL 680
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
484-682 |
7.79e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 7.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 484 DVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGElLVQYDHHYLHTQVAAVGQ 563
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ-SIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 E----PLLfgrSFRENIAYGLTRTPTMEEITAVAMESGAHDFISgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPR 639
Cdd:PRK13540 82 RsginPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 158262052 640 LLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL 682
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPL 190
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
483-677 |
1.50e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.45 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSFAYPnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYdhhylhtqvaaVG 562
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGY-----------LP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 563 QEPLL-FGRSFRENIAYG-------LTR---------TPtMEEITAVAMESG----------AHDFIS---------GFP 606
Cdd:PRK11819 77 QEPQLdPEKTVRENVEEGvaevkaaLDRfneiyaayaEP-DADFDALAAEQGelqeiidaadAWDLDSqleiamdalRCP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 607 QGyDTEVGetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEWASR-------TVLLIT 677
Cdd:PRK11819 156 PW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-----------ESVAWLEQflhdypgTVVAVT 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
476-716 |
1.96e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.03 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY---QPTGGKVLLDGELL-----V 547
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQH---QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqregrL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 548 QYDHHYLHTQVAAVGQEPLLFGR-SFRENIAYG-LTRTP----------------TMEEITAVAMESGAHDFISgfpqgy 609
Cdd:PRK09984 78 ARDIRKSRANTGYIFQQFNLVNRlSVLENVLIGaLGSTPfwrtcfswftreqkqrALQALTRVGMVHFAHQRVS------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 610 dtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHH 688
Cdd:PRK09984 152 ---------TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCER 222
|
250 260 270
....*....|....*....|....*....|
gi 158262052 689 ILFLKEGSVCEQGTHLQL-MER-GGCYRSM 716
Cdd:PRK09984 223 IVALRQGHVFYDGSSQQFdNERfDHLYRSI 252
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
482-699 |
2.21e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.92 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 482 FQDVSFAYPNhPNVQVlQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAV 561
Cdd:PRK10522 325 LRNVTFAYQD-NGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 562 GQEPLLFGRsfreniayglTRTPTMEEITAVAMESGAHdfISGFPQGYDTEVGETGN-QLSGGQRQAVALARALIRKPRL 640
Cdd:PRK10522 403 FTDFHLFDQ----------LLGPEGKPANPALVEKWLE--RLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 641 LILDDAtsALDAGNQLR---VQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSVCE 699
Cdd:PRK10522 471 LLLDEW--AADQDPHFRrefYQVLLPLLQE-MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
495-708 |
2.66e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE---LLVQYDHHYLHTQVAAVGQEP------ 565
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasldp 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 566 ----------------LLFGRSFRENIAYGLTRTPTMEEitavamesgaHDFisGFPqgydtevgetgNQLSGGQRQAVA 629
Cdd:PRK10261 417 rqtvgdsimeplrvhgLLPGKAAAARVAWLLERVGLLPE----------HAW--RYP-----------HEFSGGQRQRIC 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
618-709 |
3.35e-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: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 618 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGS 696
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLeSISQWADTITVLYCGQ 236
|
90
....*....|...
gi 158262052 697 VCEQGTHLQLMER 709
Cdd:COG4170 237 TVESGPTEQILKS 249
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
403-546 |
3.58e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 403 ILYLGGQLvvrGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIfEYLDRTPCSPLSGSLAPLNMKGLVKF 482
Cdd:COG4615 250 ILFLLPAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKI-EELELALAAAEPAAADAAAPPAPADF 325
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 483 Q-----DVSFAYPN--HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELL 546
Cdd:COG4615 326 QtlelrGVTYRYPGedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
179-455 |
8.01e-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: 63.62 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFagdgIYNITMGHMHSRVHGEV----FRAVLHQETGFFL 254
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSY----IRSYLLLKLSQKLDIRLilgyFKHLLKLPLSFFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 255 KNPTGSITSRVTeDTSNVCESISDK-----LNLFLwylgrGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSL 329
Cdd:cd18570 95 TRKTGEIISRFN-DANKIREAISSTtislfLDLLM-----VIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 330 AVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA-LAYVTEVWTMSVSGmLLKVGILYLGG 408
Cdd:cd18570 169 NREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGkLSNLQSSIKGLISL-IGSLLILWIGS 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 158262052 409 QLVVRGAVSSGNLVSFvlYQLQ--FTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18570 248 YLVIKGQLSLGQLIAF--NALLgyFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
500-701 |
8.94e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 8.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 500 GLTFTLYPGKVTALVGPNGSGKS-TVAALLQNL---YQPTGGKVLLDGELLVQYDHHYLHtqVAAVGQEPllfgRS-F-- 572
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRK--IATIMQNP----RSaFnp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 573 --------RENI-AYGLTRTPT--MEEITAVAMESgAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLL 641
Cdd:PRK10418 95 lhtmhthaRETClALGKPADDAtlTAALEAVGLEN-AARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 642 ILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
475-645 |
1.04e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 62.86 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYL 554
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HT---QVAAVGQEPLLF-GRSFRENIAYGL---TRTP-------TMEEITAVAMESGAHDFISgfpqgydtevgetgnQL 620
Cdd:PRK11831 80 YTvrkRMSMLFQSGALFtDMNVFDNVAYPLrehTQLPapllhstVMMKLEAVGLRGAAKLMPS---------------EL 144
|
170 180
....*....|....*....|....*
gi 158262052 621 SGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDE 169
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
180-455 |
1.04e-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: 63.32 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMG-HMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18778 17 VPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEqKVVADLRSDLYDKLQRLSLRYFDDRQT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 259 GSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLA 338
Cdd:cd18778 97 GDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 339 KSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKplnkkEALAYVTEVW-----TMSVSGMLLKVGILYLGGQLVVR 413
Cdd:cd18778 177 ELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYR-----KAQLRAMKLWaifhpLMEFLTSLGTVLVLGFGGRLVLA 251
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 158262052 414 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18778 252 GELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
497-697 |
1.22e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVqydhhyLHTQVAAVGQ-----------EP 565
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDAIRAgiayvpedrkgEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 566 LLFGRSFRENIA---------YGLTRTPTMEEITAvamesgahDFISGF---PQGYDTEVGetgnQLSGGQRQAVALARA 633
Cdd:COG1129 341 LVLDLSIRENITlasldrlsrGGLLDRRRERALAE--------EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESpewASR--TVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIREL---AAEgkAVIVISSELPeLLGLSDRILVMREGRI 472
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
494-707 |
1.25e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.26 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQV---LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTGGKVLLDGELLVQYDHH-------YLHTQVAAVGQ 563
Cdd:PRK03695 5 DVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarhraYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 EPLlfgrsFRENIAYGLTRTPTMEEITAVamesgaHDFISGFpqGYDTEVGETGNQLSGGQRQAVALARALIR-----KP 638
Cdd:PRK03695 84 MPV-----FQYLTLHQPDKTRTEAVASAL------NEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 639 --RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGTHLQLM 707
Cdd:PRK03695 151 agQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
497-695 |
1.40e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG--GKVLLDGE-----------LLVQYDHHYLHTQVaavgQ 563
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRkptkqilkrtgFVTQDDILYPHLTV----R 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 564 EPLLFGRSFReniaygLTRTPTMEEITAVAmESGAHDFisGFPQGYDTEVGETGNQ-LSGGQRQAVALARALIRKPRLLI 642
Cdd:PLN03211 159 ETLVFCSLLR------LPKSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158262052 643 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEG 695
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEG 283
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
501-706 |
1.96e-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: 64.65 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE--------------LLVQYDHHYLHTQVAavgqEPL 566
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqslgMCPQHNILFHHLTVA----EHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 567 LF-----GRSFREniaygltrtpTMEEITAVAMESGAHDfisgfpqgydtEVGETGNQLSGGQRQAVALARALIRKPRLL 641
Cdd:TIGR01257 1025 LFyaqlkGRSWEE----------AQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 642 ILDDATSALDAGNQLRVQRLL--YESpewaSRTVLLITQQLSLAE-RAHHILFLKEGSVCEQGTHLQL 706
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLlkYRS----GRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
504-676 |
4.02e-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: 60.88 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 504 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGElLVQYDHHY------------LHTQVAAVGQEPllfgrS 571
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYikadyegtvrdlLSSITKDFYTHP-----Y 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 572 FRENIAYGLtrtpTMEEItavamesgahdfisgfpqgYDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:cd03237 95 FKTEIAKPL----QIEQI-------------------LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180
....*....|....*....|....*
gi 158262052 652 AGNQLRVQRLLYESPEWASRTVLLI 676
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVV 172
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
479-651 |
5.56e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.57 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQ-YDHHylHTQ 557
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvFSQH--HVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQEPLLFgrsfreniaygltrtptMEEITAVAMESGAHDFISGFpqgydtevGETGN-------QLSGGQRQAVAL 630
Cdd:PLN03073 584 GLDLSSNPLLY-----------------MMRCFPGVPEQKLRAHLGSF--------GVTGNlalqpmyTLSGGQKSRVAF 638
|
170 180
....*....|....*....|.
gi 158262052 631 ARALIRKPRLLILDDATSALD 651
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLD 659
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
486-652 |
6.77e-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: 59.20 E-value: 6.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 486 SFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQPTGGKVLLDGELL---VQYD--HHYLHTQVAA 560
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALANRTEGNVSVEGDIHyngIPYKefAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 561 VGQE----PLLfgrsfreniaygltrtpTMEEITAVAMESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARALIR 636
Cdd:cd03233 88 VSEEdvhfPTL-----------------TVRETLDFALRCKGNEFVRGI---------------SGGERKRVSIAEALVS 135
|
170
....*....|....*.
gi 158262052 637 KPRLLILDDATSALDA 652
Cdd:cd03233 136 RASVLCWDNSTRGLDS 151
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
495-702 |
6.99e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.02 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL-------DGELLVQYDHHY---------LHTQV 558
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdKKNNHELITNPYskkiknfkeLRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVGQEP--LLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFPQGYD-TEVGETGnqLSGGQRQAVALARALI 635
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
480-701 |
8.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAY----PNHpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV---------------- 539
Cdd:PRK13651 3 IKVKNIVKIFnkklPTE--LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 540 -LLDGELLVQYDHHY-------LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFIS--GFPQ 607
Cdd:PRK13651 81 eKVLEKLVIQKTRFKkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 608 GYdteVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERA 686
Cdd:PRK13651 157 SY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLdNVLEWT 232
|
250
....*....|....*
gi 158262052 687 HHILFLKEGSVCEQG 701
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
474-650 |
1.03e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.34 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEL----- 545
Cdd:NF040905 2 LEMRGITK----TF-----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 546 LVQYDHH---YLHTQVAAVgqePLLfgrSFRENI-------AYGL-----TRTPTMEEITAVamesgahdfisGFPQGYD 610
Cdd:NF040905 72 IRDSEALgivIIHQELALI---PYL---SIAENIflgneraKRGVidwneTNRRARELLAKV-----------GLDESPD 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 158262052 611 TEVGETGNqlsgGQRQAVALARALIRKPRLLILDDATSAL 650
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 ... |
480-651 |
1.11e-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: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGELLvqydhhylhtQVA 559
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 560 AVGQ--EPLLFGRSFRENIAYGLtrtpTMEEITAVAMESGAhdFISGFP-QGYDTE--VGetgnQLSGGQRQAVALARAL 634
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGL----DIIKLGKREIPSRA--YVGRFNfKGSDQQkkVG----QLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 158262052 635 IRKPRLLILDDATSALD 651
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
496-702 |
2.32e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.37 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE-LLVQYDHHYLHTQVAAVGQEPLLFGR-SFR 573
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdISLLPLHARARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 574 ENIAYGLTrtpTMEEITAVAMESGAHDFISGFPQGYDTEvgETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK10895 97 DNLMAVLQ---IRDDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 158262052 654 NQLRVQRLLYESPEwaSRTVLLIT-----QQLSLAERAHhilFLKEGSVCEQGT 702
Cdd:PRK10895 172 SVIDIKRIIEHLRD--SGLGVLITdhnvrETLAVCERAY---IVSQGHLIAHGT 220
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
404-682 |
2.55e-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: 60.53 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 404 LYLGGQLVVRGAVSSGNLVSFV--LYQLQ-FTRAVEVLLSIYPSMQK------SVGASEKIFEYLDRTPCSPLSGSLapL 474
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLMLAGrdMTRLAgFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV--E 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYdhhyl 554
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY----- 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 htqvaaVGQEPLLFGRSFRENIAYGLT---------RTPTMEEItavaMESGAHDFISGFPQGYDTeVGETGNQLSGGQR 625
Cdd:TIGR00954 520 ------VPQRPYMTLGTLRDQIIYPDSsedmkrrglSDKDLEQI----LDNVQLTHILEREGGWSA-VQDWMDVLSGGEK 588
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 626 QAVALARALIRKPRLLILDDATSALdagnQLRVQRLLYESPEWASRTVLLITQQLSL 682
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSL 641
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
496-695 |
1.09e-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: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQPTGGKVLLDGELLV-----------------QYDhhyLHTQV 558
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVngrpldssfqrsigyvqQQD---LHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 AAVgQEPLLFGRSFREniAYGLTRTPTMEEITAV----AMESGAhdfisgfpqgyDTEVGETGNQLSGGQRQAVALARAL 634
Cdd:TIGR00956 851 STV-RESLRFSAYLRQ--PKSVSKSEKMEYVEEVikllEMESYA-----------DAVVGVPGEGLNVEQRKRLTIGVEL 916
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158262052 635 IRKPRLLI-LDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEG 695
Cdd:TIGR00956 917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaiLFEEFDRLLLLQKG 979
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
480-706 |
1.54e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 57.35 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE-------------LL 546
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergvgMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 547 VQYDHHYLHTQVAavgqepllfgrsfrENIAYGL-----------TRTPTMEEITAVAmesgaHdFISGFPQGydtevge 615
Cdd:PRK11000 81 FQSYALYPHLSVA--------------ENMSFGLklagakkeeinQRVNQVAEVLQLA-----H-LLDRKPKA------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 616 tgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGnqLRVQ----------RLlyespewaSRTVLLITQ-QLSLAE 684
Cdd:PRK11000 134 ----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA--LRVQmrieisrlhkRL--------GRTMIYVTHdQVEAMT 199
|
250 260
....*....|....*....|..
gi 158262052 685 RAHHILFLKEGSVCEQGTHLQL 706
Cdd:PRK11000 200 LADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
502-682 |
1.69e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 502 TFTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV--------LLD---GELLVQYDHHYLHTQVAAVgQE 564
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVI-VK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 565 PL---LFGRSFRENIAYGLTRTPtmeeitavamESGAHDFIS---GFPQGYDTEVgetgNQLSGGQRQAVALARALIRKP 638
Cdd:cd03236 93 PQyvdLIPKAVKGKVGELLKKKD----------ERGKLDELVdqlELRHVLDRNI----DQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 158262052 639 RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSL 682
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAV 201
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
483-685 |
2.21e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSfaYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYD-HHYLHTQVAAV 561
Cdd:COG3845 261 ENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 562 GQEPLLFG----RSFRENIAYGLTRTPTMEE---ITAVAMESGAHDFISGF---PQGYDTEVGetgnQLSGGQRQAVALA 631
Cdd:COG3845 339 PEDRLGRGlvpdMSVAENLILGRYRRPPFSRggfLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILA 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 158262052 632 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL----SLAER 685
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLdeilALSDR 471
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
502-653 |
2.76e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 502 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLV-QYDHHYLHTQVAAVGQEP----LLFGRSFRENI 576
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRkrdgLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 --------AYGLTRTPTMEEITAVAmesgahDFISGF----PqGYDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILD 644
Cdd:PRK10762 352 sltalryfSRAGGSLKHADEQQAVS------DFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420
|
....*....
gi 158262052 645 DATSALDAG 653
Cdd:PRK10762 421 EPTRGVDVG 429
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
495-681 |
2.97e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKST-VAALLQNLYQ---PTGGKVLLDG----ELLVQY----------DHHYLHT 556
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGitpeEIKKHYrgdvvynaetDVHFPHL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVaavgQEPLLFGRSFR--ENIAYGLTRTPTMEEITAVAMEsgahdfISGFPQGYDTEVG-ETGNQLSGGQRQAVALARA 633
Cdd:TIGR00956 154 TV----GETLDFAARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS 681
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCS 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
504-660 |
3.09e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 504 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGELLVQYDHHYLHTQVAAVGQEpLL------FGRSF-RENI 576
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDYDGTVED-LLrsitddLGSSYyKSEI 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYGLtrtpTMEEItavamesgahdfisgfpqgYDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQL 656
Cdd:PRK13409 438 IKPL----QLERL-------------------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490
|
....
gi 158262052 657 RVQR 660
Cdd:PRK13409 491 AVAK 494
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
178-455 |
3.26e-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: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 178 EMAIPFFTGRITDwilqDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVH----GEVFRAVLHQETGFF 253
Cdd:cd18543 15 GLAIPLLTRRAID----GPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEhdlrTDLFAHLQRLDGAFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 254 LKNPTGSITSRVTEDTSnvceSISDKLNLFLWYLGRGLCL---LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLA 330
Cdd:cd18543 91 DRWQSGQLLSRATSDLS----LVQRFLAFGPFLLGNLLTLvvgLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 331 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMkplnkkealaYVTEV----------WTMSVSGMLLK 400
Cdd:cd18543 167 RRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRL----------RATRLraarlrarfwPLLEALPELGL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 401 VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18543 237 AAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
483-651 |
4.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.50 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 483 QDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQY-DHHYlhtqvAAV 561
Cdd:PRK11147 323 ENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYfDQHR-----AEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 562 GQEpllfgRSFRENIAYGltrtptMEEITAVAMESGAHDFISGF---PQGYDTEVgetgNQLSGGQRQAVALARALIRKP 638
Cdd:PRK11147 395 DPE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPS 459
|
170
....*....|...
gi 158262052 639 RLLILDDATSALD 651
Cdd:PRK11147 460 NLLILDEPTNDLD 472
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
332-430 |
4.65e-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: 55.10 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGILYLGGQL 410
Cdd:cd18548 169 KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKaGRLMALLNPLMMLIMNLAI-VAILWFGGHL 247
|
90 100
....*....|....*....|
gi 158262052 411 VVRGAVSSGNLVSFVLYQLQ 430
Cdd:cd18548 248 INAGSLQVGDLVAFINYLMQ 267
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
496-651 |
4.74e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.80 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGELLV----------------QY-------- 549
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLelspedragegifmafQYpveipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 550 DHHYLHTQVAAV----GQEPLlfGR-SFRENIAygltrtptmEEITAVAMesgahdfisgfPQGYDTEVGETGnqLSGGQ 624
Cdd:PRK09580 95 NQFFLQTALNAVrsyrGQEPL--DRfDFQDLME---------EKIALLKM-----------PEDLLTRSVNVG--FSGGE 150
|
170 180
....*....|....*....|....*..
gi 158262052 625 RQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
510-651 |
4.91e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 510 VTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVqyDHH---YLHTQVAAVG---QEPLLFGR-SFRENIAYGLTR 582
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEkgiCLPPEKRRIGyvfQDARLFPHyKVRGNLRYGMAK 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 583 TPTMEEITAVAMESGAHdFISGFPQGydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK11144 104 SMVAQFDKIVALLGIEP-LLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
493-650 |
5.38e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG-ELLVQYDHHYLHTQVAAVGQE-PLLFGR 570
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkEIDFKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 SFRENIAYGltRTPTMEEItaVAMESGAHDFISGFPQ-GYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 649
Cdd:PRK10982 89 SVMDNMWLG--RYPTKGMF--VDQDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
.
gi 158262052 650 L 650
Cdd:PRK10982 165 L 165
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
474-706 |
6.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.01 E-value: 6.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 474 LNMKGLVKFQDVSFAYPNHP--NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY-QPTGGKVLLDGELLVQYD 550
Cdd:PRK13645 1 FDFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiSETGQTIVGDYAIPANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 551 H----HYLHTQVAAVGQEP--LLFGRSFRENIAYG-LTRTPTMEEITAVAMEsgAHDFISgFPQGYdteVGETGNQLSGG 623
Cdd:PRK13645 81 KikevKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGENKQEAYKKVPE--LLKLVQ-LPEDY---VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
....
gi 158262052 703 HLQL 706
Cdd:PRK13645 235 PFEI 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
497-677 |
7.10e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 7.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY--QPTGGKVLLDgellvqydhhylhtqVAAVGQE-PLLfgrsfr 573
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP---------------DNQFGREaSLI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 574 ENIAYGLTRTPTMEEITAVAMeSGAHDFISGFPqgydtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:COG2401 104 DAIGRKGDFKDAVELLNAVGL-SDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....
gi 158262052 654 NQLRVQRLLYESPEWASRTVLLIT 677
Cdd:COG2401 171 TAKRVARNLQKLARRAGITLVVAT 194
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
180-424 |
8.93e-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: 54.49 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFagdgIYNITMGHMHSRVH----GEVFRAVLHQETGFFLK 255
Cdd:cd18568 20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSA----VRQYLLDYFANRIDlsllSDFYKHLLSLPLSFFAS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 256 NPTGSITSRVTED-------TSNVCESISDKLNLFLwYLGrglcllaFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQS 328
Cdd:cd18568 96 RKVGDIITRFQENqkirrflTRSALTTILDLLMVFI-YLG-------LMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 329 LAVKVQESLAKSTQVALEALSAMPTVRSFANEegeaQKFRQKLEE--MKPLN---KKEALAYVTEVwTMSVSGMLLKVGI 403
Cdd:cd18568 168 NSREIFQANAEQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNtrfRGQKLSIVLQL-ISSLINHLGTIAV 242
|
250 260
....*....|....*....|.
gi 158262052 404 LYLGGQLVVRGAVSSGNLVSF 424
Cdd:cd18568 243 LWYGAYLVISGQLTIGQLVAF 263
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
497-651 |
1.19e-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: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGE----------------LLVQY--------D 550
Cdd:TIGR01978 15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQdllelepderaraglfLAFQYpeeipgvsN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 551 HHYLHTQVAAV----GQEPL---LFGRSFRENIAygltrtptmeeitAVAM-ESGAHDFIS-GFpqgydtevgetgnqlS 621
Cdd:TIGR01978 95 LEFLRSALNARrsarGEEPLdllDFEKLLKEKLA-------------LLDMdEEFLNRSVNeGF---------------S 146
|
170 180 190
....*....|....*....|....*....|
gi 158262052 622 GGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:TIGR01978 147 GGEKKRNEILQMALLEPKLAILDEIDSGLD 176
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
495-709 |
1.52e-07 |
|
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: 54.42 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVL----------------LDGELLVQYDHHYLHT 556
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLLFgRSFRENIAYGLTRT--------------PTMEEITAVAMES--GAHDFISGFPQGYdtEVGETGNQL 620
Cdd:TIGR03269 93 EVDFWNLSDKLR-RRIRKRIAIMLQRTfalygddtvldnvlEALEEIGYEGKEAvgRAVDLIEMVQLSH--RITHIARDL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 621 SGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEGSVC 698
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVK-ASGISMVLTSHWPevIEDLSDKAIWLENGEIK 248
|
250
....*....|.
gi 158262052 699 EQGTHLQLMER 709
Cdd:TIGR03269 249 EEGTPDEVVAV 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
504-662 |
1.59e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.79 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 504 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGELLVQYDHHYLHTQVAAVGQEPLlfgrsfRENIAYGLTRT 583
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFL------RSANTDDFGSS 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 584 PTMEEITavamesgahdfisgFPQG----YDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ 659
Cdd:COG1245 434 YYKTEII--------------KPLGleklLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495
|
...
gi 158262052 660 RLL 662
Cdd:COG1245 496 KAI 498
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
490-680 |
1.72e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.28 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 490 PNHPN--VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYDHHYLHTQVAAVgqepll 567
Cdd:PRK13546 30 PKHKNktFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 568 fgrsfrENIAY-----GLTRtptmEEITAVAMEsgahdfISGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKP 638
Cdd:PRK13546 104 ------ENIEFkmlcmGFKR----KEIKAMTPK------IIEF-----SELGEFIYQpvkkYSSGMRAKLGFSINITVNP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 158262052 639 RLLILDDatsALDAGNQLRVQRLL---YESPEwASRTVLLITQQL 680
Cdd:PRK13546 163 DILVIDE---ALSVGDQTFAQKCLdkiYEFKE-QNKTIFFVSHNL 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
479-651 |
2.12e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQYdhhylhtqv 558
Cdd:PRK10636 312 LLKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGY--------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 559 aaVGQEPLLFGRSfRENIAYGLTRTPTMEeitavaMESGAHDFISGFP-QGydTEVGETGNQLSGGQRQAVALARALIRK 637
Cdd:PRK10636 380 --FAQHQLEFLRA-DESPLQHLARLAPQE------LEQKLRDYLGGFGfQG--DKVTEETRRFSGGEKARLVLALIVWQR 448
|
170
....*....|....
gi 158262052 638 PRLLILDDATSALD 651
Cdd:PRK10636 449 PNLLLLDEPTNHLD 462
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
480-651 |
3.13e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpnvQVL-QGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEllvqydhhylhT-Q 557
Cdd:PRK11819 325 IEAENLSKSFGD----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE-----------TvK 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 558 VAAVGQepllfgrsFRENIAYGLTrtpTMEEItavameSGAHDFIS---------------GFpQGYDTE--VGetgnQL 620
Cdd:PRK11819 389 LAYVDQ--------SRDALDPNKT---VWEEI------SGGLDIIKvgnreipsrayvgrfNF-KGGDQQkkVG----VL 446
|
170 180 190
....*....|....*....|....*....|.
gi 158262052 621 SGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
496-695 |
4.27e-07 |
|
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: 50.70 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 496 QVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQPT-----GGKVLLDGELLVQY--------DHHYLHTQVAAVg 562
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDKNfqrstgyvEQQDVHSPNLTV- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 563 QEPLLFGRSFREniaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLI 642
Cdd:cd03232 97 REALRFSALLRG---------------------------------------------LSVEQRKRLTIGVELAAKPSILF 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 643 LDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEG 695
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
491-695 |
5.10e-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: 50.05 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 491 NHPNVQVLQGLTFTlyPGKVTALVGPNGSGKSTVAallqnlyqptggkvlldgellvqydhhylhTQVAAVgqeplLFGR 570
Cdd:cd03227 6 RFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTIL------------------------------DAIGLA-----LGGA 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 SFRENIAYGLTRTptmEEITAVAMEsgahdFISGFPQgydtevgetgnqLSGGQRQAVALARALI---RKPR-LLILDDA 646
Cdd:cd03227 49 QSATRRRSGVKAG---CIVAAVSAE-----LIFTRLQ------------LSGGEKELSALALILAlasLKPRpLYILDEI 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 158262052 647 TSALDAGNQLRVQRLLYE-SPEwaSRTVLLITQQLSLAERA---HHILFLKEG 695
Cdd:cd03227 109 DRGLDPRDGQALAEAILEhLVK--GAQVIVITHLPELAELAdklIHIKKVITG 159
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
188-455 |
5.52e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 52.13 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 188 ITDWILQDKTAPSFA--------RNM---WLMCILTVASTALEFAGDGIYNITMG----HMHSRVHGEVFRAVLHQETGF 252
Cdd:cd18564 25 VIDDVLGDKPLPGLLglapllgpDPLallLLAAAALVGIALLRGLASYAGTYLTAlvgqRVVLDLRRDLFAHLQRLSLSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 253 FLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVK 332
Cdd:cd18564 105 HDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASRE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 333 VQESLAKSTQVALEALSAMPTVRSFANEEGEAQKF----RQKLEE-MKPLNKKEALAYVTEVwTMSVSGMLlkvgILYLG 407
Cdd:cd18564 185 QRRREGALASVAQESLSAIRVVQAFGREEHEERRFarenRKSLRAgLRAARLQALLSPVVDV-LVAVGTAL----VLWFG 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 158262052 408 GQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18564 260 AWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
190-458 |
7.29e-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: 51.35 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 190 DWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSR----VHGEVFRAVLHQETGFFLKNPTGSITSRV 265
Cdd:cd18580 23 DWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRasrrLHDKLLRSVLRAPMSFFDTTPSGRILNRF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 266 TEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTllslPLLFLLPRRLGKVYQSLA--VKVQESLAKS--- 340
Cdd:cd18580 103 SKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL----PPLLVVYYLLQRYYLRTSrqLRRLESESRSply 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 341 TQVaLEALSAMPTVRSFANEEGEAQKFRQKLEE-MKPLNkkeaLAYVTEVW-----TMSVSGMLLKVGILylggqLVVRG 414
Cdd:cd18580 179 SHF-SETLSGLSTIRAFGWQERFIEENLRLLDAsQRAFY----LLLAVQRWlglrlDLLGALLALVVALL-----AVLLR 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 158262052 415 AVSSGNLVSFVLYQ-LQFTRAVEVLLSIYPSMQKSVGASEKIFEY 458
Cdd:cd18580 249 SSISAGLVGLALTYaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
498-701 |
1.10e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 50.65 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVlldgellvqydhhylhtqvaAVGQEPLlfGRSFREN-I 576
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI--------------------SILGQPT--RQALQKNlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 577 AYgltrTPTMEEIT---------AVAMESGAHDFISGFPQGYDTEVGETG--------------NQLSGGQRQAVALARA 633
Cdd:PRK15056 81 AY----VPQSEEVDwsfpvlvedVVMMGRYGHMGWLRRAKKRDRQIVTAAlarvdmvefrhrqiGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERAHHILFLKeGSVCEQG 701
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLgSVTEFCDYTVMVK-GTVLASG 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
494-550 |
1.39e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQN--LYQPTGGKVLLDGELLVQYD 550
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE 77
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
508-705 |
2.24e-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: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 508 GKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDgellvqydhhylhtqvaavgqepllfgrsfRENIAYGltrtptme 587
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------------------------GITPVYK-------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 588 eitavamesgahdfisgfPQGYDtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPE 667
Cdd:cd03222 67 ------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 158262052 668 WASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQ 705
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQ 157
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
206-432 |
3.05e-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: 49.87 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 206 WLMCILTVASTALEFAGDGIYNITMGH-----MHS-RVhgEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDK 279
Cdd:cd18565 54 WLLGGLTVAAFLLESLFQYLSGVLWRRfaqrvQHDlRT--DTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 280 LNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAK-STQvaLE-ALSAMPTVRSF 357
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNAR--LEnNLSGIAVIKAF 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 358 ANEEGEAQKFRQKLEEMKPLNK---KEALAYVTEVWTMSVSGMLLkvgILYLGGQLVVRGAV------SSGNLVSFVLYQ 428
Cdd:cd18565 210 TAEDFERERVADASEEYRDANWraiRLRAAFFPVIRLVAGAGFVA---TFVVGGYWVLDGPPlftgtlTVGTLVTFLFYT 286
|
....
gi 158262052 429 LQFT 432
Cdd:cd18565 287 QRLL 290
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
479-651 |
3.35e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLyqptGGKVLLD---------------- 542
Cdd:PRK11147 3 LISIHGAWLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKST---LMKIL----NGEVLLDdgriiyeqdlivarlq 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 543 ----------------------GELLVQYdHHYLHTqvaaVGQEPllfgrsfRENIaygLTRTPTMEEITAVA----MES 596
Cdd:PRK11147 73 qdpprnvegtvydfvaegieeqAEYLKRY-HDISHL----VETDP-------SEKN---LNELAKLQEQLDHHnlwqLEN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 597 GAHDFISGFPQGYDTEVGEtgnqLSGG-QRQAvALARALIRKPRLLILDDATSALD 651
Cdd:PRK11147 138 RINEVLAQLGLDPDAALSS----LSGGwLRKA-ALGRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
485-707 |
3.93e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.42 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 485 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVA----ALLQNLYQPTGGKVLLDGELLVQYD----HHYLHT 556
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLLRLSprerRKLVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 557 QVAAVGQEPLL-------FGRSFRENIA-----------YGLTRTPTMEEITAVAMESgAHDFISGFPQgydtevgetgn 618
Cdd:PRK15093 90 NVSMIFQEPQScldpserVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD-HKDAMRSFPY----------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADKINVLYCGQT 237
|
250
....*....|
gi 158262052 698 CEQGTHLQLM 707
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
497-651 |
5.22e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELlvqydhhylhtQVAAVGQE-PLLF------- 568
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNW-----------QLAWVNQEtPALPqpaleyv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 569 ---GRSFRE-----------NIAYGL-TRTPTMEEITAVAMESGAHDFIS--GFPQgydTEVGETGNQLSGGQRQAVALA 631
Cdd:PRK10636 85 idgDREYRQleaqlhdanerNDGHAIaTIHGKLDAIDAWTIRSRAASLLHglGFSN---EQLERPVSDFSGGWRMRLNLA 161
|
170 180
....*....|....*....|
gi 158262052 632 RALIRKPRLLILDDATSALD 651
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD 181
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
180-446 |
9.07e-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: 48.26 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNitmgHMHSRVHGE----VFRAVLHQETGFFLK 255
Cdd:cd18588 20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFS----HTTNRIDAElgarLFRHLLRLPLSYFES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 256 NPTGSITSRVTEdtsnvCESISDklnlFLwyLGRGLCL----------LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 325
Cdd:cd18588 96 RQVGDTVARVRE-----LESIRQ----FL--TGSALTLvldlvfsvvfLAVMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 326 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEegeaQKFRQKLEEMkplnkkeaLA-YVTEV--------WTMSVSG 396
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVE----PQFQRRWEEL--------LArYVKASfktanlsnLASQIVQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 158262052 397 MLLK---VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQ 446
Cdd:cd18588 233 LIQKlttLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQ 285
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
586-651 |
9.78e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 9.78e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 586 MEEITAVAMESGAHDFISGFPQGYDTEVGETgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQVKAT-KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
620-698 |
1.33e-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: 48.28 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYespEWASRTVLLITQQLSLAE---RAHHILFLKEGS 696
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLIN---QLAQEGVAIIVVSSELAEvlgLSDRVLVIGEGK 480
|
..
gi 158262052 697 VC 698
Cdd:TIGR02633 481 LK 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
501-653 |
3.49e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 3.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVqydhhylhtqvaavgqepllfGRSFRENIAYGL 580
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEIN---------------------ALSTAQRLARGL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 581 TRTPTMEEITAVAMESG--------AHDFISGFPQ-GYDTEVGET-----------GNQ----LSGGQRQAVALARALIR 636
Cdd:PRK15439 341 VYLPEDRQSSGLYLDAPlawnvcalTHNRRGFWIKpARENAVLERyrralnikfnhAEQaartLSGGNQQKVLIAKCLEA 420
|
170
....*....|....*..
gi 158262052 637 KPRLLILDDATSALDAG 653
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVS 437
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
503-676 |
3.61e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 503 FTLY------PGKVTALVGPNGSGKSTVAALLQ-----NLYQPTGG-------------------KVLLDGELLV----Q 548
Cdd:PRK13409 88 FKLYglpipkEGKVTGILGPNGIGKTTAVKILSgelipNLGDYEEEpswdevlkrfrgtelqnyfKKLYNGEIKVvhkpQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 549 YdhhylhtqvaaVGQEPllfgRSFRENIAYGLTRTPTMEEITAVAMESGAHDFIsgfpqgyDTEVgetgNQLSGGQRQAV 628
Cdd:PRK13409 168 Y-----------VDLIP----KVFKGKVRELLKKVDERGKLDEVVERLGLENIL-------DRDI----SELSGGELQRV 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 158262052 629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLI 676
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVV 267
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
179-446 |
4.88e-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: 46.05 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18782 19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 259 GSITSRVTEdtsnvcesiSDKLNLFLwyLGRGLCL----------LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQS 328
Cdd:cd18782 99 GELSTRISE---------LDTIRGFL--TGTALTTlldvlfsviyIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 329 LAVKVQESLAKSTQVALEALSAMPTVRSFANEEgeaqKFRQKLEEmkplnkkEALAYVTEVWTMSVSGMLL--------- 399
Cdd:cd18782 168 QIRRRAEASAKTQSYLVESLTGIQTVKAQNAEL----KARWRWQN-------RYARSLGEGFKLTVLGTTSgslsqflnk 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 158262052 400 --KVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQ 446
Cdd:cd18782 237 lsSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQ 285
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
211-373 |
5.48e-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: 45.54 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 211 LTVASTALEFAGdGIYNITMGHMHSRV-HGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgr 289
Cdd:cd18606 44 LGVLQAIFLFLF-GLLLAYLGIRASKRlHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFL----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 290 glcLLAFMIWGSFYLTVVT----LLSLPLLFLLPRRLGKVYQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFanee 361
Cdd:cd18606 118 ---YTLSSIIGTFILIIIYlpwfAIALPPLLVLYYFIANYYRASSreLKRLESILRSFVYANfsESLSGLSTIRAY---- 190
|
170
....*....|..
gi 158262052 362 GEAQKFRQKLEE 373
Cdd:cd18606 191 GAQDRFIKKNEK 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
480-712 |
7.61e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqnlyqpTGGKVLLDGELLV----QYDHHYLh 555
Cdd:NF033858 2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AGARKIQQGRVEVlggdMADARHR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 556 tqvAAVGQE----PLLFGR------SFRENIA-----YGLTRTPTMEEITAVAMESGAHDFISGfPQGydtevgetgnQL 620
Cdd:NF033858 72 ---RAVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAAERRRRIDELLRATGLAPFADR-PAG----------KL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 621 SGGQRQAVALARALIRKPRLLILDDATSALD--AGNQ-------LRVQRllyespewASRTVLLITQQLSLAERAHHILF 691
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRRQfwelidrIRAER--------PGMSVLVATAYMEEAERFDWLVA 209
|
250 260
....*....|....*....|.
gi 158262052 692 LKEGSVCEQGTHLQLMERGGC 712
Cdd:NF033858 210 MDAGRVLATGTPAELLARTGA 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
503-664 |
7.96e-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: 45.93 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 503 FTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV------------------------LLDGELLV----Q 548
Cdd:COG1245 88 FRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkkLANGEIKVahkpQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 549 YdhhylhtqvaaVGQEPllfgRSFReniayGLTRtptmeEITAVAMESGAHDFIS---GFPQGYDTEVGEtgnqLSGGQR 625
Cdd:COG1245 168 Y-----------VDLIP----KVFK-----GTVR-----ELLEKVDERGKLDELAeklGLENILDRDISE----LSGGEL 218
|
170 180 190
....*....|....*....|....*....|....*....
gi 158262052 626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 664
Cdd:COG1245 219 QRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
497-662 |
9.29e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqnlyqpTGGkvlldgellvqydhhylHTQvaAVGQEPLLFGR------ 570
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGD-----------------HPQ--GYSNDLTLFGRrrgsge 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 ---SFRENIAYgLTRTPTME-----EITAVAMeSGAHDFISGFPQ----------------GYDTEVGETGNQ-LSGGQR 625
Cdd:PRK10938 330 tiwDIKKHIGY-VSSSLHLDyrvstSVRNVIL-SGFFDSIGIYQAvsdrqqklaqqwldilGIDKRTADAPFHsLSWGQQ 407
|
170 180 190
....*....|....*....|....*....|....*..
gi 158262052 626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLL 662
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
502-697 |
9.76e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 502 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVqydhhyLHTQVAAV-----------GQEPLLFGR 570
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 571 SFRENIAygltrtptmeeITAVAMESGAHDFISGfpqGYDTEVGET-----------GNQ----LSGGQRQAVALARALI 635
Cdd:PRK11288 347 SVADNIN-----------ISARRHHLRAGCLINN---RWEAENADRfirslniktpsREQlimnLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158262052 636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL----SLAERahhILFLKEGSV 697
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLpevlGVADR---IVVMREGRI 474
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
252-455 |
9.77e-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: 9.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 252 FFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAV 331
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLE--EMKPLNKKEALAY-VTEVWTMSVSGMLLKVGIlylGG 408
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGhfLTRALKHTRWNAKtFSAVNTITDLAPLLVIGF---AA 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158262052 409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18554 253 YLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
468-711 |
1.10e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.11 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 468 SGSLAPLNMKGLVKfqdvsfaypNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvAALLQNLYQPTGGKVLLDGELLV 547
Cdd:NF000106 8 NGARNAVEVRGLVK---------HFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 548 QyDHHYLHTQVAAvgQEPLLFGR----SFRENIaYGLTRTPTMEEITAVAMesgAHDFISGFpqGYDTEVGETGNQLSGG 623
Cdd:NF000106 78 A-NRRALRRTIG*--HRPVR*GRresfSGRENL-YMIGR*LDLSRKDARAR---ADELLERF--SLTEAAGRAAAKYSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 624 QRQAVALARALIRKPRLLILDDATSALDAgnqlRVQRLLYESPEWASR---TVLLITQQLSLAER-AHHILFLKEGSVCE 699
Cdd:NF000106 149 MRRRLDLAASMIGRPAVLYLDEPTTGLDP----RTRNEVWDEVRSMVRdgaTVLLTTQYMEEAEQlAHELTVIDRGRVIA 224
|
250
....*....|..
gi 158262052 700 QGTHLQLMERGG 711
Cdd:NF000106 225 DGKVDELKTKVG 236
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
346-455 |
1.77e-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: 44.02 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 346 EALSAMPTVRSFANEEGEAQKFRQkleemkpLNKKEALAYVTEVWTMSV-------SGMLLKVGILYLGGQLVVRGAVSS 418
Cdd:cd18546 183 ETLAGIRVVQAFRRERRNAERFAE-------LSDDYRDARLRAQRLVAIyfpgvelLGNLATAAVLLVGAWRVAAGTLTV 255
|
90 100 110
....*....|....*....|....*....|....*..
gi 158262052 419 GNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18546 256 GVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
182-449 |
2.46e-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: 43.75 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 182 PFFTGRITDwILQDKTAPSFARNMW---LMCILTVASTALEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18560 16 PLFLGRAVN-ALTLAKVKDLESAVTlilLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 259 GSITSRVTEDTsnvcESISDKLNLFLWYLGR-----GLCLLAFMIWGSFYLTVVTLLSLPllfllprrlgkVYQSLAVKV 333
Cdd:cd18560 95 GEVVRIMDRGT----ESANTLLSYLVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSVL-----------LYGVFTIKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 334 QESLAK-----------STQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVG 402
Cdd:cd18560 160 TEWRTKfrraankkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 158262052 403 ILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSV 449
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
619-653 |
3.47e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 3.47e-04
10 20 30
....*....|....*....|....*....|....*
gi 158262052 619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
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 ... |
345-435 |
5.88e-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: 42.45 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 345 LEALSAMPTVRSFANEEGEAQKFRQKLEEMkpLNKKEALAYVTeVWTMSVSGMLL---KVGILYLGGQLVVRGAVSSGNL 421
Cdd:cd18567 184 LETIRGIQTIKLFGREAEREARWLNLLVDA--INADIRLQRLQ-ILFSAANGLLFgleNILVIYLGALLVLDGEFTVGML 260
|
90
....*....|....
gi 158262052 422 VSFVLYQLQFTRAV 435
Cdd:cd18567 261 FAFLAYKDQFSSRA 274
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
252-455 |
6.72e-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: 6.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 252 FFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAV 331
Cdd:cd18540 92 YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYR 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEAL---AYVTEVWTMSVSGMLLkvgILYLGG 408
Cdd:cd18540 172 KVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARlsaLFLPIVLFLGSIATAL---VLWYGG 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 158262052 409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18540 249 ILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
494-662 |
1.16e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG-------ELLVQYDHHYLHTQVAAVGQEPL 566
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 567 LFGRSFRENIaygltrtptmEEITAVAMESGAHDFISgfpqgydtevgETGNQLSGGQRQAVALARALIRKPRLLILDDA 646
Cdd:PRK13541 92 KFWSEIYNSA----------ETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
170
....*....|....*.
gi 158262052 647 TSALDAGNQLRVQRLL 662
Cdd:PRK13541 151 ETNLSKENRDLLNNLI 166
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
476-681 |
1.49e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 476 MKGLVKFQDVSFAYP--NHPNVQV---------------LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 538
Cdd:PRK13545 1 MNYKVKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 539 VLLDGELLVQYDHHYLHTQVAAVgqepllfgrsfrENIAY-GLTRTPTMEEITAVAmesgahdfisgfPQGYD-TEVGET 616
Cdd:PRK13545 81 VDIKGSAALIAISSGLNGQLTGI------------ENIELkGLMMGLTKEKIKEII------------PEIIEfADIGKF 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158262052 617 GNQ----LSGGQRQAVALARALIRKPRLLILDDatsALDAGNQLRVQRLLYESPEWAS--RTVLLITQQLS 681
Cdd:PRK13545 137 IYQpvktYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNEFKEqgKTIFFISHSLS 204
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
608-664 |
2.48e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 2.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 158262052 608 GYDTEVGetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 664
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE 436
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
475-665 |
2.55e-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: 41.54 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 475 NMKGLVKFQDVSFAYPNHPNVQVlQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGELLVQyDHHYL 554
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 555 HTQVAAVGQ----EPLLFGRsfrENI-AYGLTRTPTMEEITAVAMESgahdfISGFpqGYDTEVGETGNQLSGGQRQAVA 629
Cdd:TIGR01257 2011 HQNMGYCPQfdaiDDLLTGR---EHLyLYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLS 2080
|
170 180 190
....*....|....*....|....*....|....*.
gi 158262052 630 LARALIRKPRLLILDDATSALDAgnqlRVQRLLYES 665
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDP----QARRMLWNT 2112
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
505-598 |
2.82e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 40.65 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 505 LYPGKVTALVGPNGSGKSTvaaLLQNL------------YQPTGGKVL-LDGELlvqyDHHYLHTQVAAVGQEPLLFGRS 571
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSF---LALQLaaavaaggpwlgRRVPPGKVLyLAAED----DRGELRRRLKALGADLGLPFAD 82
|
90 100 110
....*....|....*....|....*....|..
gi 158262052 572 FRENI-----AYGLTRTPTMEEITAVAMESGA 598
Cdd:COG3598 83 LDGRLrllslAGDLDDTDDLEALERAIEEEGP 114
|
|
| SRP54 |
pfam00448 |
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ... |
509-541 |
3.96e-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: 3.96e-03
10 20 30
....*....|....*....|....*....|...
gi 158262052 509 KVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL 541
Cdd:pfam00448 1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLL 33
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
488-523 |
5.09e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 39.36 E-value: 5.09e-03
10 20 30
....*....|....*....|....*....|....*..
gi 158262052 488 AYPNH-PNVQVLQGLTFTlypGKVTALVGPNGSGKST 523
Cdd:COG3910 19 AYPFNlPAVRNLEGLEFH---PPVTFFVGENGSGKST 52
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
494-532 |
5.86e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 38.63 E-value: 5.86e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 158262052 494 NVQVLQGLTFTLYPGkVTALVGPNGSGKST-VAALLQNLY 532
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 ... |
236-372 |
6.01e-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: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTllslPLL 315
Cdd:cd18605 76 RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLL----LPL 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158262052 316 FLLPRRLGKVYQSLA--VKVQESLAKS---TQVAlEALSAMPTVRSFANEEGEAQKFRQKLE 372
Cdd:cd18605 152 AFIYYRIQRYYRATSreLKRLNSVNLSplyTHFS-ETLKGLVTIRAFRKQERFLKEYLEKLE 212
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
503-524 |
6.18e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 6.18e-03
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
502-522 |
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
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
515-651 |
7.28e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 7.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158262052 515 GPNGSGKSTVAALLQNLYQPTGGKVLLDGELLvqyDHHYLHT--QVAAVGQEPLLFGR-SFRENIA-----YGLTRTPTM 586
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATrrRVGYMSQAFSLYGElTVRQNLElharlFHLPAAEIA 375
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158262052 587 EEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:NF033858 376 ARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| |
