|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-649 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 969.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 1 MRLPDLRPWTSLLLVDAALLW-LLQGPLGTLLP--QGLPGLWLEGTL------RLGGLWGLLKLRGLLGFVGTLLLPLCL 71
Cdd:TIGR00958 1 AALAYLLPWFSLLLVDWALLRdLLQGIFGLLLPfeKGLYVLWLEGTLrlgvlwLGALGILLNKAGGLLAAVKPLVAALCL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 72 ATPLTVSLRALVAGASRAPPARVASAPWSWLLVGYGAAGLSWSLWAVLSPPGAQEK--EQDQVNNKVLMWRLLKLSRPDL 149
Cdd:TIGR00958 81 ATPSLSSLRALAFWEALDPAVRVALGLWSWFVWSYGAALPAAALWAVLSSAGASEKeaEQGQSETADLLFRLLGLSGRDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 150 PLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQL 229
Cdd:TIGR00958 161 PWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 230 FSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKV 309
Cdd:TIGR00958 241 FRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 310 YNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQM 389
Cdd:TIGR00958 321 FGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 390 LMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLPSPGTLAPTTLQGVVK 469
Cdd:TIGR00958 401 LVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 470 FQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSV 549
Cdd:TIGR00958 481 FQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 550 GQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
650 660
....*....|....*....|
gi 73747917 630 LDEATSALDVQCEQAKTLWK 649
Cdd:TIGR00958 641 LDEATSALDAECEQLLQESR 660
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
155-443 |
1.31e-176 |
|
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: 503.41 E-value: 1.31e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLL 234
Cdd:cd18590 1 AFLFLTLAVICETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 235 RQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRH 314
Cdd:cd18590 81 QQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 315 QEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSC 394
Cdd:cd18590 161 QKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYC 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 73747917 395 GLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18590 241 GRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
133-651 |
2.01e-142 |
|
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: 2.01e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 133 NNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGG 212
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 213 CFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRL 292
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 293 TLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLE 372
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 373 RALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPN 452
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 453 LPSP-GTLAPTTLQGVVKFQDVSFAYPnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDE 531
Cdd:COG1132 324 IPDPpGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 532 KPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQ 611
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 73747917 612 KQRLAIARALVRDPRVLILDEATSALDVQCEQA--KTLWKFM 651
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALiqEALERLM 523
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
155-443 |
7.84e-116 |
|
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: 347.99 E-value: 7.84e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLL 234
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 235 RQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRH 314
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 315 QEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSC 394
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 73747917 395 GLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
457-645 |
2.07e-113 |
|
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: 339.45 E-value: 2.07e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 457 GTLAPTTLQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQ 536
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 537 YEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLA 616
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
|
170 180
....*....|....*....|....*....
gi 73747917 617 IARALVRDPRVLILDEATSALDVQCEQAK 645
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
141-644 |
2.22e-109 |
|
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: 341.68 E-value: 2.22e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 141 LLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSR 220
Cdd:TIGR02204 9 LWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGER 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 221 INLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHM 300
Cdd:TIGR02204 89 VVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 301 PFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVR 380
Cdd:TIGR02204 169 PLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 381 RVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLPSPGT-- 458
Cdd:TIGR02204 249 IVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHpk 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 459 LAPTTLQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE 538
Cdd:TIGR02204 329 TLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLD 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 539 HCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIA 618
Cdd:TIGR02204 409 PAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIA 488
|
490 500
....*....|....*....|....*.
gi 73747917 619 RALVRDPRVLILDEATSALDVQCEQA 644
Cdd:TIGR02204 489 RAILKDAPILLLDEATSALDAESEQL 514
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
118-644 |
3.39e-101 |
|
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: 324.09 E-value: 3.39e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 118 VLSPPGAQEKEQDQVNNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVLgetLIPHYSGRVID--ILGGDFDP-HAFASAIF 194
Cdd:COG2274 127 LLEPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLAL---ATPLFTQVVIDrvLPNQDLSTlWVLAIGLL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 195 FMCLFSFGSSLSagcRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTL---MSNWLplnANVL 271
Cdd:COG2274 204 LALLFEGLLRLL---RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRDVESIrefLTGSL---LTAL 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 272 LRSLVKVVGLyGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHE 351
Cdd:COG2274 278 LDLLFVLIFL-IVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 352 VCRYKEALEqcRQLYWRRDLER--ALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYI 429
Cdd:COG2274 357 RRRWENLLA--KYLNARFKLRRlsNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGL 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 430 YGDMLSNVGAAEKVFSYMDRQP-NLPSPGTLAPTTLQGVVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSG 508
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 509 KSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDF 588
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDF 593
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 73747917 589 IQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:COG2274 594 IEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAI 649
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
155-443 |
1.51e-97 |
|
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: 301.02 E-value: 1.51e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLL 234
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 235 RQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRH 314
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 315 QEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSC 394
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 73747917 395 GLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
140-644 |
3.10e-90 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 291.24 E-value: 3.10e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 140 RLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAfasaIFFMCLFSFGSSLSAGCRGGCFTYTMS 219
Cdd:TIGR02203 4 RLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSV----LWWVPLVVIGLAVLRGICSFVSTYLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 220 RINLR----IREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLL 295
Cdd:TIGR02203 80 WVSNKvvrdIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 296 SLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERAL 375
Cdd:TIGR02203 160 VVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 376 YL-LVRRVLHLGVQMLMLsCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDrQPNLP 454
Cdd:TIGR02203 240 SSpITQLIASLALAVVLF-IALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLD-SPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 455 SPGTLAPTTLQGVVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI 534
Cdd:TIGR02203 318 DTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 535 SQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYG-LQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQ 613
Cdd:TIGR02203 397 ADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQ 476
|
490 500 510
....*....|....*....|....*....|.
gi 73747917 614 RLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERL 507
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
155-443 |
9.35e-87 |
|
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: 273.03 E-value: 9.35e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLL 234
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 235 RQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRH 314
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 315 QEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSC 394
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 73747917 395 GLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
468-651 |
1.65e-77 |
|
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: 247.07 E-value: 1.65e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVV 547
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180
....*....|....*....|....*.
gi 73747917 628 LILDEATSALDVQCEQA--KTLWKFM 651
Cdd:cd03249 161 LLLDEATSALDAESEKLvqEALDRAM 186
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
120-644 |
1.14e-68 |
|
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: 235.10 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 120 SPPGAQEKEQDQVNNKVLMWRLLKLSRPDLPLLVAAFFFLVLAVL-GETLIPHYSGRVIDILGGDFDPHAFASAIFFMCL 198
Cdd:COG5265 2 PSARAMSAPAAPPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLlAAALALVVPPLLKDAIDALLSGAAALLVVPVGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 199 FSFG-----SSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELnSR-----LSSDTTLMS----NWL 264
Cdd:COG5265 82 LAYGllrllSVLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGL-SRdiergTKGIEFLLRfllfNIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 265 PLNANVLLRSLVkVVGLYGFMLSIsprLTLLSL-LHMPFTIAAEKvYNTRHQevlREIQDAVARAGQVvreAVGGL---Q 340
Cdd:COG5265 161 PTLLEIALVAGI-LLVKYDWWFAL---ITLVTVvLYIAFTVVVTE-WRTKFR---REMNEADSEANTR---AVDSLlnyE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 341 TVRSFGAEEHEVCRYKEALEQCRQlyWRRDLERALYLLvrrvlHLGvQMLMLSCGL--------QQMQDGELTQGSL--- 409
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYER--AAVKSQTSLALL-----NFG-QALIIALGLtammlmaaQGVVAGTMTVGDFvlv 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 410 ----------LSF--MIYQESVGSYVqtlvyiygDMlsnvgaaEKVFSYMDRQPNL---PSPGTLAPTtlQGVVKFQDVS 474
Cdd:COG5265 302 nayliqlyipLNFlgFVYREIRQALA--------DM-------ERMFDLLDQPPEVadaPDAPPLVVG--GGEVRFENVS 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 475 FAYpnRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPV 554
Cdd:COG5265 365 FGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTV 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 555 LFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEAT 634
Cdd:COG5265 443 LFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
570
....*....|
gi 73747917 635 SALDVQCEQA 644
Cdd:COG5265 523 SALDSRTERA 532
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
466-651 |
6.32e-64 |
|
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: 210.93 E-value: 6.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 466 GVVKFQDVSFAYpnRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQ 545
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 VVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDP 625
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180
....*....|....*....|....*...
gi 73747917 626 RVLILDEATSALDVQCEQA--KTLWKFM 651
Cdd:cd03254 159 KILILDEATSNIDTETEKLiqEALEKLM 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
468-644 |
6.63e-61 |
|
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: 202.85 E-value: 6.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVV 547
Cdd:cd03251 1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170
....*....|....*..
gi 73747917 628 LILDEATSALDVQCEQA 644
Cdd:cd03251 160 LILDEATSALDTESERL 176
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
140-644 |
5.19e-60 |
|
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: 210.38 E-value: 5.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 140 RLLKLSRPDLPLLVAAFFFLVLAVLGETLIPHYSGRVID-ILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTM 218
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAgLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 219 SRINLRIREQLFSSLLRQDLGFFQETKTGELnsrlssdTTLM-----------SNWLPlnanVLLRSLVKVVGLYGFMLS 287
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGEL-------ATLLtegvealdgyfARYLP----QLFLAALVPLLILVAVFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 288 ISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQlyw 367
Cdd:COG4988 156 LDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 368 rrdleRALyllvrRVL--------------HLGVQMLMLSCGLQqMQDGELTQGS-----LLSFMIYQE--SVGSYvqtl 426
Cdd:COG4988 233 -----RTM-----KVLrvaflssavleffaSLSIALVAVYIGFR-LLGGSLTLFAalfvlLLAPEFFLPlrDLGSF---- 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 427 vyiYGDMLSNVGAAEKVFSYMDRQPNLPSPGTLAPTTLQGV-VKFQDVSFAYPNRpdRPVLKGLTFTLRPGEVTALVGPN 505
Cdd:COG4988 298 ---YHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPsIELEDVSFSYPGG--RPALDGLSLTIPPGERVALVGPS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 506 GSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHA 585
Cdd:COG4988 373 GAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGL 452
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 586 DDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:COG4988 453 DEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAE 511
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
152-416 |
2.67e-58 |
|
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: 197.48 E-value: 2.67e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGC--RGGCFTYTMSRINLRIREQL 229
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSflQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 230 FSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKV 309
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 310 YNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQM 389
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260
....*....|....*....|....*..
gi 73747917 390 LMLSCGLQQMQDGELTQGSLLSFMIYQ 416
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLF 267
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
224-644 |
3.68e-58 |
|
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: 205.77 E-value: 3.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDT-TLmsnwlplnANVLLR-------SLVKVVGLYGFMLSISPRLTLL 295
Cdd:COG4987 89 DLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVdAL--------DNLYLRvllpllvALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 296 SLLHMPFTIAAEKVYNTRHQevlREIQDAVARAGQVVR----EAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDL 371
Cdd:COG4987 161 LALGLLLAGLLLPLLAARLG---RRAGRRLAAARAALRarltDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 372 ERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTqGSLL---------SFmiyqESVGSYVQTLVYIyGDMLSnvgAAEK 442
Cdd:COG4987 238 LSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLallvlaalaLF----EALAPLPAAAQHL-GRVRA---AARR 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 443 VFSYMDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNRPdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP 522
Cdd:COG4987 309 LNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 523 TGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGE 602
Cdd:COG4987 388 QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGE 467
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 73747917 603 KGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:COG4987 468 GGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQA 509
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
468-644 |
3.94e-58 |
|
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: 193.37 E-value: 3.94e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVV 547
Cdd:cd03228 1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSGSVRNNIayglqsceddkvmaaaqaahaddfiqemehgiytdvgekgsqLAAGQKQRLAIARALVRDPRV 627
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170
....*....|....*..
gi 73747917 628 LILDEATSALDVQCEQA 644
Cdd:cd03228 118 LILDEATSALDPETEAL 134
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
213-644 |
9.42e-58 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 204.87 E-value: 9.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 213 CFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNwlplNANVLLRSLVK----VVGLYGFMLSI 288
Cdd:PRK11176 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAS----SSSGALITVVRegasIIGLFIMMFYY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 289 SPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVaraGQVVREA---VGGLQTVRSFGAEEHEVCRYKEALEQCRQL 365
Cdd:PRK11176 164 SWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTM---GQVTTSAeqmLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 366 ywrrdleralyllvrrvlhlgvQMLMLSCglQQMQDGeLTQ--GSL-LSFMIYQESVGSYVQTL-----VYIYGDM---- 433
Cdd:PRK11176 241 ----------------------GMKMVSA--SSISDP-IIQliASLaLAFVLYAASFPSVMDTLtagtiTVVFSSMialm 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 434 -----LSNV--------GAAEKVFSYMDRQPNLPSpGTLAPTTLQGVVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTA 500
Cdd:PRK11176 296 rplksLTNVnaqfqrgmAACQTLFAILDLEQEKDE-GKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 501 LVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQ-SCEDDKVMAA 579
Cdd:PRK11176 374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTeQYSREQIEEA 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73747917 580 AQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:PRK11176 454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERA 518
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
468-644 |
6.11e-56 |
|
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: 189.75 E-value: 6.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVV 547
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170
....*....|....*..
gi 73747917 628 LILDEATSALDVQCEQA 644
Cdd:cd03253 159 LLLDEATSALDTHTERE 175
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
157-443 |
1.13e-55 |
|
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: 191.15 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 157 FFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQ 236
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 237 DLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQE 316
Cdd:cd18589 83 EIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 317 VLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLMLSCGL 396
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 73747917 397 QQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18589 243 QLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
152-443 |
1.10e-54 |
|
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: 188.53 E-value: 1.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFS 231
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 232 SLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYN 311
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 312 TRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLM 391
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 73747917 392 LSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
466-643 |
3.71e-54 |
|
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: 184.33 E-value: 3.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 466 GVVKFQDVSFAYPNRPdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQ 545
Cdd:cd03245 1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 VVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDP 625
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170
....*....|....*...
gi 73747917 626 RVLILDEATSALDVQCEQ 643
Cdd:cd03245 160 PILLLDEPTSAMDMNSEE 177
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
155-443 |
1.04e-52 |
|
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: 183.22 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDIL------GGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQ 228
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVtnhsgsGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 229 LFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEK 308
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 309 VYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQ 388
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 73747917 389 MLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
155-443 |
1.12e-52 |
|
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: 183.10 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFAS------AIFFMCLFSFGSSLSAGcRGGCFTYTMSRINLRIREQ 228
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGlslktfALALLGVFVVGAAANFG-RVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 229 LFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEK 308
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 309 VYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLlvrRVLHLGVQ 388
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFF---GSTGFSGN 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 73747917 389 MLMLSC---GLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18573 237 LSLLSVlyyGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
468-644 |
1.01e-49 |
|
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: 173.06 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYpnRPDRP-VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPR 626
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170
....*....|....*...
gi 73747917 627 VLILDEATSALDVQCEQA 644
Cdd:cd03252 159 ILIFDEATSALDYESEHA 176
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
224-644 |
5.24e-48 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 177.99 E-value: 5.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFT 303
Cdd:PRK10790 99 QLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAV 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 304 IAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFgaeeHEVCRYKEAL-EQCRQLYWRRdlERALYL---LV 379
Cdd:PRK10790 179 LVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQF----RQQARFGERMgEASRSHYMAR--MQTLRLdgfLL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 380 RRVLHLGVQMLMlsCGLQQM----QDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMD--RQPNL 453
Cdd:PRK10790 253 RPLLSLFSALIL--CGLLMLfgfsASGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDgpRQQYG 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 454 PSPGTLApttlQGVVKFQDVSFAYpnRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKP 533
Cdd:PRK10790 331 NDDRPLQ----SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRP 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 534 ISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGlQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQ 613
Cdd:PRK10790 405 LSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQ 483
|
410 420 430
....*....|....*....|....*....|.
gi 73747917 614 RLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQA 514
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
389-642 |
6.19e-48 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 177.46 E-value: 6.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 389 MLMLSCGLQQMQDGELTQGSLLSFMIY-QESVGSYVQTLVYIYGDMLSNVGAAEkVFSYMDRQPNL-PSPGTLAPTTLQG 466
Cdd:PRK13657 255 LAILVLGAALVQKGQLRVGEVVAFVGFaTLLIGRLDQVVAFINQVFMAAPKLEE-FFEVEDAVPDVrDPPGAIDLGRVKG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRpdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:PRK13657 334 AVEFDDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPR 626
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
250
....*....|....*.
gi 73747917 627 VLILDEATSALDVQCE 642
Cdd:PRK13657 492 ILILDEATSALDVETE 507
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
135-638 |
7.73e-46 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 173.22 E-value: 7.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 135 KVLMWRLLKLSRPDLplLVAAFFFLVLAVLGeTLIPHYSGrvidILGGDFDPHAFASAIFFMCLFSFGSSLSAGCrggcF 214
Cdd:TIGR03797 124 RDLLRFALRGARRDL--LAILAMGLLGTLLG-MLVPIATG----ILIGTAIPDADRSLLVQIALALLAAAVGAAA----F 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 215 TYTMSRINLRIREQLFSS--------LLRQDLGFFQETKTGELNSRLSSDTTLMSnwlpLNANVLLRSLVKVV-GL--YG 283
Cdd:TIGR03797 193 QLAQSLAVLRLETRMDASlqaavwdrLLRLPVSFFRQYSTGDLASRAMGISQIRR----ILSGSTLTTLLSGIfALlnLG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 284 FMLSISPRLTLLSLLHMPFTIA---AEKVYNTRHQEVLREIQDAVAraGQVVrEAVGGLQTVRSFGAEEHEVCRYKEALE 360
Cdd:TIGR03797 269 LMFYYSWKLALVAVALALVAIAvtlVLGLLQVRKERRLLELSGKIS--GLTV-QLINGISKLRVAGAENRAFARWAKLFS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 361 QCRQLYWRRDLERALYLLVRRVLHLGVQMLML-SCGLQQMQDGeLTQGSLLSFM----IYQESVGSYVQTLVyiygDMLS 435
Cdd:TIGR03797 346 RQRKLELSAQRIENLLTVFNAVLPVLTSAALFaAAISLLGGAG-LSLGSFLAFNtafgSFSGAVTQLSNTLI----SILA 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 436 NVGAAEKVFSYMDRQPNLPSpGTLAPTTLQGVVKFQDVSFAYpnRPDRP-VLKGLTFTLRPGEVTALVGPNGSGKSTVAA 514
Cdd:TIGR03797 421 VIPLWERAKPILEALPEVDE-AKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLR 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 515 LLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDkVMAAAQAAHADDFIQEMEH 594
Cdd:TIGR03797 498 LLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDE-AWEAARMAGLAEDIRAMPM 576
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 73747917 595 GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:TIGR03797 577 GMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
225-644 |
5.97e-45 |
|
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: 168.23 E-value: 5.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 225 IREQLFSSLLRQDLGFFQETKTGELNS----RLSSDTTLMSNWLPLNANVLLRSLVKVVglygFMLSISPRLTLLSLLHM 300
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATlaleGVEALDGYFARYLPQLVLAVIVPLAILA----AVFPQDWISGLILLLTA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 301 PFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQlywrRDLE--RALYL- 377
Cdd:TIGR02857 155 PLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRE----RTMRvlRIAFLs 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 378 -LVRRVL-HLGVQMLMLSCGLQqMQDGELT-QGSLLSFMIYQESVGSYVQtLVYIYGDMLSNVGAAEKVFSYMDRQPnLP 454
Cdd:TIGR02857 231 sAVLELFaTLSVALVAVYIGFR-LLAGDLDlATGLFVLLLAPEFYLPLRQ-LGAQYHARADGVAAAEALFAVLDAAP-RP 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 455 SPGTL-APTTLQGVVKFQDVSFAYPNRpdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKP 533
Cdd:TIGR02857 308 LAGKApVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 534 ISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQ 613
Cdd:TIGR02857 386 LADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQ 465
|
410 420 430
....*....|....*....|....*....|.
gi 73747917 614 RLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAE 496
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
155-443 |
7.50e-45 |
|
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: 161.50 E-value: 7.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRggcfTYTMSRINLR----IREQLF 230
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR----FYLVSWLGERvvadLRKAVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 231 SSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVY 310
Cdd:cd18575 77 AHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 311 NTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQML 390
Cdd:cd18575 157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 73747917 391 MLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18575 237 VLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
466-643 |
7.50e-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: 159.20 E-value: 7.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 466 GVVKFQDVSFAYpnRPD-RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHS 544
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSGSVRNNIAyGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRD 624
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170
....*....|....*....
gi 73747917 625 PRVLILDEATSALDVQCEQ 643
Cdd:cd03244 158 SKILVLDEATASVDPETDA 176
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
151-443 |
2.28e-43 |
|
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: 157.65 E-value: 2.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 151 LLVAAFFFLVLavlgetliPHYSGRVIDILGGDFDPHAFAS-AIFFMCLFSFGSSLSAGcRGGCFTYTMSRINLRIREQL 229
Cdd:cd18576 5 LLLSSAIGLVF--------PLLAGQLIDAALGGGDTASLNQiALLLLGLFLLQAVFSFF-RIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 230 FSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKV 309
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 310 YNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQM 389
Cdd:cd18576 156 FGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 73747917 390 LMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18576 236 AVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
220-644 |
1.31e-42 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 161.37 E-value: 1.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 220 RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWL-----PLNANVLLRSLVkvVGLYGFMLSISPRLTL 294
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYvrvivPAGVALVVGAAA--VAAIAVLSVPAALILA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 295 LSLLHMPFTIAAEKVYNTRHQEVLReiQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQcrqlyWRRDLERA 374
Cdd:TIGR02868 161 AGLLLAGFVAPLVSLRAARAAEQAL--ARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRE-----LTRAERRA 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 375 lyllvRRVLHLGVQMLMLSCGL----------QQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVF 444
Cdd:TIGR02868 234 -----AAATALGAALTLLAAGLavlgalwaggPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 445 SYMD-----RQPNLPSPGTLAPTTLQgvVKFQDVSFAYPnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL 519
Cdd:TIGR02868 309 EVLDaagpvAEGSAPAAGAVGLGKPT--LELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGL 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 520 YQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTD 599
Cdd:TIGR02868 385 LDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTV 464
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 73747917 600 VGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:TIGR02868 465 LGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
220-643 |
7.30e-42 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 159.88 E-value: 7.30e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 220 RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFM-LSISPRLTLLSLL 298
Cdd:PRK10789 66 QLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 299 HMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKE-ALEQCRQlywrrdleralYL 377
Cdd:PRK10789 146 PMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAAdAEDTGKK-----------NM 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 378 LVRRV-------LHLGVQM---LMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYM 447
Cdd:PRK10789 215 RVARIdarfdptIYIAIGManlLAIGGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAML 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 448 DRQPNLpSPGTLAPTTLQGVVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQV 527
Cdd:PRK10789 295 AEAPVV-KDGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 528 LLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQL 607
Cdd:PRK10789 373 RFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVML 452
|
410 420 430
....*....|....*....|....*....|....*.
gi 73747917 608 AAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQ 643
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEH 488
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
486-635 |
3.15e-41 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.02 E-value: 3.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSG-SVRNNI 564
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747917 565 AYGLQSCEDDKvmaAAQAAHADDFIQE--MEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:pfam00005 81 RLGLLLKGLSK---REKDARAEEALEKlgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
367-644 |
9.44e-41 |
|
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: 156.83 E-value: 9.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 367 WRRDLERALYLLVR------------RVLHLGVQMLMLSCG----LQqmqdGELTQGSLL--SFMI-------------- 414
Cdd:COG4618 220 WQRANARALALQARasdraggfsalsKFLRLLLQSAVLGLGaylvIQ----GEITPGAMIaaSILMgralapieqaiggw 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 415 --YQESVGSYvQTLvyiyGDMLSNVGAAEKVFSymdrqpnLPSPgtlapttlQGVVKFQDVSFAYPNRpDRPVLKGLTFT 492
Cdd:COG4618 296 kqFVSARQAY-RRL----NELLAAVPAEPERMP-------LPRP--------KGRLSVENLTVVPPGS-KRPILRGVSFS 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 493 LRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAyGLQSCE 572
Cdd:COG4618 355 LEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA-RFGDAD 433
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747917 573 DDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:COG4618 434 PEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAA 505
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
238-643 |
5.57e-40 |
|
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: 156.44 E-value: 5.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 238 LGFFQETKTGELNSRLSS--------DTTLMSNWLPLnanvllrSLVKVVGLygFMLSISPRLTLLSLLHMP----FTIA 305
Cdd:TIGR01193 244 MSFFSTRRTGEIVSRFTDassiidalASTILSLFLDM-------WILVIVGL--FLVRQNMLLFLLSLLSIPvyavIIIL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 306 AEKVYNTRHQEVLReiqdAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHL 385
Cdd:TIGR01193 315 FKRTFNKLNHDAMQ----ANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKL 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 386 GVQMLMLSCGLQQMQDGELTQGSLLSFmiyqesvgsyvQTLVYIYGDMLSNVgaaekvfsyMDRQPNLP----------- 454
Cdd:TIGR01193 391 ILNVVILWTGAYLVMRGKLTLGQLITF-----------NALLSYFLTPLENI---------INLQPKLQaarvannrlne 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 455 ----------SPGTLAPTTLQGVVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG 524
Cdd:TIGR01193 451 vylvdsefinKKKRTELNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARS 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 525 GQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQ-SCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEK 603
Cdd:TIGR01193 529 GEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEE 608
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 73747917 604 GSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQ 643
Cdd:TIGR01193 609 GSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEK 648
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
471-644 |
2.87e-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: 2.87e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVG 550
Cdd:cd03246 4 ENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 QEPVLFSGSVRNNIayglqsceddkvmaaaqaahaddfiqemehgiytdvgekgsqLAAGQKQRLAIARALVRDPRVLIL 630
Cdd:cd03246 83 QDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170
....*....|....
gi 73747917 631 DEATSALDVQCEQA 644
Cdd:cd03246 121 DEPNSHLDVEGERA 134
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
439-643 |
4.18e-36 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 143.43 E-value: 4.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 439 AAEKVFSYMDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNRPDrPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQN 518
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 519 LYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEmEHGIYT 598
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNA 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 73747917 599 DVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQ 643
Cdd:PRK11160 468 WLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER 512
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
152-416 |
6.44e-36 |
|
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: 136.78 E-value: 6.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPhafaSAIFFMCLFSFGSSLsagCRGGCF---TYTMSRINLRI--- 225
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDL----EALLLVPLAIIGLFL---LRGLASylqTYLMAYVGQRVvrd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 226 -REQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTI 304
Cdd:cd18552 74 lRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 305 AAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVrrvlh 384
Cdd:cd18552 154 LPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPL----- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 73747917 385 lgVQML-------MLSCGLQQMQDGELTQGSLLSF-----MIYQ 416
Cdd:cd18552 229 --MELLgaiaialVLWYGGYQVISGELTPGEFISFitallLLYQ 270
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
225-643 |
3.42e-35 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 143.25 E-value: 3.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 225 IREQLFSSLLRQDLGFFQETKT--GELNSRLSSDTTLMSNWLPLN----ANVLLRSLVKVVGLYGFMLSISPRLTLLSLL 298
Cdd:PTZ00265 901 MKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNivifTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFI 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 299 HMP-FTIAA---------EKVYNTRHQEVLREIQDAVARAGQ-VVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYW 367
Cdd:PTZ00265 981 FMRvFAIRArltankdveKKEINQPGTVFAYNSDDEIFKDPSfLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQK 1060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 368 RRDLERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELT----QGSLLSFMIyqesVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:PTZ00265 1061 RKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILvddfMKSLFTFLF----TGSYAGKLMSLKGDSENAKLSFEKY 1136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 444 FSYMDRQPNLP---SPGTLAPTT--LQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQN 518
Cdd:PTZ00265 1137 YPLIIRKSNIDvrdNGGIRIKNKndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMR 1216
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 519 LY------------QPTG------------------------------------------GQVLLDEKPISQYEHCYLHS 544
Cdd:PTZ00265 1217 FYdlkndhhivfknEHTNdmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRN 1296
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRD 624
Cdd:PTZ00265 1297 LFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLRE 1376
|
490
....*....|....*....
gi 73747917 625 PRVLILDEATSALDVQCEQ 643
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEK 1395
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
468-638 |
3.52e-35 |
|
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: 132.84 E-value: 3.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVV 547
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPV--LFSGSVRNNIAYGL--QSCEDDKVmaaaqaahaDDFIQEM--EHGIyTDVGEKG-SQLAAGQKQRLAIARA 620
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPenLGLPREEI---------RERVEEAleLVGL-EHLADRPpHELSGGQKQRVAIAGV 148
|
170
....*....|....*...
gi 73747917 621 LVRDPRVLILDEATSALD 638
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLD 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
469-638 |
1.18e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVS 548
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 VGQEPVLFSGSVRNNIAYGLQsceddkvmAAAQAAHADDFIQEMEH-GIYTDVGEKG-SQLAAGQKQRLAIARALVRDPR 626
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQ--------LRERKFDRERALELLERlGLPPDILDKPvERLSGGERQRLALIRALLLQPD 150
|
170
....*....|..
gi 73747917 627 VLILDEATSALD 638
Cdd:COG4619 151 VLLLDEPTSALD 162
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
142-451 |
1.92e-34 |
|
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: 133.35 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 142 LKLSRPDLPLLVAAFFFlvlAVLGETLIPHYS---GRVIDILGGDFDPHAFASAIFFMCLF---SFGSSLSAGCRGGCFT 215
Cdd:cd18578 1 LKLNKPEWPLLLLGLIG---AIIAGAVFPVFAilfSKLISVFSLPDDDELRSEANFWALMFlvlAIVAGIAYFLQGYLFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 216 YTMSRINLRIREQLFSSLLRQDLGFFQETK--TGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLT 293
Cdd:cd18578 78 IAGERLTRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 294 LLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLER 373
Cdd:cd18578 158 LVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALIS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 374 ALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQG------SLLSFMIyqESVGsyvQTLVYIyGDMLSNVGAAEKVFSYM 447
Cdd:cd18578 238 GLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEqffivfMALIFGA--QSAG---QAFSFA-PDIAKAKAAAARIFRLL 311
|
....
gi 73747917 448 DRQP 451
Cdd:cd18578 312 DRKP 315
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
469-638 |
2.46e-33 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 126.81 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVS 548
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 VGQEP--VLFSGSVRNNIAYGL-QSCEDDKVMAAAQAAHADDF-IQE-MEHGIYTdvgekgsqLAAGQKQRLAIARALVR 623
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLeNLGLPEEEIEERVEEALELVgLEGlRDRSPFT--------LSGGQKQRVAIAGVLAM 151
|
170
....*....|....*
gi 73747917 624 DPRVLILDEATSALD 638
Cdd:cd03225 152 DPDILLLDEPTAGLD 166
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
152-415 |
9.59e-33 |
|
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: 127.93 E-value: 9.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFS 231
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 232 SLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYN 311
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 312 TRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHLGVQMLM 391
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260
....*....|....*....|....
gi 73747917 392 LSCGLQQMQDGELTQGSLLSFMIY 415
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISY 264
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
469-639 |
1.45e-32 |
|
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: 125.74 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcYLHSQVVS 548
Cdd:COG4555 3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 VGQEPVLFSG-SVRNNI-----AYGLQSCEDDKVMaaaqaahaDDFIQEMEHGIYTDvgEKGSQLAAGQKQRLAIARALV 622
Cdd:COG4555 79 LPDERGLYDRlTVRENIryfaeLYGLFDEELKKRI--------EELIELLGLEEFLD--RRVGELSTGMKKKVALARALV 148
|
170
....*....|....*..
gi 73747917 623 RDPRVLILDEATSALDV 639
Cdd:COG4555 149 HDPKVLLLDEPTNGLDV 165
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-639 |
2.40e-32 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 131.18 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 438 GAAEKVFSYMDR---QPNLPSPGTLAPTTLQG---VVKFQDVSFAYPNRP--DRPVLKGLTFTLRPGEVTALVGPNGSGK 509
Cdd:COG1123 225 GPPEEILAAPQAlaaVPRLGAARGRAAPAAAAaepLLEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 510 STVAALLQNLYQPTGGQVLLDEKPISQYEHC---YLHSQVVSVGQEPV--LFSG-SVRNNIAYGLqsceddKVMAAAQAA 583
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQDPYssLNPRmTVGDIIAEPL------RLHGLLSRA 378
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 584 HADDFIQEM--EHGIYTDVGEK-GSQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG1123 379 ERRERVAELleRVGLPPDLADRyPHELSGGQRQRVAIARALALEPKLLILDEPTSALDV 437
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
470-644 |
4.43e-32 |
|
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: 122.42 E-value: 4.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 470 FQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCyLHSQVVSV 549
Cdd:cd03247 3 INNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 550 GQEPVLFSGSVRNNIayglqsceddkvmaaaqaahaddfiqemehgiytdvgekGSQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:cd03247 81 NQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170
....*....|....*
gi 73747917 630 LDEATSALDVQCEQA 644
Cdd:cd03247 122 LDEPTVGLDPITERQ 136
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
468-638 |
4.86e-32 |
|
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: 123.83 E-value: 4.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY-----QPTGGQVLLDEKPI--SQYEHC 540
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 541 YLHSQVVSVGQEPVLFSGSVRNNIAYGLqsceddKVMAAAQAAHADDFIQEM--EHGIYTDVGEK--GSQLAAGQKQRLA 616
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGL------RLHGIKLKEELDERVEEAlrKAALWDEVKDRlhALGLSGGQQQRLC 151
|
170 180
....*....|....*....|..
gi 73747917 617 IARALVRDPRVLILDEATSALD 638
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALD 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
468-640 |
6.13e-32 |
|
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: 123.35 E-value: 6.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPDR-PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcyLHSQV 546
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEPVLFS-GSVRNNIAYGLqscEDDKVMAAAQAAHADDFIQEmehgiytdVGEKG------SQLAAGQKQRLAIAR 619
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGL---ELQGVPKAEARERAEELLEL--------VGLSGfenaypHQLSGGMRQRVALAR 144
|
170 180
....*....|....*....|.
gi 73747917 620 ALVRDPRVLILDEATSALDVQ 640
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAL 165
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
180-642 |
6.25e-32 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 132.85 E-value: 6.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 180 LGGDFDPHAFASAI--FFMCLFSFGSSLsagcrggCFTYTMSRINLRIREQLFSSLLRQDlGFFQETKTGelnSRLSSDT 257
Cdd:PTZ00265 92 LGENVNDIIFSLVLigIFQFILSFISSF-------CMDVVTTKILKTLKLEFLKSVFYQD-GQFHDNNPG---SKLTSDL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 258 TLMSNwlPLNANVLLRSLV------KVVGLYGFMLSISPRLTL-----LSLLHMPFTIAAEKVYNTRHQEVLREiqdavA 326
Cdd:PTZ00265 161 DFYLE--QVNAGIGTKFITiftyasAFLGLYIWSLFKNARLTLcitcvFPLIYICGVICNKKVKINKKTSLLYN-----N 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 327 RAGQVVREAVGGLQTVRSFGAEEHEVCRYKEAleqcRQLYWRRDLERALYllvrRVLHLGV----------------QML 390
Cdd:PTZ00265 234 NTMSIIEEALVGIRTVVSYCGEKTILKKFNLS----EKLYSKYILKANFM----ESLHIGMingfilasyafgfwygTRI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 391 MLSCGLQQMQDGELTQGSLLSFMIyQESVGSYVQTLVYI-YGDMLSNVGAAEKVFSYMDRQPNLPS--PGTLAPTTLQgv 467
Cdd:PTZ00265 306 IISDLSNQQPNNDFHGGSVISILL-GVLISMFMLTIILPnITEYMKSLEATNSLYEIINRKPLVENndDGKKLKDIKK-- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLL-DEKPISQYEHCYLHSQV 546
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEPVLFSGSVRNNIAYGL---------------------------------------------------------Q 569
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyQ 542
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747917 570 SCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCE 642
Cdd:PTZ00265 543 TIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
468-640 |
9.66e-32 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 122.19 E-value: 9.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPDR--PVLKGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLyQPTGGQVlldekpisqyehcYLHS 544
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSGSVRNNIAYG-----------LQSC--EDDkvmaaaqaahaddfIQEMEHGIYTDVGEKGSQLAAGQ 611
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGkpfdeeryekvIKACalEPD--------------LEILPDGDLTEIGEKGINLSGGQ 132
|
170 180
....*....|....*....|....*....
gi 73747917 612 KQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAH 161
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
467-639 |
1.05e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 123.62 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:COG1120 1 MLEAENLSVGYG---GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEPVL-FSGSVRNNIAYGLQ---------SCEDDKVmaaaqaahaddfIQE-MEhgiYTDVGEKG----SQLAAGQ 611
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRYphlglfgrpSAEDREA------------VEEaLE---RTGLEHLAdrpvDELSGGE 142
|
170 180
....*....|....*....|....*...
gi 73747917 612 KQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
437-644 |
1.22e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 129.96 E-value: 1.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 437 VGAAEKVFSYMDRQPNLPSPGTLAPTTLQGV-VKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKST-VAA 514
Cdd:PRK11174 318 VGAAESLVTFLETPLAHPQQGEKELASNDPVtIEAEDLEILSPD--GKTLAGPLNFTLPAGQRIALVGPSGAGKTSlLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 515 LLQNL-YQptgGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEME 593
Cdd:PRK11174 396 LLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLP 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 73747917 594 HGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:PRK11174 473 QGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
462-640 |
1.31e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.66 E-value: 1.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 462 TTLQGVVKFQDVSFAYPNRP-DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehc 540
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 541 yLHSQVVSVGQEPVLFs-gSVRNNIAYGLqscEDDKVMAAAQAAHADDFIQEmehgiytdVGEKG------SQLAAGQKQ 613
Cdd:COG1116 78 -PGPDRGVVFQEPALLpwlTVLDNVALGL---ELRGVPKAERRERARELLEL--------VGLAGfedaypHQLSGGMRQ 145
|
170 180
....*....|....*....|....*..
gi 73747917 614 RLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDAL 172
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
224-642 |
1.81e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 131.64 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPrLTLLSLlhMPFT 303
Cdd:PLN03232 984 RLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVST-ISLWAI--MPLL 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 304 I---AAEKVYNTRHQEVLReiQDAVARAGQVVR--EAVGGLQTVRSFGA-EEHEVCRYKEALEQCRQLYWRRDLERALYL 377
Cdd:PLN03232 1061 IlfyAAYLYYQSTSREVRR--LDSVTRSPIYAQfgEALNGLSSIRAYKAyDRMAKINGKSMDNNIRFTLANTSSNRWLTI 1138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 378 lvrRVLHLGVQMLMLSCGLQQMQDGEL--------TQGSLLSfmiYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDr 449
Cdd:PLN03232 1139 ---RLETLGGVMIWLTATFAVLRNGNAenqagfasTMGLLLS---YTLNITTLLSGVLRQASKAENSLNSVERVGNYID- 1211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 450 qpnLPSPGT--------LAPTTLQGVVKFQDVSFAY-PNRPdrPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY 520
Cdd:PLN03232 1212 ---LPSEATaiiennrpVSGWPSRGSIKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV 1286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 521 QPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAyGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDV 600
Cdd:PLN03232 1287 ELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEV 1365
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 73747917 601 GEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCE 642
Cdd:PLN03232 1366 SEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD 1407
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
174-413 |
2.02e-31 |
|
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: 124.12 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 174 GRVIDILG----GDFDPHAFASAI----FFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETK 245
Cdd:cd18577 23 GDLFDAFTdfgsGESSPDEFLDDVnkyaLYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 246 TGELNSRLSSDTTL----MSNWLPLnanvLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREI 321
Cdd:cd18577 103 AGELTSRLTSDTNLiqdgIGEKLGL----LIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 322 QDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERAlyllvrrvLHLGVQMLMLSC------- 394
Cdd:cd18577 179 QEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSG--------LGLGLLFFIIFAmyalafw 250
|
250 260
....*....|....*....|.
gi 73747917 395 -GLQQMQDGELTQGSLLS-FM 413
Cdd:cd18577 251 yGSRLVRDGEISPGDVLTvFF 271
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
468-651 |
5.12e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 121.32 E-value: 5.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyEHCYLHSQVV 547
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSG-SVRNNI-----AYGLQSCEDDKvmaaaqaaHADDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARAL 621
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARE--------RIDELLELF--GLTDAADRKVGTLSGGMKQRLGLALAL 146
|
170 180 190
....*....|....*....|....*....|
gi 73747917 622 VRDPRVLILDEATSALDVQceQAKTLWKFM 651
Cdd:COG1131 147 LHDPELLILDEPTSGLDPE--ARRELWELL 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
224-642 |
1.97e-30 |
|
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: 128.14 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSL-LHMPF 302
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPpLGLLY 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 303 TIAaEKVYNTRHQEVLReiQDAVARAG--QVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRrdleralYLLVR 380
Cdd:TIGR00957 1119 FFV-QRFYVASSRQLKR--LESVSRSPvySHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYP-------SIVAN 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 381 RVLHLGVQ-----MLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVFSYMDRQPNLP- 454
Cdd:TIGR00957 1189 RWLAVRLEcvgncIVLFAALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPw 1268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 455 -SPGTLAPTTL--QGVVKFQDVSFAYpnRPDRP-VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLD 530
Cdd:TIGR00957 1269 qIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIID 1346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 531 EKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAyGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAG 610
Cdd:TIGR00957 1347 GLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVG 1425
|
410 420 430
....*....|....*....|....*....|..
gi 73747917 611 QKQRLAIARALVRDPRVLILDEATSALDVQCE 642
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
467-639 |
5.80e-30 |
|
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: 117.99 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPD-RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI---SQYEHCYL 542
Cdd:cd03257 1 LLEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 HSQVVSVGQE------PVLfsgSVRNNIAYGLQSCEDDKVMAAAQAAHADDFiqeMEHGIYTDVGEK-GSQLAAGQKQRL 615
Cdd:cd03257 81 RKEIQMVFQDpmsslnPRM---TIGEQIAEPLRIHGKLSKKEARKEAVLLLL---VGVGLPEEVLNRyPHELSGGQRQRV 154
|
170 180
....*....|....*....|....
gi 73747917 616 AIARALVRDPRVLILDEATSALDV 639
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDV 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
466-640 |
7.07e-30 |
|
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: 117.13 E-value: 7.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 466 GVVKFQDVSFAY-PNRPdrPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHS 544
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSGSVRNNI-AYGLQSceDDKVMAAAQaahaddfiqemehgiytdVGEKGSQLAAGQKQRLAIARALVR 623
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170
....*....|....*..
gi 73747917 624 DPRVLILDEATSALDVQ 640
Cdd:cd03369 143 RPRVLVLDEATASIDYA 159
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
469-640 |
9.73e-30 |
|
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: 115.03 E-value: 9.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcylhsqvvs 548
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 vgqepvLFSGSVRNNIAYglqsceddkvmaaaqaahaddfiqemehgiytdvgekGSQLAAGQKQRLAIARALVRDPRVL 628
Cdd:cd00267 66 ------LPLEELRRRIGY-------------------------------------VPQLSGGQRQRVALARALLLNPDLL 102
|
170
....*....|..
gi 73747917 629 ILDEATSALDVQ 640
Cdd:cd00267 103 LLDEPTSGLDPA 114
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
480-640 |
2.82e-29 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 115.27 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYlHSQVVSVGQEPVLFSG- 558
Cdd:COG4133 12 RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKPEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIA-----YGLQSCEDDkvmaaaqaahADDFIQEMEHGIYTDVgeKGSQLAAGQKQRLAIARALVRDPRVLILDEA 633
Cdd:COG4133 91 TVRENLRfwaalYGLRADREA----------IDEALEAVGLAGLADL--PVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
....*..
gi 73747917 634 TSALDVQ 640
Cdd:COG4133 159 FTALDAA 165
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
471-639 |
2.96e-29 |
|
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: 114.45 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcylhsqvvsvg 550
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSP----------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 QEpvlfsgsVRNNIAYGLQSCEDDKvmaaaqaahaddfIQEMEHGIYTdvgekgsQLAAGQKQRLAIARALVRDPRVLIL 630
Cdd:cd03214 69 KE-------LARKIAYVPQALELLG-------------LAHLADRPFN-------ELSGGERQRVLLARALAQEPPILLL 121
|
....*....
gi 73747917 631 DEATSALDV 639
Cdd:cd03214 122 DEPTSHLDI 130
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
224-639 |
3.84e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 124.47 E-value: 3.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRS---LVKVVGLYGFMLSISprltLLSLlhM 300
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLGQifqLLSTFVLIGIVSTIS----LWAI--M 1060
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 301 PFTIAAEKVYnTRHQEVLREIQ--DAVARAGQVVR--EAVGGLQTVRSFGAEEhevcRYKEALEQCRQLYWRRDLER--A 374
Cdd:PLN03130 1061 PLLVLFYGAY-LYYQSTAREVKrlDSITRSPVYAQfgEALNGLSTIRAYKAYD----RMAEINGRSMDNNIRFTLVNmsS 1135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 375 LYLLVRRVLHLGVQMLMLSCGLQQMQDGEL--------TQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVgaaEKVFSY 446
Cdd:PLN03130 1136 NRWLAIRLETLGGLMIWLTASFAVMQNGRAenqaafasTMGLLLSYALNITSLLTAVLRLASLAENSLNAV---ERVGTY 1212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 447 MDRQP--------NLPSPGTlaPTTlqGVVKFQDVSFAY-PNRPdrPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQ 517
Cdd:PLN03130 1213 IDLPSeaplvienNRPPPGW--PSS--GSIKFEDVVLRYrPELP--PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALF 1286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 518 NLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAyGLQSCEDDKVMAAAQAAHADDFIQEMEHGIY 597
Cdd:PLN03130 1287 RIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRRNSLGLD 1365
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 73747917 598 TDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PLN03130 1366 AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
468-651 |
4.67e-29 |
|
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: 113.65 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHsQVV 547
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSG-SVRNNIAYglqsceddkvmaaaqaahaddfiqemehgiytdvgekgSQlaaGQKQRLAIARALVRDPR 626
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKL--------------------------------------SG---GMKQRLALAQALLHDPE 115
|
170 180
....*....|....*....|....*
gi 73747917 627 VLILDEATSALDVqcEQAKTLWKFM 651
Cdd:cd03230 116 LLILDEPTSGLDP--ESRREFWELL 138
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
472-638 |
5.33e-29 |
|
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: 114.66 E-value: 5.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 472 DVSFAYPNRPDrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEH---CYLhsqvvs 548
Cdd:cd03226 4 NISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksIGY------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 VGQEP--VLFSGSVRNNIAYGLQSCEDDKvmaaaqaAHADDFIQEMEhgIYTDVGEKGSQLAAGQKQRLAIARALVRDPR 626
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKELDAGN-------EQAETVLKDLD--LYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170
....*....|..
gi 73747917 627 VLILDEATSALD 638
Cdd:cd03226 147 LLIFDEPTSGLD 158
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
465-638 |
1.20e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 465 QGVVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHS 544
Cdd:PRK13632 5 SVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEP-VLFSGS-VRNNIAYGLQS-CEDDKVMaaaqaahaDDFIQEMEH--GIyTDVGEKGSQ-LAAGQKQRLAIA 618
Cdd:PRK13632 84 KIGIIFQNPdNQFIGAtVEDDIAFGLENkKVPPKKM--------KDIIDDLAKkvGM-EDYLDKEPQnLSGGQKQRVAIA 154
|
170 180
....*....|....*....|
gi 73747917 619 RALVRDPRVLILDEATSALD 638
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLD 174
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
471-639 |
2.00e-28 |
|
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: 114.13 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPNRPDR-PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSV 549
Cdd:COG1124 5 RNLSVSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 550 GQEPvlfSGS------VRNNIAYGLQSCEDDKVmaaaqaahaDDFIQEM--EHGIYTDVGEK-GSQLAAGQKQRLAIARA 620
Cdd:COG1124 85 FQDP---YASlhprhtVDRILAEPLRIHGLPDR---------EERIAELleQVGLPPSFLDRyPHQLSGGQRQRVAIARA 152
|
170
....*....|....*....
gi 73747917 621 LVRDPRVLILDEATSALDV 639
Cdd:COG1124 153 LILEPELLLLDEPTSALDV 171
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
468-640 |
4.17e-28 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 112.23 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqyeHCYLHSQVV 547
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT---GVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 S-VGQEPVLFSG-SVRNNIAYGLqsceddKVMAAAQAAHADDFIQEMEH-GIYTDVGEKGSQLAAGQKQRLAIARALVRD 624
Cdd:cd03259 75 GmVFQDYALFPHlTVAENIAFGL------KLRGVPKAEIRARVRELLELvGLEGLLNRYPHELSGGQQQRVALARALARE 148
|
170
....*....|....*.
gi 73747917 625 PRVLILDEATSALDVQ 640
Cdd:cd03259 149 PSLLLLDEPLSALDAK 164
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
159-414 |
4.79e-28 |
|
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: 114.56 E-value: 4.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 159 LVLAVLGeTLIPHYSGRVIDIL-------GGDFDPHAFASAIFFMCLFSFGSSLSAgcrggCFTYTMS----RINLRIRE 227
Cdd:cd18574 6 LAAALVN-IQIPLLLGDLVNVIsrslketNGDFIEDLKKPALKLLGLYLLQSLLTF-----AYISLLSvvgeRVAARLRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 228 QLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAE 307
Cdd:cd18574 80 DLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 308 KVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLywRRDLER-----------ALY 376
Cdd:cd18574 160 TLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKL--NEKLGLgigifqglsnlALN 237
|
250 260 270
....*....|....*....|....*....|....*...
gi 73747917 377 LLVrrvlhLGVqmlmLSCGLQQMQDGELTQGSLLSFMI 414
Cdd:cd18574 238 GIV-----LGV----LYYGGSLVSRGELTAGDLMSFLV 266
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
468-639 |
6.64e-28 |
|
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: 110.35 E-value: 6.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE-HCYLHSQV 546
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VS-VGQEPVLFSG-SVRNNIAYGlqsceddkvmaaaqaahaddfiqemehgiytdvgekgsqLAAGQKQRLAIARALVRD 624
Cdd:cd03229 78 IGmVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170
....*....|....*
gi 73747917 625 PRVLILDEATSALDV 639
Cdd:cd03229 119 PDVLLLDEPTSALDP 133
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
464-651 |
6.68e-28 |
|
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: 109.83 E-value: 6.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 464 LQGVVKfqdvSFaypnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqyehcylh 543
Cdd:cd03216 3 LRGITK----RF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 sqvvsvgqepvlfSGSVRnniayglqsceddkvmaaaqaahaddfiQEMEHGIYTdVgekgSQLAAGQKQRLAIARALVR 623
Cdd:cd03216 66 -------------FASPR----------------------------DARRAGIAM-V----YQLSVGERQMVEIARALAR 99
|
170 180
....*....|....*....|....*...
gi 73747917 624 DPRVLILDEATSALDVQceQAKTLWKFM 651
Cdd:cd03216 100 NARLLILDEPTAALTPA--EVERLFKVI 125
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
152-443 |
9.81e-28 |
|
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: 113.35 E-value: 9.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRggcfTYTMSRINLRI----RE 227
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLR----RYLAGRLSLGVehdlRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 228 QLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWL---PLnanvLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTI 304
Cdd:cd18543 77 DLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLafgPF----LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 305 AAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLH 384
Cdd:cd18543 153 LVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 385 LGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18543 233 ELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
468-638 |
2.88e-27 |
|
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: 111.37 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCY-LHSQV 546
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEP--VLFSGSVRNNIAYGLqscEDDKVMAaaqaahaddfiQEMEHGIY---TDVGEKG------SQLAAGQKQRL 615
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGL---ENLGVPR-----------EEMRKRVDealKLVGMEDfrdrepHLLSGGQKQRV 145
|
170 180
....*....|....*....|...
gi 73747917 616 AIARALVRDPRVLILDEATSALD 638
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLD 168
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
152-415 |
2.28e-26 |
|
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: 109.40 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVID--ILGGDFDPHAFASAIFFMCLFSFGSSLSagcrGGCFTYTMSRINLRI---- 225
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyIVPGQGDLQGLLLLALLYLGLLLLSFLL----QYLQTYLLQKLGQRIiydl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 226 REQLFSSLLRQDLGFFQETKTGELNSRLSSDT----TLMSNWLPlnanVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMP 301
Cdd:cd18544 77 RRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTealnELFTSGLV----TLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 302 FTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRrdlERALYLLVRR 381
Cdd:cd18544 153 LLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLK---SIKLFALFRP 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 73747917 382 VLHLgVQMLMLSC----GLQQMQDGELTQGSLLSFMIY 415
Cdd:cd18544 230 LVEL-LSSLALALvlwyGGGQVLSGAVTLGVLYAFIQY 266
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
467-644 |
2.76e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 107.87 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKST-VAALLqNLYQPTGGQVLLDEKPISQYEHC--YLh 543
Cdd:COG1121 6 AIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRRigYV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQE-PVlfsgSVRNNIAYGLQScedDKVMAAAQAAHADDFIQE------MEHGIYTDVGEkgsqLAAGQKQRLA 616
Cdd:COG1121 81 PQRAEVDWDfPI----TVRDVVLMGRYG---RRGLFRRPSRADREAVDEalervgLEDLADRPIGE----LSGGQQQRVL 149
|
170 180
....*....|....*....|....*...
gi 73747917 617 IARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEA 177
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
468-640 |
3.07e-26 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 107.32 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQ---YEHcylhs 544
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlppHKR----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSG-SVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHGiytdvGEKGSQLAAGQKQRLAIARALVR 623
Cdd:cd03300 73 PVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYA-----NRKPSQLSGGQQQRVAIARALVN 147
|
170
....*....|....*..
gi 73747917 624 DPRVLILDEATSALDVQ 640
Cdd:cd03300 148 EPKVLLLDEPLGALDLK 164
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
467-639 |
4.05e-26 |
|
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: 112.69 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG---GQVLLDEKPISQYEHCYLH 543
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQEP--VLFSGSVRNNIAYGLQ-SCEDDKVMAAAQAAHADDFiqemehGIYTDVGEKGSQLAAGQKQRLAIARA 620
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAV------GLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170
....*....|....*....
gi 73747917 621 LVRDPRVLILDEATSALDV 639
Cdd:COG1123 157 LALDPDLLIADEPTTALDV 175
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
467-638 |
9.78e-26 |
|
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: 106.13 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPDR-PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQ 545
Cdd:cd03258 1 MIELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 VVSVG---QEPVLFSG-SVRNNIAYGLQSCEDDKvmaaaqaahadDFIQEMEHGIYTDVG--EKG----SQLAAGQKQRL 615
Cdd:cd03258 81 RRRIGmifQHFNLLSSrTVFENVALPLEIAGVPK-----------AEIEERVLELLELVGleDKAdaypAQLSGGQKQRV 149
|
170 180
....*....|....*....|...
gi 73747917 616 AIARALVRDPRVLILDEATSALD 638
Cdd:cd03258 150 GIARALANNPKVLLCDEATSALD 172
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
468-640 |
1.21e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 108.65 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcylhsqvV 547
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG----------L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPV--------LFSG-SVRNNIAYGLQsceddkvMAAAQAAHADDFIQEM-------EHGiytdvGEKGSQLAAGQ 611
Cdd:COG3842 73 PPEKRNVgmvfqdyaLFPHlTVAENVAFGLR-------MRGVPKAEIRARVAELlelvgleGLA-----DRYPHQLSGGQ 140
|
170 180
....*....|....*....|....*....
gi 73747917 612 KQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAK 169
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
463-638 |
1.76e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 463 TLQGVVKfqdvSFaypnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyeHCYL 542
Cdd:COG1129 6 EMRGISK----SF-----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF--RSPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 HSQ---VVSVGQEPVLFSG-SVRNNIAYGLQSCE----DDKVMAAAQAAHADDFiqemehGIYTDVGEKGSQLAAGQKQR 614
Cdd:COG1129 75 DAQaagIAIIHQELNLVPNlSVAENIFLGREPRRggliDWRAMRRRARELLARL------GLDIDPDTPVGDLSVAQQQL 148
|
170 180
....*....|....*....|....
gi 73747917 615 LAIARALVRDPRVLILDEATSALD 638
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLT 172
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
152-415 |
2.45e-25 |
|
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: 106.36 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPhaFASAIFFMCLFSFGSSLSAGCrggcfTYTMSRIN----LRIRE 227
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSS--GGLLALLVALFLLQAVLSALS-----SYLLGRTGervvLDLRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 228 QLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAE 307
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 308 KVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERAlylLVRRVLHLGV 387
Cdd:cd18551 154 LPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEA---LIGPLMGLAV 230
|
250 260 270
....*....|....*....|....*....|.
gi 73747917 388 QMLMLSC---GLQQMQDGELTQGSLLSFMIY 415
Cdd:cd18551 231 QLALLVVlgvGGARVASGALTVGTLVAFLLY 261
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
469-644 |
5.35e-25 |
|
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: 103.38 E-value: 5.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEH--CYLhSQV 546
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKriGYV-PQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEpvlFSGSVRNNIAYGL---------QSCED-DKVMAAAQAAHADDFIqemEHGIytdvgekgSQLAAGQKQRLA 616
Cdd:cd03235 77 RSIDRD---FPISVRDVVLMGLyghkglfrrLSKADkAKVDEALERVGLSELA---DRQI--------GELSGGQQQRVL 142
|
170 180
....*....|....*....|....*...
gi 73747917 617 IARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQED 170
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
152-415 |
5.97e-25 |
|
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: 105.19 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDIL-GGDFDPHAFASAIFFMCLFSFGSslsagcrgGCFTYTMsRINL------- 223
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALtAGTLTASQLLRYALLILLLALLI--------GIFRFLW-RYLIfgasrri 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 --RIREQLFSSLLRQDLGFFQETKTGELNSRLSSDttlmsnwlpLNA---------NVLLRSLVKVVGLYGFMLSISPRL 292
Cdd:cd18541 72 eyDLRNDLFAHLLTLSPSFYQKNRTGDLMARATND---------LNAvrmalgpgiLYLVDALFLGVLVLVMMFTISPKL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 293 TLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQcrqlYWRRDLE 372
Cdd:cd18541 143 TLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEE----YVEKNLR 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 73747917 373 ----RALYL-LVRRVLHLGVqMLMLSCGLQQMQDGELTQGSLLSFMIY 415
Cdd:cd18541 219 larvDALFFpLIGLLIGLSF-LIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
467-638 |
6.51e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 6.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:PRK13635 5 IIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEP-VLFSGS-VRNNIAYGLQSC---EDD---KVMAAAQAAHADDFIQEMEHgiytdvgekgsQLAAGQKQRLAIA 618
Cdd:PRK13635 84 GMVFQNPdNQFVGAtVQDDVAFGLENIgvpREEmveRVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIA 152
|
170 180
....*....|....*....|
gi 73747917 619 RALVRDPRVLILDEATSALD 638
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLD 172
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
468-638 |
8.08e-25 |
|
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: 102.95 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPDR-PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHC----YL 542
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 HSQVVSVGQEPVLFSG-SVRNNIAYGLQSCEDDKvmaaaqAAHADDFIQEMEH-GIYTDVGEKGSQLAAGQKQRLAIARA 620
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPK------KERRERAEELLERvGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170
....*....|....*...
gi 73747917 621 LVRDPRVLILDEATSALD 638
Cdd:cd03255 155 LANDPKIILADEPTGNLD 172
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
137-632 |
1.55e-24 |
|
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: 107.96 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 137 LMWRLLKLSRPdlPLLVAAFFFLVLAVLGETLIphysGRVIDILGGDFDPHA-----FASAIFFMCLFSFGSSLSagcrg 211
Cdd:COG4615 3 LLRLLLRESRW--LLLLALLLGLLSGLANAGLI----ALINQALNATGAALArllllFAGLLVLLLLSRLASQLL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 212 gcFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANvLLRSLVKVVGLYGFMLSISPR 291
Cdd:COG4615 72 --LTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPE-LLQSVALVLGCLAYLAWLSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 292 LTLLSLLHMPFTIAaekVYNTRHQEVLREIQDAvaragqvvREAVGGLQtvRSF-----GAEE--------HEVcrYKEA 358
Cdd:COG4615 149 LFLLTLVLLGLGVA---GYRLLVRRARRHLRRA--------REAEDRLF--KHFralleGFKElklnrrrrRAF--FDED 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 359 LEQCRQLYwrRDLERALYLLVRRVLHLGvQMLMLscglqqmqdgeLTQGSLLsFM------IYQESVGSYVQTLVYIYGD 432
Cdd:COG4615 214 LQPTAERY--RDLRIRADTIFALANNWG-NLLFF-----------ALIGLIL-FLlpalgwADPAVLSGFVLVLLFLRGP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 433 MLSNVG----------AAEKVFSyMDRQPNLPSPGTLAPTTLQGVVKFQ-----DVSFAYPNRPDRP--VLKGLTFTLRP 495
Cdd:COG4615 279 LSQLVGalptlsranvALRKIEE-LELALAAAEPAAADAAAPPAPADFQtlelrGVTYRYPGEDGDEgfTLGPIDLTIRR 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 496 GEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS--QYEHcY--LHSQVVSvgqEPVLFSGsvrnniAYGLQSC 571
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTadNREA-YrqLFSAVFS---DFHLFDR------LLGLDGE 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 572 EDDKVMaaaqaahaDDFIQ--EMEH------GIYTDVgekgsQLAAGQKQRLAIARALVRDPRVLILDE 632
Cdd:COG4615 428 ADPARA--------RELLErlELDHkvsvedGRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
467-638 |
1.66e-24 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 102.43 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPN-RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY-------- 537
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 538 --EHcylhsqvvsVG---QEPVLFSG-SVRNNIAYGLQ-SCEDDKVMAAAQAAHADDFiqemehGIYTDVGEKGSQLAAG 610
Cdd:COG1136 84 rrRH---------IGfvfQFFNLLPElTALENVALPLLlAGVSRKERRERARELLERV------GLGDRLDHRPSQLSGG 148
|
170 180
....*....|....*....|....*...
gi 73747917 611 QKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLD 176
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
485-632 |
2.01e-24 |
|
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: 102.13 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY-EHcylhsQVVSVG-----QEPVLFSG 558
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPH-----EIARLGigrtfQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 -SVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEH-----GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDE 632
Cdd:cd03219 90 lTVLENVMVAAQARTGSGLLLARARREEREARERAEEllervGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
460-638 |
4.91e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.26 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 460 APTTLQGVVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEH 539
Cdd:PRK09452 7 QPSSLSPLVELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 540 CylHSQVVSVGQEPVLFSG-SVRNNIAYGL--QSCEDD----KVMAAAQAAHADDFIQEmehgiytdvgeKGSQLAAGQK 612
Cdd:PRK09452 84 E--NRHVNTVFQSYALFPHmTVFENVAFGLrmQKTPAAeitpRVMEALRMVQLEEFAQR-----------KPHQLSGGQQ 150
|
170 180
....*....|....*....|....*.
gi 73747917 613 QRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
468-638 |
5.98e-24 |
|
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: 101.04 E-value: 5.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI---SQYEHCYLHS 544
Cdd:cd03261 1 IELRGLTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSG-SVRNNIAYGLQsceddkvmaaaqaahaddfiqemEHGIYTD-------------VGEKG------ 604
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLR-----------------------EHTRLSEeeireivlekleaVGLRGaedlyp 134
|
170 180 190
....*....|....*....|....*....|....
gi 73747917 605 SQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:cd03261 135 AELSGGMKKRVALARALALDPELLLYDEPTAGLD 168
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
152-350 |
2.06e-23 |
|
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: 100.94 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDIL------GGDFDPHAFASAIFFMCLFSFGSSLsagcrggcFTYTMSRIN--- 222
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIieglggGGGVDFSGLLRILLLLLGLYLLSAL--------FSYLQNRLMarv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 223 -----LRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSL 297
Cdd:cd18547 73 sqrtvYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 73747917 298 LHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEH 350
Cdd:cd18547 153 VTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEE 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
483-638 |
2.12e-23 |
|
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: 99.15 E-value: 2.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE-H-------CYLhsqvvsvGQEPV 554
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHkrarlgiGYL-------PQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 555 LFSG-SVRNNIAYGLQSCEDDKvmaAAQAAHADDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEA 633
Cdd:cd03218 86 IFRKlTVEENILAVLEIRGLSK---KEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
....*
gi 73747917 634 TSALD 638
Cdd:cd03218 161 FAGVD 165
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
467-638 |
2.51e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.21 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYpnRPDRP-VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQ 545
Cdd:PRK13648 7 IIVFKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 VVSVGQEPV-LFSGS-VRNNIAYGLqscEDDKVMAAAQAAHADDFIQEMEHGIYTDvgEKGSQLAAGQKQRLAIARALVR 623
Cdd:PRK13648 85 IGIVFQNPDnQFVGSiVKYDVAFGL---ENHAVPYDEMHRRVSEALKQVDMLERAD--YEPNALSGGQKQRVAIAGVLAL 159
|
170
....*....|....*
gi 73747917 624 DPRVLILDEATSALD 638
Cdd:PRK13648 160 NPSVIILDEATSMLD 174
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
482-638 |
4.88e-23 |
|
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: 97.60 E-value: 4.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCY--LHSQVVSVGQEPVLFSG- 558
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGMVFQQFNLFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQsceddKVmaaaqAAHADDFIQEMEHGIYTDVG--EKG----SQLAAGQKQRLAIARALVRDPRVLILDE 632
Cdd:cd03262 92 TVLENITLAPI-----KV-----KGMSKAEAEERALELLEKVGlaDKAdaypAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
....*.
gi 73747917 633 ATSALD 638
Cdd:cd03262 162 PTSALD 167
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
467-638 |
7.26e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 97.76 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCyLHSQV 546
Cdd:COG1126 1 MIEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD-INKLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVG---QEPVLFSG-SVRNNIAYGL-----QSCED---------DKVmaaaqaahaddfiqemehGIytdvGEKG---- 604
Cdd:COG1126 77 RKVGmvfQQFNLFPHlTVLENVTLAPikvkkMSKAEaeeramellERV------------------GL----ADKAdayp 134
|
170 180 190
....*....|....*....|....*....|....
gi 73747917 605 SQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG1126 135 AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
458-638 |
1.16e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.80 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 458 TLAPTTLQGVVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL--------YQPTGGQVLL 529
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 530 DEKPISQ-----YEhcyLHSQVVSVGQEPVLFSGSVRNNIAYGLqsceddKVMAAAQAAHADDFIqemEH-----GIYTD 599
Cdd:COG1117 76 DGEDIYDpdvdvVE---LRRRVGMVFQKPNPFPKSIYDNVAYGL------RLHGIKSKSELDEIV---EEslrkaALWDE 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 73747917 600 V----GEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG1117 144 VkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
482-638 |
1.35e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVR 561
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 562 NNIAYGLQ---SCEDDKVMaaaqaahADDFiqeMEHGIYTDVGEKG-SQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK10247 99 DNLIFPWQirnQQPDPAIF-------LDDL---ERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
.
gi 73747917 638 D 638
Cdd:PRK10247 169 D 169
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
468-640 |
1.52e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.38 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcylhsqvV 547
Cdd:COG3839 4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----------L 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVG--------QEPVLF-SGSVRNNIAYGLQSCEDDKvmaaaqaahaddfiQEMEH---------GIyTDVGE-KGSQLA 608
Cdd:COG3839 71 PPKdrniamvfQSYALYpHMTVYENIAFPLKLRKVPK--------------AEIDRrvreaaellGL-EDLLDrKPKQLS 135
|
170 180 190
....*....|....*....|....*....|..
gi 73747917 609 AGQKQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
467-638 |
1.72e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 96.27 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLY---QPTGGQVLLDEKPISQYEH---C 540
Cdd:COG2884 1 MIRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRreiP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 541 YLHSQVVSVGQE-PVLFSGSVRNNIAYGLQsceddkvmaaaqaahaddfIQEMEHGIYTD--------VG--EKG----S 605
Cdd:COG2884 76 YLRRRIGVVFQDfRLLPDRTVYENVALPLR-------------------VTGKSRKEIRRrvrevldlVGlsDKAkalpH 136
|
170 180 190
....*....|....*....|....*....|...
gi 73747917 606 QLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG2884 137 ELSGGEQQRVAIARALVNRPELLLADEPTGNLD 169
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
485-632 |
1.76e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 97.03 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE-HcylhsQVVSVG-----QEPVLFSG 558
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPpH-----RIARLGiartfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 -SVRNNIAYGLQSCEDDKVMAAAQAAHA-----DDFIQEMEH-----GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:COG0411 94 lTVLENVLVAAHARLGRGLLAALLRLPRarreeREARERAEEllervGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
....*
gi 73747917 628 LILDE 632
Cdd:COG0411 174 LLLDE 178
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
152-443 |
2.75e-22 |
|
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: 97.58 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVID----ILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIRE 227
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDdvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 228 QLFSSLLRQDLGFFQETKTGELNSRLSSDTT----LMSNWLPlnanVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFT 303
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDrlqdFLSDGLP----DFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 304 IAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLywRRDLERaLYLLVRRVL 383
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDA--NIRAEK-LWATFFPLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73747917 384 HLGVQM---LMLSCGLQQMQDGELTQGSLLSF-----MIYQesvgsYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18563 234 TFLTSLgtlIVWYFGGRQVLSGTMTLGTLVAFlsylgMFYG-----PLQWLSRLNNWITRALTSAERI 296
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
464-642 |
3.28e-22 |
|
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: 96.52 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 464 LQGVVKFQDVSFAYPNRPdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLH 543
Cdd:cd03288 16 LGGEIKIHDLCVRYENNL-KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQEPVLFSGSVRNNIAyGLQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVR 623
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170
....*....|....*....
gi 73747917 624 DPRVLILDEATSALDVQCE 642
Cdd:cd03288 174 KSSILIMDEATASIDMATE 192
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
468-640 |
6.73e-22 |
|
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: 95.10 E-value: 6.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcyLHSQVV 547
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-----VPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVG---QEPVLFSG-SVRNNIAYGLQsceddkvMAAAQAAHADDFIQEMEHGIYTDVGEKG------SQLAAGQKQRLAI 617
Cdd:cd03296 75 NVGfvfQHYALFRHmTVFDNVAFGLR-------VKPRSERPPEAEIRAKVHELLKLVQLDWladrypAQLSGGQRQRVAL 147
|
170 180
....*....|....*....|...
gi 73747917 618 ARALVRDPRVLILDEATSALDVQ 640
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAK 170
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
471-640 |
8.60e-22 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 97.14 E-value: 8.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYehcyLHSQVVSVG 550
Cdd:COG1118 6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN----LPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 ---QEPVLFSG-SVRNNIAYGLQSCE------DDKVMAAAqaahadDFIQ--EMEHgiytdvgEKGSQLAAGQKQRLAIA 618
Cdd:COG1118 79 fvfQHYALFPHmTVAENIAFGLRVRPpskaeiRARVEELL------ELVQleGLAD-------RYPSQLSGGQRQRVALA 145
|
170 180
....*....|....*....|..
gi 73747917 619 RALVRDPRVLILDEATSALDVQ 640
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALDAK 167
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
220-415 |
1.23e-21 |
|
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: 96.10 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 220 RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLH 299
Cdd:cd18565 84 RVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 300 MPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLV 379
Cdd:cd18565 164 VPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPV 243
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 73747917 380 RRVLHLGVQMLMLSCGL------QQMQDGELTQGSLLSFMIY 415
Cdd:cd18565 244 IRLVAGAGFVATFVVGGywvldgPPLFTGTLTVGTLVTFLFY 285
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
484-637 |
1.25e-21 |
|
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: 93.65 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 484 PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE-HCYLHSQVVSVGQEPVLFSG-SVR 561
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 562 NNIAYGLQSCEDDKVmaaaqaahaDDFIQEMeHGIYTDVGEKGSQLAA----GQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:cd03224 94 ENLLLGAYARRRAKR---------KARLERV-YELFPRLKERRKQLAGtlsgGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
485-639 |
1.26e-21 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 93.59 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEkpisqyehcylhsqvVSVGQEP--------VLF 556
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG---------------FDVVKEPaearrrlgFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 557 SG-------SVRNNIAY-----GLQSCEddkvmaaaQAAHADDFIQEMEHGIYTDVgeKGSQLAAGQKQRLAIARALVRD 624
Cdd:cd03266 85 DStglydrlTARENLEYfaglyGLKGDE--------LTARLEELADRLGMEELLDR--RVGGFSTGMRQKVAIARALVHD 154
|
170
....*....|....*
gi 73747917 625 PRVLILDEATSALDV 639
Cdd:cd03266 155 PPVLLLDEPTTGLDV 169
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
468-638 |
1.27e-21 |
|
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: 94.29 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRpdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVV 547
Cdd:cd03295 1 IEFENVTKRYGGG--KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSG-SVRNNIAYGLQScedDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPR 626
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALVPKL---LKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170
....*....|..
gi 73747917 627 VLILDEATSALD 638
Cdd:cd03295 156 LLLMDEPFGALD 167
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
469-638 |
2.37e-21 |
|
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: 93.40 E-value: 2.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVS 548
Cdd:cd03256 2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 VG---QEPVLFSG-SVRNNIAYG-------LQSC------ED--------DKVmaaaqaahaddfiqemehGIYTDVGEK 603
Cdd:cd03256 80 IGmifQQFNLIERlSVLENVLSGrlgrrstWRSLfglfpkEEkqralaalERV------------------GLLDKAYQR 141
|
170 180 190
....*....|....*....|....*....|....*
gi 73747917 604 GSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:cd03256 142 ADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
480-640 |
3.09e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.68 E-value: 3.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLH------SQVVSVGqep 553
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELArrravlPQHSSLS--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 554 vlFSGSVRNNIAYGL----QSCEDDKVMAAAQAAHADdfIQEMEHGIYTdvgekgsQLAAGQKQRLAIARALVR------ 623
Cdd:PRK13548 89 --FPFTVEEVVAMGRaphgLSRAEDDALVAAALAQVD--LAHLAGRDYP-------QLSGGEQQRVQLARVLAQlwepdg 157
|
170
....*....|....*..
gi 73747917 624 DPRVLILDEATSALDVQ 640
Cdd:PRK13548 158 PPRWLLLDEPTSALDLA 174
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
469-638 |
3.59e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.90 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPNRPDRpvlkgLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYehcylhsqvvS 548
Cdd:COG3840 3 RLDDLTYRYGDFPLR-----FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL----------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 VGQEPV--------LFSG-SVRNNIAYGLQS----CEDDKvmaaaqaahaddfiQEMEH-----GIYTDVGEKGSQLAAG 610
Cdd:COG3840 68 PAERPVsmlfqennLFPHlTVAQNIGLGLRPglklTAEQR--------------AQVEQalervGLAGLLDRLPGQLSGG 133
|
170 180
....*....|....*....|....*...
gi 73747917 611 QKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
467-638 |
5.10e-21 |
|
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: 92.35 E-value: 5.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:COG1127 5 MIEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVG---QEPVLFSG-SVRNNIAYGLQsceddkvmaaaqaahaddfiqemEHGIYTD-------------VGEKG----- 604
Cdd:COG1127 82 RRIGmlfQGGALFDSlTVFENVAFPLR-----------------------EHTDLSEaeirelvleklelVGLPGaadkm 138
|
170 180 190
....*....|....*....|....*....|....*
gi 73747917 605 -SQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG1127 139 pSELSGGMRKRVALARALALDPEILLYDEPTAGLD 173
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
467-638 |
5.72e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.22 E-value: 5.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqYEHCYLHSQV 546
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVG---QEP--VLFSGSVRNNIAYG---LQSCEDD---KVMAAAQAAHADDFIQEMEHgiytdvgekgsQLAAGQKQRL 615
Cdd:PRK13639 78 KTVGivfQNPddQLFAPTVEEDVAFGplnLGLSKEEvekRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRV 146
|
170 180
....*....|....*....|...
gi 73747917 616 AIARALVRDPRVLILDEATSALD 638
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLD 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
484-637 |
9.42e-21 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.89 E-value: 9.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 484 PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHS-QVVSVGQEPVLFSG-SVR 561
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQlGIYLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73747917 562 NNIAYGLQSCEDDKvmaaaqaAHADDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK15439 105 ENILFGLPKRQASM-------QKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
467-638 |
9.49e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 92.94 E-value: 9.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP--------TGGQVLLDEKPISQye 538
Cdd:PRK13640 5 IVEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVWD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 539 hcyLHSQVVSVGQEP-VLFSG-SVRNNIAYGLqscEDDKVMAAAQAAHADDFIQEMEHGIYTDvgEKGSQLAAGQKQRLA 616
Cdd:PRK13640 82 ---IREKVGIVFQNPdNQFVGaTVGDDVAFGL---ENRAVPRPEMIKIVRDVLADVGMLDYID--SEPANLSGGQKQRVA 153
|
170 180
....*....|....*....|..
gi 73747917 617 IARALVRDPRVLILDEATSALD 638
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLD 175
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
152-415 |
1.17e-20 |
|
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: 92.96 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVID-ILGGDFDPHAFA----------SAIFFMCLFSFGSSLSAGCRGGCFTYTMS- 219
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDdVLGDKPLPGLLGlapllgpdplALLLLAAAALVGIALLRGLASYAGTYLTAl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 220 ---RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTT-----LMSNWLPLNANVLLrslvkVVGLYGFMLSISPR 291
Cdd:cd18564 81 vgqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGaiqdlLVSGVLPLLTNLLT-----LVGMLGVMFWLDWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 292 LTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWR-RD 370
Cdd:cd18564 156 LALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRaAR 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 73747917 371 LERALYLLVRRVLHLGVqMLMLSCGLQQMQDGELTQGSLLSFMIY 415
Cdd:cd18564 236 LQALLSPVVDVLVAVGT-ALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
468-638 |
1.36e-20 |
|
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: 90.39 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcyLHSQVV 547
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP--KDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSG-SVRNNIAYGLQSCEDDKvmaaaqaahadDFIQEMEH------GIYTDVGEKGSQLAAGQKQRLAIARA 620
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAFGLKLRKVPK-----------DEIDERVRevaellQIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170
....*....|....*...
gi 73747917 621 LVRDPRVLILDEATSALD 638
Cdd:cd03301 145 IVREPKVFLMDEPLSNLD 162
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
468-640 |
1.62e-20 |
|
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: 90.64 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI-SQYEHCYLHSQV 546
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSvgQEPVLFSG-SVRNNIAY--GLQSCEDDKVMaaaqaAHADDFIQEMEHGIYTDVgeKGSQLAAGQKQRLAIARALVR 623
Cdd:cd03263 80 CP--QFDALFDElTVREHLRFyaRLKGLPKSEIK-----EEVELLLRVLGLTDKANK--RARTLSGGMKRKLSLAIALIG 150
|
170
....*....|....*..
gi 73747917 624 DPRVLILDEATSALDVQ 640
Cdd:cd03263 151 GPSVLLLDEPTSGLDPA 167
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
485-640 |
1.62e-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: 90.86 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY---EHcylhsQVVSVGQEPVLFSG-SV 560
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppeKR-----DISYVPQNYALFPHmTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 RNNIAYGLQSCEDDKVmaaaqaaHADDFIQEMEH--GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:cd03299 89 YKNIAYGLKKRKVDKK-------EIERKVLEIAEmlGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
|
..
gi 73747917 639 VQ 640
Cdd:cd03299 162 VR 163
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
153-417 |
1.94e-20 |
|
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: 92.16 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 153 VAAFFFLVL--AVLGeTLIPHYSGRVID--ILGGDFDphafasAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRI--- 225
Cdd:cd18550 1 LALVLLLILlsALLG-LLPPLLLREIIDdaLPQGDLG------LLVLLALGMVAVAVASALLGVVQTYLSARIGQGVmyd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 226 -REQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTI 304
Cdd:cd18550 74 lRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 305 AAEKVYNTRHQEVLREIQDAVARAGQVVRE--AVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLE-RALYLLVRR 381
Cdd:cd18550 154 LPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAgRWFFAALGL 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 73747917 382 VLHLGVQMLMLSCGLqQMQDGELTQGSLLSFMIYQE 417
Cdd:cd18550 234 FTAIGPALVYWVGGL-LVIGGGLTIGTLVAFTALLG 268
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
468-638 |
2.06e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 92.83 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRpDRPV--LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcylhSQ 545
Cdd:COG1135 2 IELENLSKTFPTK-GGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSE----RE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 VV----SVG---QEPVLFSG-SVRNNIAYGLQsceddkvmaaaqaahaddfIQEMEHG-IYTDVGE---------KG--- 604
Cdd:COG1135 77 LRaarrKIGmifQHFNLLSSrTVAENVALPLE-------------------IAGVPKAeIRKRVAEllelvglsdKAday 137
|
170 180 190
....*....|....*....|....*....|....*
gi 73747917 605 -SQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG1135 138 pSQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
483-639 |
2.61e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.95 E-value: 2.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY-------------EHCYLH-----S 544
Cdd:COG4559 14 RTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWspwelarrravlpQHSSLAfpftvE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSGSVRNNIAyglqscedDKVMAAAQaahaddfIQEMEHGIYTdvgekgsQLAAGQKQRLAIARALV-- 622
Cdd:COG4559 94 EVVALGRAPHGSSAAQDRQIV--------REALALVG-------LAHLAGRSYQ-------TLSGGEQQRVQLARVLAql 151
|
170 180
....*....|....*....|..
gi 73747917 623 -----RDPRVLILDEATSALDV 639
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDL 173
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
467-638 |
3.06e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPDrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI--SQYEHCYLHS 544
Cdd:PRK13636 5 ILKVEELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEP--VLFSGSVRNNIAYGLQSCE--DDKVMAAAQAAHADDFIQEMEHgiytdvgEKGSQLAAGQKQRLAIARA 620
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGV 155
|
170
....*....|....*...
gi 73747917 621 LVRDPRVLILDEATSALD 638
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLD 173
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
152-443 |
4.81e-20 |
|
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: 90.99 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVID--ILGGDFDPHAFASAIFFmcLFSFGSSLSAGCRggcfTYTMSRIN----LRI 225
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDeyIPNGDLSGLLIIALLFL--ALNLVNWVASRLR----IYLMAKVGqrilYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 226 REQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIA 305
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 306 AEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLyWRR--DLERALYLLVRRVL 383
Cdd:cd18545 156 VVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKA-NMRavRLNALFWPLVELIS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 384 HLGVqMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18545 235 ALGT-ALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
472-638 |
5.64e-20 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 88.79 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 472 DVSFAYPNRPdrpVLKGLTFTLRPGeVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcYLHSQVVSVGQ 551
Cdd:cd03264 5 NLTKRYGKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 552 EPVLFSG-SVRNNIAY--GLQSCEDDKVmaaaqaahaDDFIQEM--EHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPR 626
Cdd:cd03264 80 EFGVYPNfTVREFLDYiaWLKGIPSKEV---------KARVDEVleLVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170
....*....|..
gi 73747917 627 VLILDEATSALD 638
Cdd:cd03264 151 ILIVDEPTAGLD 162
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
488-639 |
5.95e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 91.33 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 488 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYL---HSQVVSVGQEPvlfSGS----- 559
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP---YASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 560 -VRNNIAYGLqsceddKVMAAAQAAHADDFIQEMehgiYTDVGEKGS-------QLAAGQKQRLAIARALVRDPRVLILD 631
Cdd:COG4608 113 tVGDIIAEPL------RIHGLASKAERRERVAEL----LELVGLRPEhadryphEFSGGQRQRIGIARALALNPKLIVCD 182
|
....*...
gi 73747917 632 EATSALDV 639
Cdd:COG4608 183 EPVSALDV 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
491-639 |
7.63e-20 |
|
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: 88.51 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 491 FTLR-----PGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI--SQYEHCyLHSQVVSVG---QEPVLFSG-S 559
Cdd:cd03297 13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKIN-LPPQQRKIGlvfQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 560 VRNNIAYGLQSCEDDKvmaaaqaahadDFIQEMEHGIYTDVGE----KGSQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:cd03297 92 VRENLAFGLKRKRNRE-----------DRISVDELLDLLGLDHllnrYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
....
gi 73747917 636 ALDV 639
Cdd:cd03297 161 ALDR 164
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
482-638 |
8.78e-20 |
|
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: 88.04 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYlhSQVVSVGQEPVLFSG-SV 560
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 RNNI-----AYGLQSCEDDKVMAAAqaahaddfiqemehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:cd03268 90 RENLrllarLLGIRKKRIDEVLDVV--------------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
...
gi 73747917 636 ALD 638
Cdd:cd03268 156 GLD 158
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
152-415 |
8.85e-20 |
|
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: 90.29 E-value: 8.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAF--------ASAIFFMCLFSFGSSLSAGCRGGCFTYTMsrinl 223
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLllglalllLGAYLLRALLNFLRIYLNHVAEQKVVADL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 riREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFT 303
Cdd:cd18778 76 --RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 304 IAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQcrqlyWRRDLERALYL------ 377
Cdd:cd18778 154 ALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRR-----YRKAQLRAMKLwaifhp 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 73747917 378 LVRRVLHLGVqMLMLSCGLQQMQDGELTQGSLLSFMIY 415
Cdd:cd18778 229 LMEFLTSLGT-VLVLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
195-640 |
9.05e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.46 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 195 FMCLFSFGSsLSAGCRggcftyTMSRINLRireqlfsSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRs 274
Cdd:PTZ00243 1017 LRFFLSYEA-MRRGSR------NMHRDLLR-------SVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQ- 1081
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 275 lvkvvglygFMLSISPRLtLLSLLHMPFTIAA-----------EKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVR 343
Cdd:PTZ00243 1082 ---------CLFSICSSI-LVTSASQPFVLVAlvpcgylyyrlMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATIT 1151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 344 SFGaEEHEVcrYKEALEQCRQLYwrrdleRALYLLVRRVLHLGVQMLMLSC------------GLQQMQDGELTQGSLLS 411
Cdd:PTZ00243 1152 AYG-KAHLV--MQEALRRLDVVY------SCSYLENVANRWLGVRVEFLSNivvtvialigviGTMLRATSQEIGLVSLS 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 412 FMIYQESVGSyVQTLVYIYGDMLSNVGAAEKVFSYMDRQPN--LP----------------------------SPGTLAP 461
Cdd:PTZ00243 1223 LTMAMQTTAT-LNWLVRQVATVEADMNSVERLLYYTDEVPHedMPeldeevdalerrtgmaadvtgtvviepaSPTSAAP 1301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 462 TTLQ-GVVKFQDVSFAYpnRPDRP-VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEH 539
Cdd:PTZ00243 1302 HPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGL 1379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 540 CYLHSQVVSVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEhGIYTDVGEKGSQLAAGQKQRLAIAR 619
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESE-GIDSRVLEGGSNYSVGQRQLMCMAR 1458
|
490 500
....*....|....*....|....*.
gi 73747917 620 ALV-RDPRVLILDEATS----ALDVQ 640
Cdd:PTZ00243 1459 ALLkKGSGFILMDEATAnidpALDRQ 1484
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
468-638 |
1.11e-19 |
|
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: 87.85 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEH---CYLHS 544
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraiPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSG-SVRNNIAYGLQSCE------DDKVMAAAQAAHADDFIQEMEhgiytdvgekgSQLAAGQKQRLAI 617
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEVTGvppreiRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180
....*....|....*....|.
gi 73747917 618 ARALVRDPRVLILDEATSALD 638
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLD 168
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
485-634 |
1.93e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 87.58 E-value: 1.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcylHSQV------VSVGQE--PVLf 556
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPP---HERAragiayVPQGREifPRL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 557 sgSVRNNIAYGLQSCEDDKvmaaaqaAHADDFI-------QEMEHgiytdvgEKGSQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:TIGR03410 91 --TVEENLLTGLAALPRRS-------RKIPDEIyelfpvlKEMLG-------RRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
....*
gi 73747917 630 LDEAT 634
Cdd:TIGR03410 155 LDEPT 159
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
469-638 |
2.82e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.00 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPN-RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEhcylhSQVV 547
Cdd:COG4525 5 TVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSG-SVRNNIAYGLQScedDKVMAAAQAAHADDFIQEM------EHGIYtdvgekgsQLAAGQKQRLAIARA 620
Cdd:COG4525 80 VVFQKDALLPWlNVLDNVAFGLRL---RGVPKAERRARAEELLALVgladfaRRRIW--------QLSGGMRQRVGIARA 148
|
170
....*....|....*...
gi 73747917 621 LVRDPRVLILDEATSALD 638
Cdd:COG4525 149 LAADPRFLLMDEPFGALD 166
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
484-634 |
3.03e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 87.34 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 484 PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE-HcylhsQVVSVG-----QEPVLFS 557
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpH-----RIARLGigyvpEGRRIFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 558 G-SVRNNIAYGLQSCEDDkvmaaaqaahaDDFIQEMEHgIYT---DVGEKGSQLAA----GQKQRLAIARALVRDPRVLI 629
Cdd:COG0410 92 SlTVEENLLLGAYARRDR-----------AEVRADLER-VYElfpRLKERRRQRAGtlsgGEQQMLAIGRALMSRPKLLL 159
|
....*
gi 73747917 630 LDEAT 634
Cdd:COG0410 160 LDEPS 164
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
486-651 |
3.06e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqyehcyLHSQVVS-------VGQEPVLFSG 558
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR------IRSPRDAialgigmVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 -SVRNNIAYGLqscEDDKVMAAAQAAHADDfIQEM--EHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:COG3845 95 lTVAENIVLGL---EPTKGGRLDRKAARAR-IRELseRYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170
....*....|....*.
gi 73747917 636 ALDVQceQAKTLWKFM 651
Cdd:COG3845 171 VLTPQ--EADELFEIL 184
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
482-639 |
3.62e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.38 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSG-SV 560
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 RNNIAYGLQ---------SCEDDKVMAaaqaahaddfiQEMEHGIYTDVGEKG-SQLAAGQKQRLAIARALVRDPRVLIL 630
Cdd:PRK11231 94 RELVAYGRSpwlslwgrlSAEDNARVN-----------QAMEQTRINHLADRRlTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
....*....
gi 73747917 631 DEATSALDV 639
Cdd:PRK11231 163 DEPTTYLDI 171
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
480-640 |
5.09e-19 |
|
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: 85.62 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYlHSQVVSVGQEPVLFSG- 558
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQSCEDDKVMaaaqaahadDFIQEMEHGIYTDVgeKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:cd03231 89 SVLENLRFWHADHSDEQVE---------EALARVGLNGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
..
gi 73747917 639 VQ 640
Cdd:cd03231 158 KA 159
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
470-639 |
6.76e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 470 FQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEkpisqyehcylHSQVVSV 549
Cdd:COG0488 1 LENLSKSFG---GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 550 GQEPVLFSG-SVRNNIAYG----------LQSCEDDKVMAAAQAAHADDFIQEMEH-----------------GIYTDVG 601
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGdaelraleaeLEELEAKLAEPDEDLERLAELQEEFEAlggweaearaeeilsglGFPEEDL 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 73747917 602 EKG-SQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
472-638 |
8.77e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 472 DVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI--SQYEHCYLHSQVVSV 549
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 550 GQEP--VLFSGSVRNNIAYGLQSCE----------DDKVMAAAQAAHADDFIQEMEHgiytdvgekgsqlaaGQKQRLAI 617
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGvpeaeitrrvDEALTLVDAQHFRHQPIQCLSH---------------GQKKRVAI 147
|
170 180
....*....|....*....|.
gi 73747917 618 ARALVRDPRVLILDEATSALD 638
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLD 168
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
460-639 |
1.30e-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: 89.36 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 460 APTTLQGvvkfQDVSFAYP------NRPDRPV--LKGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQnLyQPTGGQVLLD 530
Cdd:COG4172 272 APPLLEA----RDLKVWFPikrglfRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPSEGEIRFD 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 531 EKPISQYEHCYL-----HSQVVSvgQEPvlFSG-----SVRNNIAYGLQSCE--------DDKVmaaaqaahaddfIQEM 592
Cdd:COG4172 346 GQDLDGLSRRALrplrrRMQVVF--QDP--FGSlsprmTVGQIIAEGLRVHGpglsaaerRARV------------AEAL 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 73747917 593 EhgiytDVGEKGS-------QLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG4172 410 E-----EVGLDPAarhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
152-443 |
1.56e-18 |
|
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: 86.39 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVID--ILGGDFDPHAFASAIFFmclfsfGSSLSAGCRGGCFTYTMSRI------NL 223
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDsgVRAGDLGVLLLAAAAYL------AVVLAGWVAQRAQTRLTGRTgerllyDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 224 RIReqLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFT 303
Cdd:cd18546 75 RLR--VFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 304 IAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLywRRDLER--ALYLLVRR 381
Cdd:cd18546 153 ALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDA--RLRAQRlvAIYFPGVE 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747917 382 VLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18546 231 LLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
467-638 |
1.66e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 86.32 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEP-VLFSG-SVRNNIAYGLQSceddkvmaaaQAAHADDFIQEMEHGI----YTDVGEKG-SQLAAGQKQRLAIAR 619
Cdd:PRK13650 84 GMVFQNPdNQFVGaTVEDDVAFGLEN----------KGIPHEEMKERVNEALelvgMQDFKEREpARLSGGQKQRVAIAG 153
|
170
....*....|....*....
gi 73747917 620 ALVRDPRVLILDEATSALD 638
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLD 172
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
486-639 |
1.74e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 86.00 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLfSGSVRNNIA 565
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST-SLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 566 yglqsceddKVMAAAQAAHADDFIQEMEHGIYTDVGEKG----------SQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:PRK15112 108 ---------QILDFPLRLNTDLEPEQREKQIIETLRQVGllpdhasyypHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
....
gi 73747917 636 ALDV 639
Cdd:PRK15112 179 SLDM 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
480-640 |
3.62e-18 |
|
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: 83.18 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQ-----YEHC-YL-HSQvvsvGQE 552
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEqrdepHENIlYLgHLP----GLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 553 PVLfsgSVRNNIAYGLQSCEDDkvmaaaqaahaddfiQEMEHGIYTDVGEKG------SQLAAGQKQRLAIARALVRDPR 626
Cdd:TIGR01189 86 PEL---SALENLHFWAAIHGGA---------------QRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRP 147
|
170
....*....|....
gi 73747917 627 VLILDEATSALDVQ 640
Cdd:TIGR01189 148 LWILDEPTTALDKA 161
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
472-647 |
5.00e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 472 DVSFAypnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQ 551
Cdd:PRK09536 10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 552 EPVL-FSGSVRNNIAYG---------LQSCEDDKVMAaaqaahaddfiQEMEHGIYTDVGEKG-SQLAAGQKQRLAIARA 620
Cdd:PRK09536 85 DTSLsFEFDVRQVVEMGrtphrsrfdTWTETDRAAVE-----------RAMERTGVAQFADRPvTSLSGGERQRVLLARA 153
|
170 180
....*....|....*....|....*..
gi 73747917 621 LVRDPRVLILDEATSALDVQcEQAKTL 647
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDIN-HQVRTL 179
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
467-638 |
5.37e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.40 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:PRK13647 4 IIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEP--VLFSGSVRNNIAYGLQSCE------DDKVMAAAQAAHADDFIQEMEHgiytdvgekgsQLAAGQKQRLAIA 618
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVNMGldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180
....*....|....*....|
gi 73747917 619 RALVRDPRVLILDEATSALD 638
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLD 170
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
480-639 |
6.85e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 6.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcylHSQVVSVGQ----EPVL 555
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 556 fsgSVRNNIA-----YGlqsceddkvmaaAQAAHADDFIQEMEHGIYTDVgeKGSQLAAGQKQRLAIARALVRDPRVLIL 630
Cdd:PRK13539 89 ---TVAENLEfwaafLG------------GEELDIAAALEAVGLAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
....*....
gi 73747917 631 DEATSALDV 639
Cdd:PRK13539 152 DEPTAALDA 160
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
482-639 |
8.11e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQVLLDEKPIS----------------QYehcylh 543
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILelspderaragiflafQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 sqvvsvgqePVLFSG-SVRN--NIAYGLQSCEDDKVMaaaqaahadDFIQEMEH-----GI-------YTDVGEKGsqla 608
Cdd:COG0396 86 ---------PVEIPGvSVSNflRTALNARRGEELSAR---------EFLKLLKEkmkelGLdedfldrYVNEGFSG---- 143
|
170 180 190
....*....|....*....|....*....|.
gi 73747917 609 aGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG0396 144 -GEKKRNEILQMLLLEPKLAILDETDSGLDI 173
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
483-632 |
9.69e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQ---YEHC-----YLhsqvvsvGQEPV 554
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRArlgigYL-------PQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 555 LFSG-SVRNNIAYGLQSCEDDKvmaAAQAAHADDFIQEMehGIyTDVGE-KGSQLAAGQKQRLAIARALVRDPRVLILDE 632
Cdd:COG1137 89 IFRKlTVEDNILAVLELRKLSK---KEREERLEELLEEF--GI-THLRKsKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
468-638 |
1.58e-17 |
|
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: 81.77 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPDRpvlkgLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCylHSQVV 547
Cdd:cd03298 1 VRLDKIRFSYGEQPMH-----FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSG-SVRNNIAYGLQ-----SCEDDKVMaaaqaahaddfiqemeHGIYTDVGEKG------SQLAAGQKQRL 615
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSpglklTAEDRQAI----------------EVALARVGLAGlekrlpGELSGGERQRV 137
|
170 180
....*....|....*....|...
gi 73747917 616 AIARALVRDPRVLILDEATSALD 638
Cdd:cd03298 138 ALARVLVRDKPVLLLDEPFAALD 160
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
490-638 |
1.83e-17 |
|
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: 82.69 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 490 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYL---HSQVVS-VGQEPVLFSG-SVRNNI 564
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKKISmVFQSFALLPHrTVLENV 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73747917 565 AYGLqscEDDKVMAAAQAAHADDFIQEMEHGIYTDvgEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:cd03294 124 AFGL---EVQGVPRAEREERAAEALELVGLEGWEH--KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
472-644 |
2.90e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.02 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 472 DVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ------PTGGQVLLDEKPISQYEHCYLHSQ 545
Cdd:PRK14246 12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 VVSVGQEPVLFSG-SVRNNIAYGLQSC------EDDKVMAAAQAAHAddfiqeMEHGIYTDVGEKGSQLAAGQKQRLAIA 618
Cdd:PRK14246 92 VGMVFQQPNPFPHlSIYDNIAYPLKSHgikekrEIKKIVEECLRKVG------LWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180
....*....|....*....|....*.
gi 73747917 619 RALVRDPRVLILDEATSALDVQCEQA 644
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQA 191
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
469-639 |
3.23e-17 |
|
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: 81.04 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEhcylhsqvVS 548
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG--------LG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 VGQEPVLfsgSVRNNI-----AYGLQSCEDDKVMaaaqaahadDFIQEmehgiYTDVGEKGSQ----LAAGQKQRLAIAR 619
Cdd:cd03220 93 GGFNPEL---TGRENIylngrLLGLSRKEIDEKI---------DEIIE-----FSELGDFIDLpvktYSSGMKARLAFAI 155
|
170 180
....*....|....*....|
gi 73747917 620 ALVRDPRVLILDEATSALDV 639
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDA 175
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
467-638 |
3.84e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 81.29 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLD----------EKPISQ 536
Cdd:PRK09493 1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglkvndpkvdERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 537 -----YEHCYLHSQVVSVgqEPVLFsGSVRnniAYGLQSCEDDKvmaaaqaahaddfiQEMEhgIYTDVG--EKG----S 605
Cdd:PRK09493 78 eagmvFQQFYLFPHLTAL--ENVMF-GPLR---VRGASKEEAEK--------------QARE--LLAKVGlaERAhhypS 135
|
170 180 190
....*....|....*....|....*....|...
gi 73747917 606 QLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
467-638 |
4.11e-17 |
|
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: 79.90 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRP---DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQVLLDEKPISQYEhcy 541
Cdd:cd03213 3 TLSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 542 LHSQVVSVGQEPVLFSG-SVRNNIayglqsceddkvmaaaqaahadDFIQEMehgiytdvgekgSQLAAGQKQRLAIARA 620
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETL----------------------MFAAKL------------RGLSGGERKRVSIALE 125
|
170
....*....|....*...
gi 73747917 621 LVRDPRVLILDEATSALD 638
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLD 143
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
483-638 |
4.12e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.73 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcylhsqvVSVGQEPV-------- 554
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----------VPPYQRPInmmfqsya 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 555 LFSG-SVRNNIAYGLQScedDKVmaaaQAAHADDFIQEMEHGIYTD--VGEKGSQLAAGQKQRLAIARALVRDPRVLILD 631
Cdd:PRK11607 102 LFPHmTVEQNIAFGLKQ---DKL----PKAEIASRVNEMLGLVHMQefAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
....*..
gi 73747917 632 EATSALD 638
Cdd:PRK11607 175 EPMGALD 181
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
467-638 |
4.79e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.93 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNrPDRPV--LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQ-------- 536
Cdd:PRK11153 1 MIELKNISKVFPQ-GGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 537 --------YEHCYLhsqvvsvgqepvLFSGSVRNNIAYGLQSCEDDKvmaaaqaahadDFIQEMEHGIYTDVG--EKG-- 604
Cdd:PRK11153 80 arrqigmiFQHFNL------------LSSRTVFDNVALPLELAGTPK-----------AEIKARVTELLELVGlsDKAdr 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 73747917 605 --SQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK11153 137 ypAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
467-639 |
5.66e-17 |
|
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: 80.90 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAypnRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ----NLYQPTGGQV-LLDEKPisqyehcy 541
Cdd:COG1119 3 LLELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKST---LLSlitgDLPPTYGNDVrLFGERR-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 542 lhsqvvsvGQEPV--------LFSGSVRNNIAYGLqSCED----------------DKVMAAAQAAHADDFiqEMEHGIY 597
Cdd:COG1119 69 --------GGEDVwelrkrigLVSPALQLRFPRDE-TVLDvvlsgffdsiglyrepTDEQRERARELLELL--GLAHLAD 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 73747917 598 TDVGekgsQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG1119 138 RPFG----TLSQGEQRRVLIARALVKDPELLILDEPTAGLDL 175
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
465-638 |
7.68e-17 |
|
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: 80.01 E-value: 7.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 465 QGVVKFQDVSFAYPN-RPDRPVLKGLTFTLRPGEVTALVGPNGSGKST----VAALLQNLYQpTGGQVLLDEKPISQYEh 539
Cdd:cd03234 1 QRVLPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRKPDQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 540 cyLHSQVVSVGQEPVLFSG-SVRNNIAYG----LQSCEDDKVmaaaqAAHADDFIQEMEHGIyTDVG-EKGSQLAAGQKQ 613
Cdd:cd03234 79 --FQKCVAYVRQDDILLPGlTVRETLTYTailrLPRKSSDAI-----RKKRVEDVLLRDLAL-TRIGgNLVKGISGGERR 150
|
170 180
....*....|....*....|....*
gi 73747917 614 RLAIARALVRDPRVLILDEATSALD 638
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
447-644 |
1.01e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 447 MDRQPNLPSPGTLAPTTLQGVVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPT 523
Cdd:COG4178 342 LEAADALPEAASRIETSEDGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaGLWPYG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 524 GGQVLLDEkpisqyehcylHSQVVSVGQEPVLFSGSVRNNIAYGLQSCE--DDKVMAAAQAAHADDFIQEMEhgiytDVG 601
Cdd:COG4178 417 SGRIARPA-----------GARVLFLPQRPYLPLGTLREALLYPATAEAfsDAELREALEAVGLGHLAERLD-----EEA 480
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 73747917 602 EKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:COG4178 481 DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAA 523
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
468-638 |
1.08e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG-----GQVLLDEKPIsqYEH--- 539
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI--YERrvn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 540 -CYLHSQVVSVGQEPVLFSGSVRNNIAYGLQ------SCEDDKVMAAAQAAHadDFIQEMEHGIYtdvgEKGSQLAAGQK 612
Cdd:PRK14258 83 lNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrpKLEIDDIVESALKDA--DLWDEIKHKIH----KSALDLSGGQQ 156
|
170 180
....*....|....*....|....*.
gi 73747917 613 QRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLD 182
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
480-639 |
1.11e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.27 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIsQYEHCYLHSQVV------------ 547
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYKYRCKHIrmifqdpntsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 ---SVGQ---EPVLF----SGSVRNN-IAYGLQsceddKVmaaaqaahaddfiqemehGIYTDVGEKGSQ-LAAGQKQRL 615
Cdd:COG4167 102 prlNIGQileEPLRLntdlTAEEREErIFATLR-----LV------------------GLLPEHANFYPHmLSSGQKQRV 158
|
170 180
....*....|....*....|....
gi 73747917 616 AIARALVRDPRVLILDEATSALDV 639
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDM 182
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
468-638 |
1.25e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.83 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAY-PNRP-DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS----QYEHCY 541
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 542 LHSQVVSVGQ--EPVLFSGSVRNNIAYGLQ----SCEDDKvmaaaqaAHADDFIQEMehGIYTDVGEKGS-QLAAGQKQR 614
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMnfgvSEEDAK-------QKAREMIELV--GLPEELLARSPfELSGGQMRR 153
|
170 180
....*....|....*....|....
gi 73747917 615 LAIARALVRDPRVLILDEATSALD 638
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
485-640 |
1.28e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcyLHS---QVVSVGQEPVLFSG-SV 560
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-----LHArdrKVGFVFQHYALFRHmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 RNNIAYGLQ----------SCEDDKVMAAAqaahadDFIQeMEHgiytdVGEK-GSQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:PRK10851 92 FDNIAFGLTvlprrerpnaAAIKAKVTQLL------EMVQ-LAH-----LADRyPAQLSGGQKQRVALARALAVEPQILL 159
|
170
....*....|.
gi 73747917 630 LDEATSALDVQ 640
Cdd:PRK10851 160 LDEPFGALDAQ 170
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
486-638 |
2.22e-16 |
|
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: 78.66 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIsqyehcylhsqvvsvgQEP-----VLFSG-- 558
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----------------TEPgpdrmVVFQNys 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 -----SVRNNIAYGLqscedDKVMAAAQAAHADDFIQemEH----GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:TIGR01184 65 llpwlTVRENIALAV-----DRVLPDLSKSERRAIVE--EHialvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLL 137
|
....*....
gi 73747917 630 LDEATSALD 638
Cdd:TIGR01184 138 LDEPFGALD 146
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
468-644 |
2.44e-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: 76.81 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVlldekpisqyeHCYLHSQVV 547
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSGSVRNNIAYGLqscedDKVmaaaqaahaddfiqemehgiytdvgekgsqLAAGQKQRLAIARALVRDPRV 627
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPW-----DDV------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170
....*....|....*..
gi 73747917 628 LILDEATSALDVQCEQA 644
Cdd:cd03223 113 VFLDEATSALDEESEDR 129
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
193-638 |
2.45e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.42 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 193 IFFMCLFSFGSSLSAGC-RGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVL 271
Cdd:TIGR01271 927 IFYIYVGTADSVLALGFfRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDF 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 272 LRSLVKVVGLYgFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQdAVARAGQVVR--EAVGGLQTVRSFGAEE 349
Cdd:TIGR01271 1007 IQLTLIVLGAI-FVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLE-SEARSPIFSHliTSLKGLWTIRAFGRQS 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 350 HEVCRYKEALEQCRQLYWrrdleraLYLLVRRVLHLGVQML---------MLSCGLQQMQDGELtqGSLLSF-MIYQESV 419
Cdd:TIGR01271 1085 YFETLFHKALNLHTANWF-------LYLSTLRWFQMRIDIIfvfffiavtFIAIGTNQDGEGEV--GIILTLaMNILSTL 1155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 420 GSYVQTLVYIYGDMLSnvgaAEKVFSYMDRQPNLPSP----GTLAPTTL--------------QGVVKFQDVSFAYpNRP 481
Cdd:TIGR01271 1156 QWAVNSSIDVDGLMRS----VSRVFKFIDLPQEEPRPsgggGKYQLSTVlvienphaqkcwpsGGQMDVQGLTAKY-TEA 1230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLyqPTGGQVLLDEkpISqYEHCYLHSQVVSVG---QEPVLFS 557
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTlLSALLRLL--STEGEIQIDG--VS-WNSVTLQTWRKAFGvipQKVFIFS 1305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 558 GSVRNNI-AYGLQSceDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSA 636
Cdd:TIGR01271 1306 GTFRKNLdPYEQWS--DEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAH 1383
|
..
gi 73747917 637 LD 638
Cdd:TIGR01271 1384 LD 1385
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
463-638 |
2.67e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 2.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 463 TLQGVVKfqdvSFAypnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqyehcyl 542
Cdd:COG4152 3 ELKGLTK----RFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 HSQVVSVG---QEPVLFSG-SVRNNIAY-----GLQSCEDDKVMaaaqaahaDDFIQEMEHGIYTDvgEKGSQLAAGQKQ 613
Cdd:COG4152 67 PEDRRRIGylpEERGLYPKmKVGEQLVYlarlkGLSKAEAKRRA--------DEWLERLGLGDRAN--KKVEELSKGNQQ 136
|
170 180
....*....|....*....|....*
gi 73747917 614 RLAIARALVRDPRVLILDEATSALD 638
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLD 161
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
467-638 |
2.88e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 78.38 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY---EHCYLH 543
Cdd:PRK10908 1 MIRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQE-PVLFSGSVRNNIAYGL----QSCED---------DKVmaaaqaahaddfiqemehGIYTDVGEKGSQLAA 609
Cdd:PRK10908 79 RQIGMIFQDhHLLMDRTVYDNVAIPLiiagASGDDirrrvsaalDKV------------------GLLDKAKNFPIQLSG 140
|
170 180
....*....|....*....|....*....
gi 73747917 610 GQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK10908 141 GEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
485-638 |
5.10e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 78.25 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDE------KPISQYEHCY--LHSQVVSVGQEPVLF 556
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtaRSLSQQKGLIrqLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 557 SG-SVRNNIAYGlqsceddkvmAAAQAAHADDFIQEMEHGIYTDVGEKGSQ------LAAGQKQRLAIARALVRDPRVLI 629
Cdd:PRK11264 98 PHrTVLENIIEG----------PVIVKGEPKEEATARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVIL 167
|
....*....
gi 73747917 630 LDEATSALD 638
Cdd:PRK11264 168 FDEPTSALD 176
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
471-639 |
5.64e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVG 550
Cdd:PRK10575 15 RNVSFRVP---GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 QE-PVLFSGSVRNNIAYGLQ---------SCEDDkvmaaaqaahaddfiQEMEHGIyTDVGEKG------SQLAAGQKQR 614
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGRYpwhgalgrfGAADR---------------EKVEEAI-SLVGLKPlahrlvDSLSGGERQR 155
|
170 180
....*....|....*....|....*
gi 73747917 615 LAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
152-437 |
6.18e-16 |
|
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: 78.59 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVID--ILGGDFDphAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQL 229
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDegIANGDLS--YILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 230 FSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLplnaNVLLRSLVK-----VVGLYgFMLSISPRLTLLSLLHMPFTI 304
Cdd:cd18548 79 FEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFV----MMLLRMLVRapimlIGAII-MAFRINPKLALILLVAIPILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 305 AAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQcrqlyWRRDLERALYLLvrrVLH 384
Cdd:cd18548 154 LVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDD-----LTDTSLKAGRLM---ALL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 73747917 385 LGVQMLMLSCGL--------QQMQDGELTQGSLLSFMIYQesvgsyVQTLVYIYgdMLSNV 437
Cdd:cd18548 226 NPLMMLIMNLAIvailwfggHLINAGSLQVGDLVAFINYL------MQILMSLM--MLSMV 278
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
456-640 |
6.19e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.08 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 456 PGTLAPTTLQGVVKFQDvsfaypnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS 535
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYG---------DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 536 QYEHcYLHSQVVSVGQ----EPVLfsgSVRNNIA-----YGLQSCEDDKVMAAAQaahadDFIQeMEHGIYTDVGEkgsq 606
Cdd:PRK13537 73 SRAR-HARQRVGVVPQfdnlDPDF---TVRENLLvfgryFGLSAAAARALVPPLL-----EFAK-LENKADAKVGE---- 138
|
170 180 190
....*....|....*....|....*....|....
gi 73747917 607 LAAGQKQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQ 172
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
481-647 |
7.63e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.82 E-value: 7.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 481 PDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcylhSQVVSVGQEPVLFSGSV 560
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA----ERGVVFQNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 RNNIAYGLQSCEDDKVMAAAQAahaddfiQEMehgiYTDVGEKGS------QLAAGQKQRLAIARALVRDPRVLILDEAT 634
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIA-------HQM----LKKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170
....*....|....
gi 73747917 635 SALDVQC-EQAKTL 647
Cdd:PRK11248 157 GALDAFTrEQMQTL 170
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
468-640 |
8.69e-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: 8.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpisqYEHCYLhsqvv 547
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----VKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 svgqepvlfsgsvrnniayglqsceddkvmaaaqaahaddfiqemehgiytdvgekgSQLAAGQKQRLAIARALVRDPRV 627
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170
....*....|...
gi 73747917 628 LILDEATSALDVQ 640
Cdd:cd03221 92 LLLDEPTNHLDLE 104
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
464-638 |
9.02e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.21 E-value: 9.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 464 LQGVVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLH 543
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQEP--VLFSGSVRNNIAYGLqscEDDKVMAAAQAAHADDFIQEMEHGIYTDvgEKGSQLAAGQKQRLAIARAL 621
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGM---ENQGIPREEMIKRVDEALLAVNMLDFKT--REPARLSGGQKQRVAVAGII 155
|
170
....*....|....*..
gi 73747917 622 VRDPRVLILDEATSALD 638
Cdd:PRK13642 156 ALRPEIIILDESTSMLD 172
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
468-638 |
1.00e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAY-PNRP-DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI-SQYEHCYLHS 544
Cdd:PRK13649 3 INLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVG-----QEPVLFSGSVRNNIAYGLQ----SCEDDKVMAAAQAAHAddfiqemehGIYTDVGEKGS-QLAAGQKQR 614
Cdd:PRK13649 83 IRKKVGlvfqfPESQLFEETVLKDVAFGPQnfgvSQEEAEALAREKLALV---------GISESLFEKNPfELSGGQMRR 153
|
170 180
....*....|....*....|....
gi 73747917 615 LAIARALVRDPRVLILDEATSALD 638
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLD 177
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
468-638 |
1.04e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.93 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNRPDRpvlkgLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEK-----PISQyehcyl 542
Cdd:PRK10771 2 LKLTDITWLYHHLPMR-----FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttPPSR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 hsQVVSV-GQEPVLFSG-SVRNNIAYG------LQSCEDDKVMAAAQAAHADDFIQEMEhgiytdvgekgSQLAAGQKQR 614
Cdd:PRK10771 71 --RPVSMlFQENNLFSHlTVAQNIGLGlnpglkLNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQR 137
|
170 180
....*....|....*....|....
gi 73747917 615 LAIARALVRDPRVLILDEATSALD 638
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
474-639 |
1.22e-15 |
|
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: 76.60 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 474 SFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQV-LLDEKPISQYEHcYLHSQVVSVGQE 552
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRKK-FLRRIGVVFGQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 553 -------PVLFSGSVRNNIaYGLQSCEDDKVMaaaqaahadDFIQEM---EHGIYTDVgekgSQLAAGQKQRLAIARALV 622
Cdd:cd03267 104 tqlwwdlPVIDSFYLLAAI-YDLPPARFKKRL---------DELSELldlEELLDTPV----RQLSLGQRMRAEIAAALL 169
|
170
....*....|....*..
gi 73747917 623 RDPRVLILDEATSALDV 639
Cdd:cd03267 170 HEPEILFLDEPTIGLDV 186
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
473-639 |
1.26e-15 |
|
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: 78.17 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 473 VSFAYPNRPdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQVLLDEKPIS-----QYEHcYLHS 544
Cdd:COG0444 9 VYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLklsekELRK-IRGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQE------PVLfsgSVRNNIAYGLQSCED-------DKVmaaaqaahaddfIQEMEH-GIYTDVGEKGS---QL 607
Cdd:COG0444 87 EIQMIFQDpmtslnPVM---TVGDQIAEPLRIHGGlskaearERA------------IELLERvGLPDPERRLDRyphEL 151
|
170 180 190
....*....|....*....|....*....|..
gi 73747917 608 AAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
213-427 |
1.32e-15 |
|
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: 77.84 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 213 CFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSD---------TTLMSNWLPLNAnvllrsLVKVVGLyg 283
Cdd:cd18554 69 FAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDveqtkdfitTGLMNIWLDMIT------IIIAICI-- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 284 fMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEvcryKEALEQCR 363
Cdd:cd18554 141 -MLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHE----QKQFDKRN 215
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 364 QLYWRRDLERALY-----LLVRRVLHLGvQMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLV 427
Cdd:cd18554 216 GHFLTRALKHTRWnaktfSAVNTITDLA-PLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLV 283
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
149-358 |
1.33e-15 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 77.88 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 149 LPLLVAAFFFLVLAVLGETLIPHYSGRVIDilggDFDPHAFASAIFFMCLFSFG-SSLSAGCRggcftYTMS-------- 219
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIID----DLLPSKNLRLILIIGAILLAlYILRTLLN-----YFVTywghvmga 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 220 RINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWL---PlnaNVLLRSLVKVVGLYGFMLSISPRLTLLS 296
Cdd:cd18549 72 RIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAhhgP---EDLFISIITIIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747917 297 LLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEA 358
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEG 210
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
146-414 |
1.42e-15 |
|
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: 77.63 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 146 RPDLPLLVAAFFflVLAVLGeTLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRI 225
Cdd:cd18782 1 RRALIEVLALSF--VVQLLG-LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 226 REQLFSSLLRQDLGFFQETKTGELNSRLsSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIA 305
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 306 AEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLVRRVLHL 385
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNK 236
|
250 260
....*....|....*....|....*....
gi 73747917 386 GVQMLMLSCGLQQMQDGELTQGSLLSFMI 414
Cdd:cd18782 237 LSSLLVLWVGAYLVLRGELTLGQLIAFRI 265
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
467-638 |
1.49e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 76.74 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ--------PTGGQVLLDEKPI--SQ 536
Cdd:PRK14239 5 ILQVSDLSVYYN---KKKALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIysPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 537 YEHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQ--SCEDDKVMaaaqaahaDDFIQEMEHG--IYTDVGEK----GSQLA 608
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRlkGIKDKQVL--------DEAVEKSLKGasIWDEVKDRlhdsALGLS 150
|
170 180 190
....*....|....*....|....*....|
gi 73747917 609 AGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
485-638 |
1.50e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLD-----EKPISQYEHCYlhsqvvsVGQEPVLFSG- 558
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvtHRSIQQRDICM-------VFQSYALFPHm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQsceddkvMAAAQAAHADDFIQE---------MEHGiYTDvgekgsQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:PRK11432 94 SLGENVGYGLK-------MLGVPKEERKQRVKEalelvdlagFEDR-YVD------QISGGQQQRVALARALILKPKVLL 159
|
....*....
gi 73747917 630 LDEATSALD 638
Cdd:PRK11432 160 FDEPLSNLD 168
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
460-638 |
1.86e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 78.35 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 460 APTTLQGVVKfqdvsfAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE- 538
Cdd:PRK11650 2 AGLKLQAVRK------SYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 539 ------------HCYLHSqvvsvgqepvlfsgSVRNNIAYGLQSCEDDKvmaaaqaAHADDFIQE----MEHGIYTDvgE 602
Cdd:PRK11650 74 adrdiamvfqnyALYPHM--------------SVRENMAYGLKIRGMPK-------AEIEERVAEaariLELEPLLD--R 130
|
170 180 190
....*....|....*....|....*....|....*.
gi 73747917 603 KGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK11650 131 KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
481-638 |
2.15e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 2.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 481 PDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYehcylhsqVVSVGQEPVLFSGSV 560
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY--------VPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 RNNIAYGL---------QSCEDDKVMaaaqaahaDDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILD 631
Cdd:NF040873 75 RDLVAMGRwarrglwrrLTRDDRAAV--------DDALERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
....*..
gi 73747917 632 EATSALD 638
Cdd:NF040873 145 EPTTGLD 151
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
454-638 |
2.43e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.95 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 454 PSPGTLAPTTlqgvVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQV-LLDEK 532
Cdd:PRK13536 32 SIPGSMSTVA----IDLAGVSKSYG---DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 533 PISQYEHCYLHSQVVS----VGQEpvlFsgSVRNNIA-----YGLQSCEDDKVMAAAQaahadDFIQeMEHGIYTDVgek 603
Cdd:PRK13536 105 VPARARLARARIGVVPqfdnLDLE---F--TVRENLLvfgryFGMSTREIEAVIPSLL-----EFAR-LESKADARV--- 170
|
170 180 190
....*....|....*....|....*....|....*
gi 73747917 604 gSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK13536 171 -SDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
480-640 |
2.90e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYlHSQVVSVGQ----EPVL 555
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHqpgiKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 556 fsgSVRNNIAY--GLQSCEDDkvmaaaqaahaDDFIQEMEHgiytdVGEKG------SQLAAGQKQRLAIARALVRDPRV 627
Cdd:PRK13538 90 ---TALENLRFyqRLHGPGDD-----------EALWEALAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPL 150
|
170
....*....|...
gi 73747917 628 LILDEATSALDVQ 640
Cdd:PRK13538 151 WILDEPFTAIDKQ 163
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
486-652 |
3.01e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVS-VGQE-PVLFSGSVRNN 563
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGiIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 564 IAYGLQSCE--------DDKVMAAAQAAHADDFiqemehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:PRK09700 101 LYIGRHLTKkvcgvniiDWREMRVRAAMMLLRV------GLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170
....*....|....*..
gi 73747917 636 ALdvqcEQAKTLWKFMI 652
Cdd:PRK09700 175 SL----TNKEVDYLFLI 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
485-638 |
3.22e-15 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPTGGQVLLDEKPISQYEHCYL---HSQVVSVGQEPvlFSG-- 558
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP--NSSln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 ---SVRNNIAYGLQSCEDDkvmaAAQAAHADDFIQEMEhgiytDVG-------EKGSQLAAGQKQRLAIARALVRDPRVL 628
Cdd:PRK15134 377 prlNVLQIIEEGLRVHQPT----LSAAQREQQVIAVME-----EVGldpetrhRYPAEFSGGQRQRIAIARALILKPSLI 447
|
170
....*....|
gi 73747917 629 ILDEATSALD 638
Cdd:PRK15134 448 ILDEPTSSLD 457
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
467-639 |
4.11e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 75.50 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYP-------------------NRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQ---NLYQPTG 524
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 525 GQVLLDEK---PISqyehcylhsqvVSVGQEPVLfsgSVRNNI-----AYGLQSCEDDKVMaaaqaahadDFIQEmehgi 596
Cdd:COG1134 81 GRVEVNGRvsaLLE-----------LGAGFHPEL---TGRENIylngrLLGLSRKEIDEKF---------DEIVE----- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 73747917 597 YTDVGEKGSQ----LAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG1134 133 FAELGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDA 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
482-639 |
4.82e-15 |
|
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: 74.10 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQVLLDEKPISQ---YEHCYLhsqvvsvG-----Q 551
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDlppEERARL-------GiflafQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 552 EPVLFSGsVRNNiayglqsceddkvmaaaqaahadDFIQEMehgiytDVGEKGsqlaaGQKQRLAIARALVRDPRVLILD 631
Cdd:cd03217 85 YPPEIPG-VKNA-----------------------DFLRYV------NEGFSG-----GEKKRNEILQLLLLEPDLAILD 129
|
....*...
gi 73747917 632 EATSALDV 639
Cdd:cd03217 130 EPDSGLDI 137
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
468-638 |
4.93e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 75.85 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAY-PNRP-DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLD-----EKPISQYEhc 540
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditDKKVKLSD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 541 yLHSQVVSVGQEP--VLFSGSVRNNIAYGLQSC--EDDKVmaaaqaahADDFIQEMEH-GI-YTDVGEKGS-QLAAGQKQ 613
Cdd:PRK13637 81 -IRKKVGLVFQYPeyQLFEETIEKDIAFGPINLglSEEEI--------ENRVKRAMNIvGLdYEDYKDKSPfELSGGQKR 151
|
170 180
....*....|....*....|....*
gi 73747917 614 RLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK13637 152 RVAIAGVVAMEPKILILDEPTAGLD 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
467-640 |
5.10e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYpnRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQV 546
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQEP--VLFSGSVRNNIAYGLQSCEDD------KVMAAAQAAHADDFIQEMEHgiytdvgekgsQLAAGQKQRLAIA 618
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDeetvahRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIA 149
|
170 180
....*....|....*....|..
gi 73747917 619 RALVRDPRVLILDEATSALDVQ 640
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQ 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
467-640 |
5.43e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpisqyehcylhsqv 546
Cdd:COG0488 315 VLELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET-------------- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVG---QEPVLFSG--SVRNNIAYGLQSCEDDKVMaaaqaahadDFIQEM----EhgiytDVGEKGSQLAAGQKQRLAI 617
Cdd:COG0488 378 VKIGyfdQHQEELDPdkTVLDELRDGAPGGTEQEVR---------GYLGRFlfsgD-----DAFKPVGVLSGGEKARLAL 443
|
170 180
....*....|....*....|...
gi 73747917 618 ARALVRDPRVLILDEATSALDVQ 640
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIE 466
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
486-640 |
5.55e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 74.33 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGqvlldEKPISQYehcylhsqvvSVGQEPvlfsGSVRNNIA 565
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-----RATVAGH----------DVVREP----REVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 566 Y---------GLQSCEDDKVMAAAQAAHADDFIQEMEHGI-YTDVGEKGSQLAA----GQKQRLAIARALVRDPRVLILD 631
Cdd:cd03265 77 IvfqdlsvddELTGWENLYIHARLYGVPGAERRERIDELLdFVGLLEAADRLVKtysgGMRRRLEIARSLVHRPEVLFLD 156
|
....*....
gi 73747917 632 EATSALDVQ 640
Cdd:cd03265 157 EPTIGLDPQ 165
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
491-640 |
6.33e-15 |
|
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: 76.68 E-value: 6.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 491 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI--SQYEHC---------YlhsqvvsVGQEPVLFSG- 558
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFlpphrrrigY-------VFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQSCEddkvmAAAQAAHADDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG4148 93 SVRGNLLYGRKRAP-----RAERRISFDEVVELL--GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
..
gi 73747917 639 VQ 640
Cdd:COG4148 166 LA 167
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
485-638 |
6.99e-15 |
|
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: 73.85 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIsQYEH------------CYLHSQVvsvgQE 552
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAArnrigylpeergLYPKMKV----ID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 553 PVLFSGSVRN-NIAYGLQSceddkvmaaaqaahADDFIQEMEHGIYTDvgEKGSQLAAGQKQRLAIARALVRDPRVLILD 631
Cdd:cd03269 90 QLVYLAQLKGlKKEEARRR--------------IDEWLERLELSEYAN--KRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
....*..
gi 73747917 632 EATSALD 638
Cdd:cd03269 154 EPFSGLD 160
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
481-640 |
8.09e-15 |
|
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: 73.90 E-value: 8.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 481 PDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQ----VVSVGQEPVLF 556
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 557 SGSVRNNIAYGLQSCEDDKVMAAAQAAHADDfIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSA 636
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDACSLQPD-IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
....
gi 73747917 637 LDVQ 640
Cdd:cd03290 171 LDIH 174
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
480-638 |
1.05e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY---EHCYLHSQVVSVGQEP--- 553
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraQRKAFRRDIQMVFQDSisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 554 VLFSGSVRNNIAYGLQSCEDdkVMAAAQAAHADDFIQEMEHGIyTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEA 633
Cdd:PRK10419 102 VNPRKTVREIIREPLRHLLS--LDKAERLARASEMLRAVDLDD-SVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
....*
gi 73747917 634 TSALD 638
Cdd:PRK10419 179 VSNLD 183
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
488-640 |
1.30e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.26 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 488 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY-EHCYLHSQVVSVGQEPVLFSG-------- 558
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHVRLFREmtvienll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 -----SVRNNIAYGL------QSCEDDKVMAAAQaahaddFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:PRK11300 103 vaqhqQLKTGLFSGLlktpafRRAESEALDRAAT------WLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170
....*....|...
gi 73747917 628 LILDEATSALDVQ 640
Cdd:PRK11300 175 LMLDEPAAGLNPK 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
467-638 |
1.47e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAY-PNRP-DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS----QYEHC 540
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 541 YLHSQVVSVGQEP--VLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIqemehGIYTDVGEKGS-QLAAGQKQRLAI 617
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSPfELSGGQMRRVAI 155
|
170 180
....*....|....*....|.
gi 73747917 618 ARALVRDPRVLILDEATSALD 638
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLD 176
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
480-651 |
1.57e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.00 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPV--LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCY---LHSQVVSVGQEPV 554
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 555 lfsGSV--RNNIAYGLQscEDDKVMAAAQAAHADDFIQEMehgiYTDVGEKGSQ-------LAAGQKQRLAIARALVRDP 625
Cdd:PRK11308 103 ---GSLnpRKKVGQILE--EPLLINTSLSAAERREKALAM----MAKVGLRPEHydryphmFSGGQRQRIAIARALMLDP 173
|
170 180
....*....|....*....|....*.
gi 73747917 626 RVLILDEATSALDVQCeQAKTLWKFM 651
Cdd:PRK11308 174 DVVVADEPVSALDVSV-QAQVLNLMM 198
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-638 |
1.72e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.31 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcyLHSQVvsvgqepvlfSGSVRNN- 563
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK-----LSSAA----------KAELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 564 IAYGLQ--------SCEDDKVMAAAQAAHADDFIQEMEHGIYTDVG------EKGSQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:PRK11629 89 LGFIYQfhhllpdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGlehranHRPSELSGGERQRVAIARALVNNPRLVL 168
|
....*....
gi 73747917 630 LDEATSALD 638
Cdd:PRK11629 169 ADEPTGNLD 177
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-638 |
6.72e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.87 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQVLLDEKPISQYEHCYLHSQVVSVGQEP-VLFSG 558
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQ--SCEDDKVMAAAQAAHADDFIQEMEHgIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSA 636
Cdd:PRK14247 98 SIFENVALGLKlnRLVKSKKELQERVRWALEKAQLWDE-VKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
..
gi 73747917 637 LD 638
Cdd:PRK14247 177 LD 178
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
456-638 |
6.78e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.02 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 456 PGTlaPTTLQGVVKfqdvSFAypnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS 535
Cdd:PRK11247 9 QGT--PLLLNAVSK----RYG-----ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 536 QyehcyLHSQVVSVGQEPVLFS-GSVRNNIAYGLQSceddkvmaaaqaAHADDFIQEMEH-GIYTDVGEKGSQLAAGQKQ 613
Cdd:PRK11247 78 E-----AREDTRLMFQDARLLPwKKVIDNVGLGLKG------------QWRDAALQALAAvGLADRANEWPAALSGGQKQ 140
|
170 180
....*....|....*....|....*
gi 73747917 614 RLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALD 165
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
480-638 |
8.43e-14 |
|
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: 75.37 E-value: 8.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLYQPTGgqvlldekpisqyeHCYLHSQVVSVGQEPVLFSG 558
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQSCEDDKVMAAAQAAHADDfIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:TIGR00957 714 SLRENILFGKALNEKYYQQVLEACALLPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
150-412 |
8.48e-14 |
|
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: 72.48 E-value: 8.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 150 PLLVAAFFF-LVLAVLGeTLIPHYSGRVID--ILGGDFDP-HAFASAIFFMCLFSFGSSLSagcRGGCFTYTMSRINLRI 225
Cdd:cd18570 2 KLLILILLLsLLITLLG-IAGSFFFQILIDdiIPSGDINLlNIISIGLILLYLFQSLLSYI---RSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 226 REQLFSSLLRQDLGFFQETKTGELNSRLS---------SDTTLmsnwlplnaNVLLRSLVKVVGLyGFMLSISPRLTLLS 296
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRFNdankireaiSSTTI---------SLFLDLLMVIISG-IILFFYNWKLFLIT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 297 LLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALY 376
Cdd:cd18570 148 LLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQ 227
|
250 260 270
....*....|....*....|....*....|....*.
gi 73747917 377 LLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSF 412
Cdd:cd18570 228 SSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAF 263
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
486-637 |
1.28e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQVLLDEKP-----ISQYEhcylHSQVVSVGQEPVLFS 557
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEElqasnIRDTE----RAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 558 G-SVRNNIAYGlqsCE-------DDKVMAAAQaahaddfiQEM--EHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:PRK13549 96 ElSVLENIFLG---NEitpggimDYDAMYLRA--------QKLlaQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170
....*....|
gi 73747917 628 LILDEATSAL 637
Cdd:PRK13549 165 LILDEPTASL 174
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
467-638 |
1.52e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 71.27 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPD---RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCY-L 542
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 HSQVVSVGQEP--VLFSGSVRNNIAYGlqsCEDDKVMAAAQAAHADDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARA 620
Cdd:PRK13633 84 RNKAGMVFQNPdnQIVATIVEEDVAFG---PENLGIPPEEIRERVDESLKKV--GMYEYRRHAPHLLSGGQKQRVAIAGI 158
|
170
....*....|....*...
gi 73747917 621 LVRDPRVLILDEATSALD 638
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLD 176
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
486-637 |
1.75e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIsQYEHCY--LHSQVVSVGQE----PVLfsgS 559
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTaaLAAGVAIIYQElhlvPEM---T 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73747917 560 VRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK11288 96 VAENLYLGQLPHKGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
467-638 |
1.78e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVL---LDEKPISQYEHCYLH 543
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQEPVLFSGSVRNNIAYG-----LQSCEDDKVMaaaqaahaDDFIQEMEHGIYTDVGEKgsQLAAGQKQRLAIA 618
Cdd:PRK13644 79 VGIVFQNPETQFVGRTVEEDLAFGpenlcLPPIEIRKRV--------DRALAEIGLEKYRHRSPK--TLSGGQGQCVALA 148
|
170 180
....*....|....*....|
gi 73747917 619 RALVRDPRVLILDEATSALD 638
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLD 168
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
470-632 |
1.84e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.47 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 470 FQDVSFAYPNRpdRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS---QYEHCYLHSQV 546
Cdd:PRK10522 325 LRNVTFAYQDN--GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeqPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSvgqEPVLFsgsvrnniayglqscedDKVMAAAQAAHADDFIQ------EMEHGIYTDVGE-KGSQLAAGQKQRLAIAR 619
Cdd:PRK10522 403 FT---DFHLF-----------------DQLLGPEGKPANPALVEkwlerlKMAHKLELEDGRiSNLKLSKGQKKRLALLL 462
|
170
....*....|...
gi 73747917 620 ALVRDPRVLILDE 632
Cdd:PRK10522 463 ALAEERDILLLDE 475
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
152-447 |
3.02e-13 |
|
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: 70.61 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 152 LVAAFFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFS 231
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 232 SLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLsllhMPFTIAAEKVYN 311
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV----LPPLLVVYYLLQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 312 TRHQEVLREIQ--DAVARAG--QVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWrrdleraLYLLVRRVLHLGV 387
Cdd:cd18580 157 RYYLRTSRQLRrlESESRSPlySHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFY-------LLLAVQRWLGLRL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 388 QML---------MLSCGLQQMQDGELTqGSLLSFMIyqeSVGSYVQTLVYIYGDMLSNVGAAEKVFSYM 447
Cdd:cd18580 230 DLLgallalvvaLLAVLLRSSISAGLV-GLALTYAL---SLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
450-640 |
3.11e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 73.23 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 450 QPNLPSpgtlapttlqgvVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTGGqvl 528
Cdd:PLN03130 609 EPGLPA------------ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDA--- 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 529 ldekpisqyeHCYLHSQVVSVGQEPVLFSGSVRNNIAYGLQScEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLA 608
Cdd:PLN03130 674 ----------SVVIRGTVAYVPQVSWIFNATVRDNILFGSPF-DPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNIS 742
|
170 180 190
....*....|....*....|....*....|..
gi 73747917 609 AGQKQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:PLN03130 743 GGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
192-397 |
4.52e-13 |
|
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: 70.25 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 192 AIFFMCLFSFGSSLSAgcrggcftytmsrinLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVL 271
Cdd:cd18605 59 TLLRAFLFAYGGLRAA---------------RRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNIL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 272 LRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYntRHQEvlREIQ--DAVARaGQV---VREAVGGLQTVRSFG 346
Cdd:cd18605 124 LAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRYY--RATS--RELKrlNSVNL-SPLythFSETLKGLVTIRAFR 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 73747917 347 AEEHEVCRYKEALEQCrqlywrrdlERALYLLVRRVLHLGVQMLMLSCGLQ 397
Cdd:cd18605 199 KQERFLKEYLEKLENN---------QRAQLASQAASQWLSIRLQLLGVLIV 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
467-638 |
5.28e-13 |
|
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: 69.00 E-value: 5.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnRPDRPV--LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYehcylhs 544
Cdd:COG4181 8 IIELRGLTKTVG-TGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 qvvsvGQEPVLfsgSVRN-NIAYGLQS---------CEDdkVMAAAQAAHADDFIQEMEHGIyTDVGEKG------SQLA 608
Cdd:COG4181 80 -----DEDARA---RLRArHVGFVFQSfqllptltaLEN--VMLPLELAGRRDARARARALL-ERVGLGHrldhypAQLS 148
|
170 180 190
....*....|....*....|....*....|
gi 73747917 609 AGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
468-638 |
5.52e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 69.34 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLhSQVV 547
Cdd:COG4604 2 IEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL-AKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SV-GQEPVLFSG-SVRNNIAYG--------LQScEDDKVMaaaqaahaDDFIQEME-HGI---YTDvgekgsQLAAGQKQ 613
Cdd:COG4604 78 AIlRQENHINSRlTVRELVAFGrfpyskgrLTA-EDREII--------DEAIAYLDlEDLadrYLD------ELSGGQRQ 142
|
170 180
....*....|....*....|....*
gi 73747917 614 RLAIARALVRDPRVLILDEATSALD 638
Cdd:COG4604 143 RAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
486-639 |
6.53e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.10 E-value: 6.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTGGQVLLDEKPISQYEH-------CYLHSQVVSVGQEPVLfsg 558
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAaelarhrAYLSQQQSPPFAMPVF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 svrNNIAYGLQSCEDDKVMAAAQAAHADDFiqemehGIYTDVGEKGSQLAAGQKQRLAIARALVR-------DPRVLILD 631
Cdd:COG4138 88 ---QYLALHQPAGASSEAVEQLLAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
....*...
gi 73747917 632 EATSALDV 639
Cdd:COG4138 159 EPMNSLDV 166
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
480-638 |
6.70e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 68.28 E-value: 6.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYQP--TGGQVLLDEKPISQyehcyLHSQVVSVG---QEP 553
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRRLTA-----LPAEQRRIGilfQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 554 VLFSG-SVRNNIAYGLQSceddkvmaAAQAAHADDFIQEMehgiYTDVGEKG------SQLAAGQKQRLAIARALVRDPR 626
Cdd:COG4136 86 LLFPHlSVGENLAFALPP--------TIGRAQRRARVEQA----LEEAGLAGfadrdpATLSGGQRARVALLRALLAEPR 153
|
170
....*....|..
gi 73747917 627 VLILDEATSALD 638
Cdd:COG4136 154 ALLLDEPFSKLD 165
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
185-638 |
7.61e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.32 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 185 DPhAFASAIFFMCLFsFGSSLSAGCRGGCFTYTMsRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWL 264
Cdd:PLN03232 335 DP-AWVGYVYAFLIF-FGVTFGVLCESQYFQNVG-RVGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANAL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 265 PLNANVL-------LRSLVKVVGLYGFMLSISPRLTLLSLLHMPFtiaaEKVYNTRHQEVLRE-IQDAVARAGqVVREAV 336
Cdd:PLN03232 412 QQIAEQLhglwsapFRIIVSMVLLYQQLGVASLFGSLILFLLIPL----QTLIVRKMRKLTKEgLQWTDKRVG-IINEIL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 337 GGLQTVRSFGAEEHEVCRYKEALEQcrQLYWRRDLERALYLLVRRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMiyq 416
Cdd:PLN03232 487 ASMDTVKCYAWEKSFESRIQGIRNE--ELSWFRKAQLLSAFNSFILNSIPVVVTLVSFGVFVLLGGDLTPARAFTSL--- 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 417 eSVGSYVQTLVYIYGDMLSNVGAA-------EKVFSYMDR--QPNLP-SPGTLApttlqgvVKFQDVSFAYPNRPDRPVL 486
Cdd:PLN03232 562 -SLFAVLRSPLNMLPNLLSQVVNAnvslqriEELLLSEERilAQNPPlQPGAPA-------ISIKNGYFSWDSKTSKPTL 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 487 KGLTFTLRPGEVTALVGPNGSGKSTVAAllqnlyqptggqVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSGSVRNNIAY 566
Cdd:PLN03232 634 SDINLEIPVGSLVAIVGGTGEGKTSLIS------------AMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILF 701
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747917 567 GlQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PLN03232 702 G-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
151-412 |
8.62e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 69.46 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 151 LLVAAFFF-LVLAVLGeTLIPHYSGRVID--ILGGDFDP-HAFASAIFFMCLFSFGSSLSagcRGGCFTYTMSRINLRIR 226
Cdd:cd18555 3 LLISILLLsLLLQLLT-LLIPILTQYVIDnvIVPGNLNLlNVLGIGILILFLLYGLFSFL---RGYIIIKLQTKLDKSLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 227 EQLFSSLLRQDLGFFQETKTGELNSRLSSDTT---LMSNwlplNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMpFT 303
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRANSNVYirqILSN----QVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 304 IAAEKVYNTRH-QEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHevcRYKEALE-QCRQLYWRRdlERALYLLVRR 381
Cdd:cd18555 154 IVLLLLLTRKKiKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKN---IYKKWENlFKKQLKAFK--KKERLSNILN 228
|
250 260 270
....*....|....*....|....*....|....*
gi 73747917 382 VLHLGVQ----MLMLSCGLQQMQDGELTQGSLLSF 412
Cdd:cd18555 229 SISSSIQfiapLLILWIGAYLVINGELTLGELIAF 263
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
202-369 |
1.37e-12 |
|
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: 69.23 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 202 GSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGl 281
Cdd:cd18558 71 IVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGT- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 282 yGFMLSISP--RLTLLSLLHMP-FTIAAEKVYNTRHQEVLREiQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEA 358
Cdd:cd18558 150 -GFIIGFIRgwKLTLVILAISPvLGLSAVVWAKILSGFTDKE-KKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQN 227
|
170
....*....|.
gi 73747917 359 LEQCRQLYWRR 369
Cdd:cd18558 228 LEIAKRNGIKK 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
483-640 |
1.90e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY--QPTGGQVLLDEKPISQyehcylhsqvvsvgQEPVLfsgsv 560
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------EASLI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 rNNIAyglqsceddkvmaaaqaaHADDFIQEMEhgIYTDVG--------EKGSQLAAGQKQRLAIARALVRDPRVLILDE 632
Cdd:COG2401 104 -DAIG------------------RKGDFKDAVE--LLNAVGlsdavlwlRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
....*...
gi 73747917 633 ATSALDVQ 640
Cdd:COG2401 163 FCSHLDRQ 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
483-639 |
2.22e-12 |
|
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: 65.92 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYehcylhsqvvsvgqepvlfsgSVRN 562
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR---------------------SPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 563 NIAYGLQsceddkvmaaaqaahaddFIQE--MEHGIYTD--VGEK---GSQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:cd03215 72 AIRAGIA------------------YVPEdrKREGLVLDlsVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
....
gi 73747917 636 ALDV 639
Cdd:cd03215 134 GVDV 137
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
484-638 |
2.59e-12 |
|
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: 66.69 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 484 PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDekpiSQYEHCYLHS----QVVSVGqepvlfsgs 559
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR----HDGGWVDLAQasprEILALR--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 560 vRNNIAYGLQ--------SCEDdKVMAAAqaahaddfiqeMEHGIYTDVG-EKGSQLAA------------------GQK 612
Cdd:COG4778 92 -RRTIGYVSQflrviprvSALD-VVAEPL-----------LERGVDREEArARARELLArlnlperlwdlppatfsgGEQ 158
|
170 180
....*....|....*....|....*.
gi 73747917 613 QRLAIARALVRDPRVLILDEATSALD 638
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLD 184
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-638 |
3.15e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.03 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 477 YPNRPD-RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY-EHcyLHSQVVS-VGQEP 553
Cdd:COG1101 12 NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpEY--KRAKYIGrVFQDP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 554 VL---FSGSVRNN--IAY------GLQSCEDDKVMaaaqaahadDFIQE--------MEHGIYTDVGekgsQLAAGQKQR 614
Cdd:COG1101 90 MMgtaPSMTIEENlaLAYrrgkrrGLRRGLTKKRR---------ELFREllatlglgLENRLDTKVG----LLSGGQRQA 156
|
170 180
....*....|....*....|....
gi 73747917 615 LAIARALVRDPRVLILDEATSALD 638
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALD 180
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
482-639 |
4.44e-12 |
|
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: 66.52 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQVLLDEKPISQYE-------HCYLHSQVvsvgqe 552
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpderaraGLFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 553 PVLFSG-SVRNNIAYGLQSCEDDKvmaAAQAAHADDFIQEMEHGI------------YTDVGEKGsqlaaGQKQRLAIAR 619
Cdd:TIGR01978 86 PEEIPGvSNLEFLRSALNARRSAR---GEEPLDLLDFEKLLKEKLalldmdeeflnrSVNEGFSG-----GEKKRNEILQ 157
|
170 180
....*....|....*....|
gi 73747917 620 ALVRDPRVLILDEATSALDV 639
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDI 177
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
486-638 |
6.96e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.75 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHS----QVVSVGQEPVLFSG-SV 560
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 561 RNNIAYGLQSC------EDDKVMAAAQAAHADDFiqemEHGiYTDvgekgsQLAAGQKQRLAIARALVRDPRVLILDEAT 634
Cdd:PRK10070 124 LDNTAFGMELAginaeeRREKALDALRQVGLENY----AHS-YPD------ELSGGMRQRVGLARALAINPDILLMDEAF 192
|
....
gi 73747917 635 SALD 638
Cdd:PRK10070 193 SALD 196
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
468-647 |
7.94e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.34 E-value: 7.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPN-RP-DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI-SQYEHCYLHS 544
Cdd:PRK13646 3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQ-----EPVLFSGSVRNNIAYGLQSCEDDkvmaaAQAAHADDFIQEMEHGIYTDVGEKGS-QLAAGQKQRLAIA 618
Cdd:PRK13646 83 VRKRIGMvfqfpESQLFEDTVEREIIFGPKNFKMN-----LDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 73747917 619 RALVRDPRVLILDEATSALD-------------VQCEQAKTL 647
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDpqskrqvmrllksLQTDENKTI 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
483-638 |
1.24e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE-HCYLHSQVVSVGQEPVLFSG-SV 560
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 73747917 561 RNNIAYGLQSCEDdkVMAAAQAAHADDFIQEMEHGIYTDvgEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK10895 96 YDNLMAVLQIRDD--LSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
495-643 |
1.29e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.78 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 495 PGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVlldekpisqyehcylhsqvvsvgqepVLFSGSvrnniayglqscedd 574
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGE--------------- 39
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 575 kvmaaaqaahaDDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQ 643
Cdd:smart00382 40 -----------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEA 97
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
484-643 |
1.52e-11 |
|
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: 65.65 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 484 PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLldekpisqyehcylHSQVVSV-GQEPVLFSGSVRN 562
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--------------HSGRISFsSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 563 NIAYGLqSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCE 642
Cdd:cd03291 117 NIIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
.
gi 73747917 643 Q 643
Cdd:cd03291 196 K 196
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
467-638 |
1.66e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.19 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PTG---GQVLLDEKPI--SQYEH 539
Cdd:PRK14243 10 VLRTENLNVYYGSFL---AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 540 CYLHSQVVSVGQEPVLFSGSVRNNIAYG-----LQSCEDDKVMAAAQAAHADDFIQEmehgiytDVGEKGSQLAAGQKQR 614
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGaringYKGDMDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQR 159
|
170 180
....*....|....*....|....
gi 73747917 615 LAIARALVRDPRVLILDEATSALD 638
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALD 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
484-643 |
2.22e-11 |
|
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: 67.24 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 484 PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLldekpisqyehcylHSQVVSVG-QEPVLFSGSVRN 562
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--------------HSGRISFSpQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 563 NIAYGLqSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCE 642
Cdd:TIGR01271 506 NIIFGL-SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
.
gi 73747917 643 Q 643
Cdd:TIGR01271 585 K 585
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
481-647 |
2.56e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 481 PDRPVLKGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNL---YQPTGGQVLLDEKPISQyehCYLHSQVVS-VGQEPVL 555
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAP---CALRGRKIAtIMQNPRS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 556 FSGSVRNNIAYGLQSCE------DDKVMaaaqaahaddfIQEMEhgiytDVGEKGS---------QLAAGQKQRLAIARA 620
Cdd:PRK10418 91 AFNPLHTMHTHARETCLalgkpaDDATL-----------TAALE-----AVGLENAarvlklypfEMSGGMLQRMMIALA 154
|
170 180
....*....|....*....|....*..
gi 73747917 621 LVRDPRVLILDEATSALDVqCEQAKTL 647
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDV-VAQARIL 180
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
482-639 |
4.58e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVG-QEPVLFSG 558
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAfQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 sVRNNiaYGLQSCEdDKVMAAAQAAHAD-----DFIQE------MEHGIYT---DVGEKGsqlaaGQKQRLAIARALVRD 624
Cdd:PRK09580 93 -VSNQ--FFLQTAL-NAVRSYRGQEPLDrfdfqDLMEEkiallkMPEDLLTrsvNVGFSG-----GEKKRNDILQMAVLE 163
|
170
....*....|....*
gi 73747917 625 PRVLILDEATSALDV 639
Cdd:PRK09580 164 PELCILDESDSGLDI 178
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
465-640 |
5.37e-11 |
|
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: 62.26 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 465 QGVVKFQDVSFAYP-NRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQPT-----GGQVLLDEKPISQY- 537
Cdd:cd03232 1 GSVLTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDKNf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 538 -------EHCYLHSQVVSVgQEPVLFSGSVRNniayglqsceddkvmaaaqaahaddfiqemehgiytdvgekgsqLAAG 610
Cdd:cd03232 78 qrstgyvEQQDVHSPNLTV-REALRFSALLRG--------------------------------------------LSVE 112
|
170 180 190
....*....|....*....|....*....|
gi 73747917 611 QKQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:cd03232 113 QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
437-650 |
6.38e-11 |
|
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: 65.54 E-value: 6.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 437 VGAAEKVFSYMDRQPNLPSPGTLAPTtlQGVVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALL 516
Cdd:TIGR00954 423 VEEIESGREGGRNSNLVPGRGIVEYQ--DNGIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 517 QNLYQPTGGQVLLDEKpisqyehcylhSQVVSVGQEPVLFSGSVRNNIAYGlQSCED-------DKVMAAAQAAHADDFI 589
Cdd:TIGR00954 499 GELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYP-DSSEDmkrrglsDKDLEQILDNVQLTHI 566
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 590 QEMEHGiYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQA------------------KTLWKF 650
Cdd:TIGR00954 567 LEREGG-WSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYmyrlcrefgitlfsvshrKSLWKY 644
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
463-637 |
6.62e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.23 E-value: 6.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 463 TLQGVVK-FQDVSfaypnrpdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQVLLDEKP----- 533
Cdd:TIGR02633 3 EMKGIVKtFGGVK----------ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPlkasn 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 534 ISQYEhcylHSQVVSVGQEPVLFSG-SVRNNIAYGLQSCEDDKVMAAAQAAH-ADDFIQEMEHGIyTDVGEKGSQLAAGQ 611
Cdd:TIGR02633 72 IRDTE----RAGIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLrAKNLLRELQLDA-DNVTRPVGDYGGGQ 146
|
170 180
....*....|....*....|....*.
gi 73747917 612 KQRLAIARALVRDPRVLILDEATSAL 637
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSL 172
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
471-638 |
7.06e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPNRPDR-PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQ--------VLLDEKP-------- 533
Cdd:PRK10535 8 KDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrvagqdvATLDADAlaqlrreh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 534 ---ISQYEHCYLH---SQVVSVgqePVLFSGSVRNniayglqsceddkvmaaAQAAHADDFIQEMehGIYTDVGEKGSQL 607
Cdd:PRK10535 88 fgfIFQRYHLLSHltaAQNVEV---PAVYAGLERK-----------------QRLLRAQELLQRL--GLEDRVEYQPSQL 145
|
170 180 190
....*....|....*....|....*....|.
gi 73747917 608 AAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK10535 146 SGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
472-639 |
8.83e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 472 DVSFAYPNR---PDRPVL--KGLT---------FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqy 537
Cdd:COG1129 240 ELEDLFPKRaaaPGEVVLevEGLSvggvvrdvsFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-- 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 538 ehcylhsqVVSVGQepvlfsgSVRNNIAY--------GL---QSCED-------DKVMAAAQ------AAHADDFIQEME 593
Cdd:COG1129 318 --------IRSPRD-------AIRAGIAYvpedrkgeGLvldLSIREnitlaslDRLSRGGLldrrreRALAEEYIKRLR 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 73747917 594 ---HGIYTDVGekgsQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG1129 383 iktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
467-638 |
1.05e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 64.44 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNrPDRPVLK---GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQV---LLDE-----KP-- 533
Cdd:TIGR03269 279 IIKVRNVSKRYIS-VDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEwvdmtKPgp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 534 -----ISQYEHcYLHsqvvsvgQEPVLFS-GSVRNNI--AYGLQSCEDDKVMAAAQAAHADDFIQEMEHGI---YTDvge 602
Cdd:TIGR03269 358 dgrgrAKRYIG-ILH-------QEYDLYPhRTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAEEIldkYPD--- 426
|
170 180 190
....*....|....*....|....*....|....*.
gi 73747917 603 kgsQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:TIGR03269 427 ---ELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
155-409 |
1.16e-10 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 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.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 62.90 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDILGGDfDPHAFASAIFFM---CLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFS 231
Cdd:cd18582 1 ALLLLVLAKLLNVAVPFLLKYAVDALSAP-ASALLAVPLLLLlayGLARILSSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 232 SLLRQDLGFFQETKTGELNSRLSSDT--------TLMSNWLPLNANVLLRSLVkVVGLYGFMLSIsprLTLLSL-LHMPF 302
Cdd:cd18582 80 HLHSLSLRFHLSRKTGALSRAIERGTrgiefllrFLLFNILPTILELLLVCGI-LWYLYGWSYAL---ITLVTVaLYVAF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 303 TIaaekVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQcrqlyWRRDLERALYLLVrrV 382
Cdd:cd18582 156 TI----KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAK-----YEKAAVKSQTSLA--L 224
|
250 260 270
....*....|....*....|....*....|....*
gi 73747917 383 LHLGvQMLMLSCGL--------QQMQDGELTQGSL 409
Cdd:cd18582 225 LNIG-QALIISLGLtaimllaaQGVVAGTLTVGDF 258
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
389-638 |
1.46e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 389 MLMLSCGlqqmQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKVfsyMDRQPNLPSPGTLAPTTLQGVV 468
Cdd:PTZ00243 602 LRMLCCE----QCRPTKRHPSPSVVVEDTDYGSPSSASRHIVEGGTGGGHEATPT---SERSAKTPKMKTDDFFELEPKV 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 469 KFQDVSFAYPNrpdrpvlkgltftlrpGEVTALVGPNGSGKSTvaaLLQNL---YQPTGGQVLLdEKPISQyehcylhsq 545
Cdd:PTZ00243 675 LLRDVSVSVPR----------------GKLTVVLGATGSGKST---LLQSLlsqFEISEGRVWA-ERSIAY--------- 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 vvsVGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDfIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDP 625
Cdd:PTZ00243 726 ---VPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANR 801
|
250
....*....|...
gi 73747917 626 RVLILDEATSALD 638
Cdd:PTZ00243 802 DVYLLDDPLSALD 814
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
482-639 |
1.67e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLH---SQVVSVGQEPVLFSG 558
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYldtTLPLTVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQSCEDDKVMAaaqaahaddfiQEMEhgiytdvgekgsQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK09544 96 TKKEDILPALKRVQAGHLID-----------APMQ------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
.
gi 73747917 639 V 639
Cdd:PRK09544 153 V 153
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
482-640 |
1.67e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQP------TGGQVLLDEKP-------ISQY-EHCYLHSQVV 547
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERvttgviTGGDRLVNGRPldssfqrSIGYvQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVgQEPVLFSGSVRNNIAYGLQSCED--DKVMAaaqaahaddfIQEMEHgiYTD--VGEKGSQLAAGQKQRLAIARALVR 623
Cdd:TIGR00956 852 TV-RESLRFSAYLRQPKSVSKSEKMEyvEEVIK----------LLEMES--YADavVGVPGEGLNVEQRKRLTIGVELVA 918
|
170
....*....|....*...
gi 73747917 624 DPRVLI-LDEATSALDVQ 640
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQ 936
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
151-443 |
1.84e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 62.50 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 151 LLVAAFFFLVLAVLgETLIPHYSGRVID--ILGGDFD--PHAFASAIFFMCLFSFGSSLSAGCRGGCFTYtmsrINLRIR 226
Cdd:cd18540 4 LILLIILMLLVALL-DAVFPLLTKYAIDhfITPGTLDglTGFILLYLGLILIQALSVFLFIRLAGKIEMG----VSYDLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 227 EQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAA 306
Cdd:cd18540 79 KKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 307 EKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEvcrYKEALEQCRQLY---WRRDLERALYLLVrrVL 383
Cdd:cd18540 159 SIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKN---LREFKELTEEMRrasVRAARLSALFLPI--VL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73747917 384 HLG--VQMLMLSCGLQQMQDGELTQGSLLSFMIYqeSVGSY--VQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18540 234 FLGsiATALVLWYGGILVLAGAITIGTLVAFISY--ATQFFepIQQLARVLAELQSAQASAERV 295
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
483-652 |
2.52e-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: 63.88 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehcYLHSQVVSVGQEPvlfsgsvRN 562
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCP-------QH 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 563 NIAYGLQSCEDDKVMAAAQAAHADDFIQ-EMEH-----GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSA 636
Cdd:TIGR01257 1012 NILFHHLTVAEHILFYAQLKGRSWEEAQlEMEAmledtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSG 1091
|
170
....*....|....*.
gi 73747917 637 LDVQCEqaKTLWKFMI 652
Cdd:TIGR01257 1092 VDPYSR--RSIWDLLL 1105
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
468-638 |
2.73e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.77 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAY-PNRP-DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI----SQYEHCY 541
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 542 LHSQVVSVGQ--EPVLFSGSVRNNIAYGLQS--CEDDKVMAAAQaahadDFIQEMehGIYTDVGEKGS-QLAAGQKQRLA 616
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180
....*....|....*....|..
gi 73747917 617 IARALVRDPRVLILDEATSALD 638
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLD 177
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
468-638 |
3.22e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCylHSQVV 547
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVGQEPVLFSG-SVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQeMEHGIytdvGEKGSQLAAGQKQRLAIARALVRDPR 626
Cdd:PRK11000 79 MVFQSYALYPHlSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQ-LAHLL----DRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170
....*....|..
gi 73747917 627 VLILDEATSALD 638
Cdd:PRK11000 154 VFLLDEPLSNLD 165
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
480-638 |
3.23e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 63.14 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlYQPTG----GQVLLDEKPISQYEH----CYLHSQVVSVG- 550
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPIDAKEMraisAYVQQDDLFIPt 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 ---QEPVLFSGSVR--------------NNI--AYGLQSCEDDKVmaaaqaahaddfiqemehGIYTDVgeKGsqLAAGQ 611
Cdd:TIGR00955 114 ltvREHLMFQAHLRmprrvtkkekrervDEVlqALGLRKCANTRI------------------GVPGRV--KG--LSGGE 171
|
170 180
....*....|....*....|....*..
gi 73747917 612 KQRLAIARALVRDPRVLILDEATSALD 638
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
485-638 |
3.30e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.14 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS-------------QYEHCYLHSQVVSVGQ 551
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 552 EPVLFSG-SVRNNI------AYGLQSCE-DDKVMAAAQAAHADDFIQemehgiytdvGEKGSQLAAGQKQRLAIARALVR 623
Cdd:PRK10619 100 HFNLWSHmTVLENVmeapiqVLGLSKQEaRERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAM 169
|
170
....*....|....*
gi 73747917 624 DPRVLILDEATSALD 638
Cdd:PRK10619 170 EPEVLLFDEPTSALD 184
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
482-640 |
3.84e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqptGGQVLLDEKPIsQYEHcylhSQVVSVGQE--PVLFSGS 559
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRI-IYEQ----DLIVARLQQdpPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 560 VRNNIAYGLQSCED-----------------DKVMAAAQAA----------HADDFIQEMEHGIYTDVGEKGSQLAAGQK 612
Cdd:PRK11147 83 VYDFVAEGIEEQAEylkryhdishlvetdpsEKNLNELAKLqeqldhhnlwQLENRINEVLAQLGLDPDAALSSLSGGWL 162
|
170 180
....*....|....*....|....*...
gi 73747917 613 QRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIE 190
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
474-638 |
4.16e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.97 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 474 SFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG---GQVLLDEKPISQYEHCYlHSQVVSVG 550
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 QE----PVLfsgSVRNNIAYGLQSCEDDKVmaaaqaahaddfiqemehgiytdvgeKGsqLAAGQKQRLAIARALVRDPR 626
Cdd:cd03233 90 EEdvhfPTL---TVRETLDFALRCKGNEFV--------------------------RG--ISGGERKRVSIAEALVSRAS 138
|
170
....*....|..
gi 73747917 627 VLILDEATSALD 638
Cdd:cd03233 139 VLCWDNSTRGLD 150
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
486-637 |
6.99e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI---SQYEHcyLHSQVVSVGQE-PVLFSGSVR 561
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEA--LENGISMVHQElNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 562 NNIAYGLQSCE----DDKVMAAAQAAHADDFiqemehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK10982 92 DNMWLGRYPTKgmfvDQDKMYRDTKAIFDEL------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
451-639 |
8.91e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 8.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 451 PNLPSPGTLAPTTLQGVV-------KFQDVSFAYP------NRPDRPV--LKGLTFTLRPGEVTALVGPNGSGKSTVAAL 515
Cdd:PRK10261 290 ISLEHPAKQEPPIEQDTVvdgepilQVRNLVTRFPlrsgllNRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRA 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 516 LQNLYQPTGGQVLLDEKPISQYEHCYLHS---QVVSVGQEPVLfSGSVRNNIAYGLQscEDDKVmaaaQAAHADDFIQEM 592
Cdd:PRK10261 370 LLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrDIQFIFQDPYA-SLDPRQTVGDSIM--EPLRV----HGLLPGKAAAAR 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 73747917 593 EHGIYTDVGEKGS-------QLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK10261 443 VAWLLERVGLLPEhawryphEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
489-639 |
9.23e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 489 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTGGQVLLDEKPISQYEH-------CYLHSQVVSVGQEPV-----LF 556
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaelarhrAYLSQQQTPPFAMPVfqyltLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 557 SGSvrnniayGLQSCEDDKVMAAAQAAHA-DDFIQEMEHgiytdvgekgsQLAAGQKQR-------LAIARALVRDPRVL 628
Cdd:PRK03695 94 QPD-------KTRTEAVASALNEVAEALGlDDKLGRSVN-----------QLSGGEWQRvrlaavvLQVWPDINPAGQLL 155
|
170
....*....|.
gi 73747917 629 ILDEATSALDV 639
Cdd:PRK03695 156 LLDEPMNSLDV 166
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
146-412 |
1.11e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 59.87 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 146 RPDLPLLVAAFFFLVLAVLgetLIPHYSGRVID--ILGGDFDPHA-FASAIFFMCLFSFGSSLsagCRGGCFTYTMSRIN 222
Cdd:cd18779 1 PGLLGQILLASLLLQLLGL---ALPLLTGVLVDrvIPRGDRDLLGvLGLGLAALVLTQLLAGL---LRSHLLLRLRTRLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 223 LRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTT---LMSNwlPLNANVLLRSLvkVVGLYGFMLSISPRLTLLSLLH 299
Cdd:cd18779 75 TQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATireLLTS--QTLSALLDGTL--VLGYLALLFAQSPLLGLVVLGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 300 MPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRRDLERALYLLV 379
Cdd:cd18779 151 AALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDAL 230
|
250 260 270
....*....|....*....|....*....|...
gi 73747917 380 RRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSF 412
Cdd:cd18779 231 LATLRLAAPLVLLWVGAWQVLDGQLSLGTMLAL 263
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
485-638 |
1.28e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLL-----------DEKPISQyehcyLHSQVVSVGQE- 552
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnhfdfsktpSDKAIRE-----LRRNVGMVFQQy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 553 ---PVLfsgSVRNNI------AYGLQSCE-DDKVMAAAQAAHADDFIQEMEhgiytdvgekgSQLAAGQKQRLAIARALV 622
Cdd:PRK11124 92 nlwPHL---TVQQNLieapcrVLGLSKDQaLARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALM 157
|
170
....*....|....*.
gi 73747917 623 RDPRVLILDEATSALD 638
Cdd:PRK11124 158 MEPQVLLFDEPTAALD 173
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
492-643 |
1.49e-09 |
|
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: 58.96 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 492 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqYEHCYLHSQvvsvgqepvlFSGSVRnniaYGLQSC 571
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD----------YEGTVR----DLLSSI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747917 572 EDDKVMAAAQAAHADDFIQeMEHGIYTDVGEkgsqLAAGQKQRLAIARALVRDPRVLILDEATSALDVqcEQ 643
Cdd:cd03237 86 TKDFYTHPYFKTEIAKPLQ-IEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQ 150
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
485-639 |
2.40e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.46 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQEPVLFSG-SVRNN 563
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 73747917 564 IAYGLQSCEddKVMAAAQAAHADDFIQEMEH-GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK10253 102 VARGRYPHQ--PLFTRWRKEDEEAVTKAMQAtGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
473-639 |
2.53e-09 |
|
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: 60.08 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 473 VSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQP---TGGQVLLDEKPI---SQYEHCYLHSQ 545
Cdd:COG4172 14 VAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLlglSERELRRIRGN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 546 VVS-VGQEPV-----LFSgsVRNNIAYGLQ-----SCED---------DKVMaaaqaahaddfIQEME-------Hgiyt 598
Cdd:COG4172 93 RIAmIFQEPMtslnpLHT--IGKQIAEVLRlhrglSGAAararalellERVG-----------IPDPErrldaypH---- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 73747917 599 dvgekgsQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:COG4172 156 -------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDV 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
482-640 |
3.24e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTGGQVLLD----------EKPISQYEHC-----YLHS 544
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyvERPSKVGEPCpvcggTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPVLFSGSVRNNIAYGLQSC----EDDKVMAAAQAAHAD-------------DFIQE--MEHGIyTDVGEkgs 605
Cdd:TIGR03269 92 EEVDFWNLSDKLRRRIRKRIAIMLQRTfalyGDDTVLDNVLEALEEigyegkeavgravDLIEMvqLSHRI-THIAR--- 167
|
170 180 190
....*....|....*....|....*....|....*
gi 73747917 606 QLAAGQKQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
467-644 |
3.24e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPdrPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEK----PISQYehcyl 542
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKvrmaVFSQH----- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 HSQVVSVGQEPVL-----FSGSVRNNIAYGLQSceddkvmaaaQAAHADDFIQEMehgiYTdvgekgsqLAAGQKQRLAI 617
Cdd:PLN03073 581 HVDGLDLSSNPLLymmrcFPGVPEQKLRAHLGS----------FGVTGNLALQPM----YT--------LSGGQKSRVAF 638
|
170 180
....*....|....*....|....*..
gi 73747917 618 ARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAVEA 665
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
485-637 |
3.50e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHSQVVSVGQE--PVLFSGSVRN 562
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEgrRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 563 NIAYGLQSCEDDKvmaaaqaahaddFIQEME--HGIYTDVGEKGSQ----LAAGQKQRLAIARALVRDPRVLILDEATSA 636
Cdd:PRK11614 100 NLAMGGFFAERDQ------------FQERIKwvYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
.
gi 73747917 637 L 637
Cdd:PRK11614 168 L 168
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
482-639 |
3.60e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQN--LYQPTGGQVLLDEKPISQYE-HCYLHSQVVSVGQEPVLFSG 558
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 sVRN----NIAYG-----LQSCEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSqlaAGQKQRLAIARALVRDPRVLI 629
Cdd:CHL00131 99 -VSNadflRLAYNskrkfQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEGFS---GGEKKRNEILQMALLDSELAI 174
|
170
....*....|
gi 73747917 630 LDEATSALDV 639
Cdd:CHL00131 175 LDETDSGLDI 184
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
492-651 |
4.54e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 492 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpISqYEHCYL-HSQVVSVG----QEPVLFSGS-VRNNIA 565
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-IS-YKPQYIkPDYDGTVEdllrSITDDLGSSyYKSEII 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 566 YGLQsceddkvmaaaqaahaddfIQE-MEHgiytDVGEkgsqLAAGQKQRLAIARALVRDPRVLILDEATSALDVqcEQ- 643
Cdd:PRK13409 439 KPLQ-------------------LERlLDK----NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQr 489
|
170
....*....|.
gi 73747917 644 ---AKTLWKFM 651
Cdd:PRK13409 490 lavAKAIRRIA 500
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
480-647 |
4.59e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVL---------------LDEKPISQYEHCYlHS 544
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvieLSEQSAAQMRHVR-GA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQEPV-----LFsgSVRNNIAYGL---QSCEDDKVMAAAQAAHADDFIQEMEhgiyTDVGEKGSQLAAGQKQRLA 616
Cdd:PRK10261 105 DMAMIFQEPMtslnpVF--TVGEQIAESIrlhQGASREEAMVEAKRMLDQVRIPEAQ----TILSRYPHQLSGGMRQRVM 178
|
170 180 190
....*....|....*....|....*....|.
gi 73747917 617 IARALVRDPRVLILDEATSALDVQCeQAKTL 647
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTI-QAQIL 208
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
485-638 |
4.65e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.86 E-value: 4.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlyQPTGGQVLLDEK------------PISQY-EHCYLHSQVVSVgQ 551
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRisgfpkkqetfaRISGYcEQNDIHSPQVTV-R 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 552 EPVLFSGSVRNNIAYGlqscEDDKVMaaaqaahaddFIQEMEHGIYTD------VGEKG-SQLAAGQKQRLAIARALVRD 624
Cdd:PLN03140 972 ESLIYSAFLRLPKEVS----KEEKMM----------FVDEVMELVELDnlkdaiVGLPGvTGLSTEQRKRLTIAVELVAN 1037
|
170
....*....|....
gi 73747917 625 PRVLILDEATSALD 638
Cdd:PLN03140 1038 PSIIFMDEPTSGLD 1051
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
480-640 |
4.69e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.78 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCylhSQVVSVGQEPVLFSG- 558
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGLKADl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAY--GLQSCEDdkvmaaaqaahaddfiQEMEHGIYTDVGEKG------SQLAAGQKQRLAIARALVRDPRVLIL 630
Cdd:PRK13543 98 STLENLHFlcGLHGRRA----------------KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170
....*....|
gi 73747917 631 DEATSALDVQ 640
Cdd:PRK13543 162 DEPYANLDLE 171
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
481-639 |
4.98e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.38 E-value: 4.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 481 PDRPVLKGLTfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQvlLDEKP-----ISQYEHCYLH---SQVVS---- 548
Cdd:cd03236 12 PNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQnyfTKLLEgdvk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 -------VGQEPVLFSGSVRNNIayglqSCEDDKVMAaaqaahaDDFIQEMEhgIYTDVGEKGSQLAAGQKQRLAIARAL 621
Cdd:cd03236 89 vivkpqyVDLIPKAVKGKVGELL-----KKKDERGKL-------DELVDQLE--LRHVLDRNIDQLSGGELQRVAIAAAL 154
|
170
....*....|....*...
gi 73747917 622 VRDPRVLILDEATSALDV 639
Cdd:cd03236 155 ARDADFYFFDEPSSYLDI 172
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
463-643 |
5.96e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.71 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 463 TLQGVVKFQDVSFAYPNRP--DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDE-------KP 533
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 534 ISQYEHcyLHSQVVSVGQEP--VLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHgiYtdVGEKGSQLAAGQ 611
Cdd:PRK13645 82 IKEVKR--LRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPED--Y--VKRSPFELSGGQ 155
|
170 180 190
....*....|....*....|....*....|..
gi 73747917 612 KQRLAIARALVRDPRVLILDEATSALDVQCEQ 643
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEE 187
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
467-644 |
6.17e-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: 58.79 E-value: 6.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpisqyehcylhSQV 546
Cdd:TIGR03719 322 VIEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-----------VKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQ--EPVLFSGSVRNNIAYGLqsceddkvmaaaqaahadDFIQ----EMEHGIY--------TDVGEKGSQLAAGQK 612
Cdd:TIGR03719 388 AYVDQsrDALDPNKTVWEEISGGL------------------DIIKlgkrEIPSRAYvgrfnfkgSDQQKKVGQLSGGER 449
|
170 180 190
....*....|....*....|....*....|..
gi 73747917 613 QRLAIARALVRDPRVLILDEATSALDVQCEQA 644
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRA 481
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
159-443 |
7.73e-09 |
|
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: 57.57 E-value: 7.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 159 LVLAVLGeTLIPHYSGRVID--ILGGDFDP-HAFasaIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLR 235
Cdd:cd18568 12 LLLQLLG-LALPLFTQIILDrvLVHKNISLlNLI---LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 236 QDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVKVVGLyGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQ 315
Cdd:cd18568 88 LPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYL-GLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 316 EVLREIQDAVARAGQVVREAVGGLQTVRSFGAEehevcrykealeqcRQLYWRRDLERALYLLVR---RVLHLGVQML-- 390
Cdd:cd18568 167 RNSREIFQANAEQQSFLVEALTGIATIKALAAE--------------RPIRWRWENKFAKALNTRfrgQKLSIVLQLIss 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 73747917 391 ---------MLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18568 233 linhlgtiaVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-638 |
9.68e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 483 RPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGG-----QVLLDEKPISQYEHCY-LHSQVVSVGQEPVLF 556
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 557 SGSVRNNIAYGLQScedDKVMAAAQAAHADDfIQEMEHGIYTDVGEKGS----QLAAGQKQRLAIARALVRDPRVLILDE 632
Cdd:PRK14271 114 PMSIMDNVLAGVRA---HKLVPRKEFRGVAQ-ARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
....*.
gi 73747917 633 ATSALD 638
Cdd:PRK14271 190 PTSALD 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
482-638 |
1.08e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG--------------GQVLLDEKPISQYEHCYLHSQV- 546
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGysndltlfgrrrgsGETIWDIKKHIGYVSSSLHLDYr 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVgqepvlfsgSVRNNIAYGLQsceddkvmaaaqaahadDFIqemehGIYTDVGEKGSQLAA----------------- 609
Cdd:PRK10938 351 VST---------SVRNVILSGFF-----------------DSI-----GIYQAVSDRQQKLAQqwldilgidkrtadapf 399
|
170 180 190
....*....|....*....|....*....|....*
gi 73747917 610 -----GQkQRLA-IARALVRDPRVLILDEATSALD 638
Cdd:PRK10938 400 hslswGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
492-639 |
1.35e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 492 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVllDEKP-----ISQYE----HCYLhSQVVS-----------VGQ 551
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRgtelQDYF-KKLANgeikvahkpqyVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 552 EPVLFSGSVRNniaygLQSCEDDKvmaaaqaAHADDFIQE--MEHGIYTDVGEkgsqLAAGQKQRLAIARALVRDPRVLI 629
Cdd:COG1245 172 IPKVFKGTVRE-----LLEKVDER-------GKLDELAEKlgLENILDRDISE----LSGGELQRVAIAAALLRDADFYF 235
|
170
....*....|
gi 73747917 630 LDEATSALDV 639
Cdd:COG1245 236 FDEPSSYLDI 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
482-638 |
1.36e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyEHCYLHSQVVSVGQE----PVLfs 557
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRsginPYL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 558 gSVRNNIAYGLQSCEDDkvmaaaqaAHADDFIQEMEHGIYTDVgeKGSQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK13540 90 -TLRENCLYDIHFSPGA--------VGITELCRLFSLEHLIDY--PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
.
gi 73747917 638 D 638
Cdd:PRK13540 159 D 159
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
467-632 |
1.98e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.93 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAypnRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHCYLHS-- 544
Cdd:PRK11831 7 LVDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 -QVVSVGQEPVLFSG-SVRNNIAYGLQSceddkvmaaaQAAHADDFIQEMEHGIYTDVGEKG------SQLAAGQKQRLA 616
Cdd:PRK11831 84 kRMSMLFQSGALFTDmNVFDNVAYPLRE----------HTQLPAPLLHSTVMMKLEAVGLRGaaklmpSELSGGMARRAA 153
|
170
....*....|....*.
gi 73747917 617 IARALVRDPRVLILDE 632
Cdd:PRK11831 154 LARAIALEPDLIMFDE 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
492-639 |
2.11e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 492 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVllDEKP-----ISQYE----HCYLhSQVVS-----------VGQ 551
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEPswdevLKRFRgtelQNYF-KKLYNgeikvvhkpqyVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 552 EPVLFSGSVRnniayglqscedDKVMAAAQAAHADDFIQE--MEHGIYTDVgekgSQLAAGQKQRLAIARALVRDPRVLI 629
Cdd:PRK13409 172 IPKVFKGKVR------------ELLKKVDERGKLDEVVERlgLENILDRDI----SELSGGELQRVAIAAALLRDADFYF 235
|
170
....*....|
gi 73747917 630 LDEATSALDV 639
Cdd:PRK13409 236 FDEPTSYLDI 245
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
485-638 |
2.48e-08 |
|
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: 55.63 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYqpTGGQVLLD-----EKPISQYEHCYlhsqvVSVGQEPVLFSG 558
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDgvswnSVPLQKWRKAF-----GVIPQKVFIFSG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNI-AYGLQSceDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:cd03289 92 TFRKNLdPYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
.
gi 73747917 638 D 638
Cdd:cd03289 170 D 170
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
155-368 |
2.86e-08 |
|
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: 55.69 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 155 AFFFLVLAVLGETLIPHYSGRVIDIL--GGDFDPHAFASAIFFMCLFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSS 232
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALtlAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 233 LLRQDLGFFQETKTGE----LNSRLSSDTTLMS----NWLPLNANVLLRSLVkvvglygFMLSISPRLTLLSLLHMP-FT 303
Cdd:cd18560 81 LHSLSLDWHLSKKTGEvvriMDRGTESANTLLSylvfYLVPTLLELIVVSVV-------FAFHFGAWLALIVFLSVLlYG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 304 IAAEKVYNTRhqevlREIQDAVA----RAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWR 368
Cdd:cd18560 154 VFTIKVTEWR-----TKFRRAANkkdnEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVK 217
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
487-639 |
3.16e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.87 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 487 KGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLL---DEKPISQYEHCYLHSQVVSVGQEPvLFSGSVRNN 563
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRAVRSDIQMIFQDP-LASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 564 ----IAYGLQS----CEDDKVMaaaqaahadDFIQEMehgiYTDVG-------EKGSQLAAGQKQRLAIARALVRDPRVL 628
Cdd:PRK15079 117 igeiIAEPLRTyhpkLSRQEVK---------DRVKAM----MLKVGllpnlinRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170
....*....|.
gi 73747917 629 ILDEATSALDV 639
Cdd:PRK15079 184 ICDEPVSALDV 194
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
479-639 |
4.49e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.21 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 479 NRPDRPVL----------KGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYE-HCYLHSQVV 547
Cdd:PRK15439 262 QAAGAPVLtvedltgegfRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 SVG---QEPVLF---------SGSVRNNIAYGLQSCEDDKVMaaaqaahaDDFIQEMehGI-YTDVGEKGSQLAAGQKQR 614
Cdd:PRK15439 342 YLPedrQSSGLYldaplawnvCALTHNRRGFWIKPARENAVL--------ERYRRAL--NIkFNHAEQAARTLSGGNQQK 411
|
170 180
....*....|....*....|....*
gi 73747917 615 LAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVDV 436
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
465-642 |
4.79e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.89 E-value: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 465 QGVVKFQDVSFAYPNrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyehCYLHS 544
Cdd:PRK15056 4 QAGIVVNDVTVTWRN--GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVGQE-------PVLFSGSVR----NNIAYGLQSCEDDKVMAAAQAAHADdfIQEMEHgiyTDVGEkgsqLAAGQKQ 613
Cdd:PRK15056 79 LVAYVPQSeevdwsfPVLVEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVD--MVEFRH---RQIGE----LSGGQKK 149
|
170 180
....*....|....*....|....*....
gi 73747917 614 RLAIARALVRDPRVLILDEATSALDVQCE 642
Cdd:PRK15056 150 RVFLARAIAQQGQVILLDEPFTGVDVKTE 178
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
485-640 |
5.71e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQY---EHCYLHSQVVS-VGQEPVLFS--G 558
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKHVGfVFQSFMLIPtlN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYGLQSCEDDKvmaaaqaAHADDFIQEMEH-GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK10584 105 ALENVELPALLRGESSR-------QSRNGAKALLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
...
gi 73747917 638 DVQ 640
Cdd:PRK10584 178 DRQ 180
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
492-651 |
6.62e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 492 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpIS---QY---EHCYLHSQVVSVGQEPVLFSGSVRNNIA 565
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-ISykpQYispDYDGTVEEFLRSANTDDFGSSYYKTEII 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 566 YGLQScedDKVMAaaqaahaddfiQEMehgiytdvgekgSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVqcEQ-- 643
Cdd:COG1245 441 KPLGL---EKLLD-----------KNV------------KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQrl 492
|
170
....*....|
gi 73747917 644 --AKTLWKFM 651
Cdd:COG1245 493 avAKAIRRFA 502
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
482-638 |
8.72e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.27 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 482 DRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTG--GQVLL-DEKPISQ--------------YEHCYLHS 544
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILAnNRKPTKQilkrtgfvtqddilYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 545 QVVSVG----------QEPVLFSGSVRNNIayGLQSCEDDKVmaaaqaahADDFIQemehGIytdvgekgsqlAAGQKQR 614
Cdd:PLN03211 160 TLVFCSllrlpksltkQEKILVAESVISEL--GLTKCENTII--------GNSFIR----GI-----------SGGERKR 214
|
170 180
....*....|....*....|....
gi 73747917 615 LAIARALVRDPRVLILDEATSALD 638
Cdd:PLN03211 215 VSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
485-640 |
1.22e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 53.94 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQV---LLDEKPISQYEHC--YLHSQVVS----------- 548
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKekVLEKLVIQktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 549 -----VG-----QEPVLFSGSVRNNIAYGLQSCEDDKvmaAAQAAHADDFIQEMehGIYTDVGEKGS-QLAAGQKQRLAI 617
Cdd:PRK13651 102 eirrrVGvvfqfAEYQLFEQTIEKDIIFGPVSMGVSK---EEAKKRAAKYIELV--GLDESYLQRSPfELSGGQKRRVAL 176
|
170 180
....*....|....*....|...
gi 73747917 618 ARALVRDPRVLILDEATSALDVQ 640
Cdd:PRK13651 177 AGILAMEPDFLVFDEPTAGLDPQ 199
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
154-427 |
1.29e-07 |
|
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: 53.62 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 154 AAFFFLVLAVLGETLI---PHYSGRVID--ILGGDFDpHAFASAIFFMCLFSFGSSLSAgCRGGCFTYTMSRINLRIREQ 228
Cdd:cd18567 3 ALLQILLLSLALELFAlasPLYLQLVIDevIVSGDRD-LLTVLAIGFGLLLLLQALLSA-LRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 229 LFSSLLRQDLGFFQETKTGELNSRLSSdttlmsnwlpLNA--NVLLRSLVK-------VVGLYGFMLSISPRLTLLSLLH 299
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFGS----------LDEiqQTLTTGFVEalldglmAILTLVMMFLYSPKLALIVLAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 300 MPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHevcrykealeqcRQLYWR--------RDL 371
Cdd:cd18567 151 VALYALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAE------------REARWLnllvdainADI 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 372 ERALYLLVRRVLHLGV----QMLMLSCGLQQMQDGELTQGSLLSFMIYQESVGSYVQTLV 427
Cdd:cd18567 219 RLQRLQILFSAANGLLfgleNILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLI 278
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
491-647 |
1.39e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.01 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 491 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpisqyEHCYLHSQVVSVGQEPVLFS---GSVRNNIAYG 567
Cdd:PRK11701 27 FDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR-----DGQLRDLYALSEAERRRLLRtewGFVHQHPRDG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 568 LQSCED------DKVMAAAQAAHAD------DFIQEMEhgIYTD-VGEKGSQLAAGQKQRLAIARALVRDPRVLILDEAT 634
Cdd:PRK11701 102 LRMQVSaggnigERLMAVGARHYGDiratagDWLERVE--IDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPT 179
|
170
....*....|...
gi 73747917 635 SALDVQCeQAKTL 647
Cdd:PRK11701 180 GGLDVSV-QARLL 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
467-640 |
1.81e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVlldekpisqyeHCYLHSQV 546
Cdd:PRK11147 319 VFEMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------HCGTKLEV 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 -------------------VSVGQEPVLFSGSVRNNIAYgLQsceddkvmaaaqaahadDFI----QEMehgiyTDVgek 603
Cdd:PRK11147 385 ayfdqhraeldpektvmdnLAEGKQEVMVNGRPRHVLGY-LQ-----------------DFLfhpkRAM-----TPV--- 438
|
170 180 190
....*....|....*....|....*....|....*..
gi 73747917 604 gSQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:PRK11147 439 -KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
471-638 |
2.75e-07 |
|
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: 53.79 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpisqyehcylhsqvVSVG 550
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG--------------IKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 ---QEPVL-FSGSVRNNIAYGLQSCED-----DKVMAAAQAAHAD------------DFIQ-----EMEHGIY------- 597
Cdd:TIGR03719 72 ylpQEPQLdPTKTVRENVEEGVAEIKDaldrfNEISAKYAEPDADfdklaaeqaelqEIIDaadawDLDSQLEiamdalr 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 73747917 598 -----TDVgekgSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:TIGR03719 152 cppwdADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
486-639 |
3.60e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.40 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVL-LDEKPISQyEHCYLHSQVVSVGQE-------PVLFS 557
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvLGYVPFKR-RKEFARRIGVVFGQRsqlwwdlPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 558 GSVRNNIaYGLQSCEDDKVMaaaqaahaDDFIQ--EMEHGIYTDVgekgSQLAAGQKQRLAIARALVRDPRVLILDEATS 635
Cdd:COG4586 117 FRLLKAI-YRIPDAEYKKRL--------DELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
....
gi 73747917 636 ALDV 639
Cdd:COG4586 184 GLDV 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
486-637 |
4.71e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.87 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTG---GQVLLDEKP-----ISQYEHCylhsQVVSVGQE----P 553
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkdIRDSEAL----GIVIIHQElaliP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 554 VLfsgSVRNNI-------AYGLQSCED---------DKVmaaaqaahaddfiqemehGIYTDVGEKGSQLAAGQKQRLAI 617
Cdd:NF040905 92 YL---SIAENIflgneraKRGVIDWNEtnrrarellAKV------------------GLDESPDTLVTDIGVGKQQLVEI 150
|
170 180
....*....|....*....|
gi 73747917 618 ARALVRDPRVLILDEATSAL 637
Cdd:NF040905 151 AKALSKDVKLLILDEPTAAL 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
480-639 |
4.96e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTV----AALLQNLYQPTG----GQVLLDEKPISQYEHCYLH--SQVVSV 549
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLArlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 550 GQEPVlFSGSVRNNI---------AYGLQSCEDDKVMAAAQAAHaddfiqemehGIYTDVGEKGSQLAAGQKQRLAIARA 620
Cdd:PRK13547 91 AAQPA-FAFSAREIVllgrypharRAGALTHRDGEIAWQALALA----------GATALVGRDVTTLSGGELARVQFARV 159
|
170 180
....*....|....*....|....*...
gi 73747917 621 L---------VRDPRVLILDEATSALDV 639
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-638 |
5.84e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.38 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQVLLDEKPI--SQYEHCYLHSQVVSVGQEPVLFS 557
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 558 G-SVRNNIAYGL--------QSCEDDKVMAAAQAAHADDFIQEMehgiytdVGEKGSQLAAGQKQRLAIARALVRDPRVL 628
Cdd:PRK14267 99 HlTIYDNVAIGVklnglvksKKELDERVEWALKKAALWDEVKDR-------LNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170
....*....|
gi 73747917 629 ILDEATSALD 638
Cdd:PRK14267 172 LMDEPTANID 181
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
498-639 |
6.50e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.80 E-value: 6.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 498 VTALVGPNGSGKSTVAALLQNLYQPT------GGQVLLD-EKPIsqyehcYLHSQVVSVG---QEPVLFSG-SVRNNIAY 566
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQkgrivlNGRVLFDaEKGI------CLPPEKRRIGyvfQDARLFPHyKVRGNLRY 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747917 567 GlqsceddkvMAAAQAAHADDFIQEMehGIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK11144 100 G---------MAKSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
464-637 |
7.09e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 464 LQGVVKfqdvSFaypnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHcyLH 543
Cdd:PRK10762 7 LKGIDK----AF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP--KS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVG---QEPVLFSG-SVRNNIAYGLQ-----SCEDDKVMaaaqAAHADDFIQEM--EHGIYTDVGEkgsqLAAGQK 612
Cdd:PRK10762 76 SQEAGIGiihQELNLIPQlTIAENIFLGREfvnrfGRIDWKKM----YAEADKLLARLnlRFSSDKLVGE----LSIGEQ 147
|
170 180
....*....|....*....|....*
gi 73747917 613 QRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
189-361 |
9.04e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 51.02 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 189 FASAIFFMCLFSFgsslsagCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNA 268
Cdd:cd18599 64 YGGSILVILLLSL-------IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 269 NVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNtrhqEVLREIQ--DAVARAGQV--VREAVGGLQTVRS 344
Cdd:cd18599 137 ENFLQNVLLVVFSLIIIAIVFPWFLIALIPLAIIFVFLSKIFR----RAIRELKrlENISRSPLFshLTATIQGLSTIHA 212
|
170
....*....|....*..
gi 73747917 345 FGAEEHEVCRYKEALEQ 361
Cdd:cd18599 213 FNKEKEFLSKFKKLLDQ 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
484-639 |
1.07e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 484 PVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS-QYEHCYLHSQVVSVGQEP----VLFSG 558
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRkrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIA---------YGLQSCEDDKVMAAaqaahaDDFIQ-------EMEHGIytdvgekgSQLAAGQKQRLAIARALV 622
Cdd:PRK10762 346 SVKENMSltalryfsrAGGSLKHADEQQAV------SDFIRlfniktpSMEQAI--------GLLSGGNQQKVAIARGLM 411
|
170
....*....|....*..
gi 73747917 623 RDPRVLILDEATSALDV 639
Cdd:PRK10762 412 TRPKVLILDEPTRGVDV 428
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
471-647 |
1.24e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPN-RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQPT----------GGQVLL--DEKPISQ 536
Cdd:PRK15134 9 ENLSVAFRQqQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPvvypsgdirfHGESLLhaSEQTLRG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 537 YEHcylhSQVVSVGQEPV------------------LFSGSVRNNIAYGLQSCEDdKVMAAAQAAHADDFiqemEHgiyt 598
Cdd:PRK15134 89 VRG----NKIAMIFQEPMvslnplhtlekqlyevlsLHRGMRREAARGEILNCLD-RVGIRQAAKRLTDY----PH---- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 73747917 599 dvgekgsQLAAGQKQRLAIARALVRDPRVLILDEATSALDVQCeQAKTL 647
Cdd:PRK15134 156 -------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-QAQIL 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
471-638 |
2.55e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 471 QDVSFAYPnrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpisqyehcylhsqvVSVG 550
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG--------------IKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 551 ---QEPVL-FSGSVRNNIAYGLQS---------------CEDDKVMaaaqaahaDDFIQEM-------EHgiyTDVGEKG 604
Cdd:PRK11819 74 ylpQEPQLdPEKTVRENVEEGVAEvkaaldrfneiyaayAEPDADF--------DALAAEQgelqeiiDA---ADAWDLD 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 73747917 605 SQL--AA-----------------GQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK11819 143 SQLeiAMdalrcppwdakvtklsgGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
444-646 |
2.96e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 444 FSYMDRQP-NLPSPgtlapttlqgVVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP 522
Cdd:PRK10636 298 FHFSFRAPeSLPNP----------LLKMEKVSAGYG---DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 523 TGGQVLLdEKPI-----SQYEHCYLHSQVVSVGQ----EPVLFSGSVRNNI-AYGLQScedDKVmaaaqaahaddfiqem 592
Cdd:PRK10636 365 VSGEIGL-AKGIklgyfAQHQLEFLRADESPLQHlarlAPQELEQKLRDYLgGFGFQG---DKV---------------- 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 73747917 593 ehgiyTDVGEKGSqlaAGQKQRLAIARALVRDPRVLILDEATSALDVQCEQAKT 646
Cdd:PRK10636 425 -----TEETRRFS---GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
468-638 |
3.10e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYP--NRPDRPV---------------LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVllD 530
Cdd:PRK13545 5 VKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 531 EKpisqyehcylhsqvvsvGQEPVLFSGSVRNNIAYGLQSCEDDKVMAAAQAAHADDFIQEMEHgiYTDVGEKGSQ---- 606
Cdd:PRK13545 83 IK-----------------GSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIE--FADIGKFIYQpvkt 143
|
170 180 190
....*....|....*....|....*....|..
gi 73747917 607 LAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK13545 144 YSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
168-443 |
5.46e-06 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to 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.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 48.68 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 168 LIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSslsagcrGGCFTYTMSRINLRI----REQL----FSSLLRQDLG 239
Cdd:cd18583 14 LVPRQLGIIVDSLSGGSGKSPWKEIGLYVLLRFLQS-------GGGLGLLRSWLWIPVeqysYRALstaaFNHVMNLSMD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 240 FFQETKTGELNS---RLSSDTTLMSNWL----PLNANVLLrSLVKVVGLYGfmlsisPRLTLLSLLHMPFTIAAEKVYNT 312
Cdd:cd18583 87 FHDSKKSGEVLKaieQGSSINDLLEQILfqivPMIIDLVI-AIVYLYYLFD------PYMGLIVAVVMVLYVWSTIKLTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 313 RHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQLYWRrdLERALYLLVrrvlhlGVQMLML 392
Cdd:cd18583 160 WRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERK--YLFSLNLLN------AVQSLIL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 393 SCGL--------QQMQDGELTQGSLLSFMIYQESVGSYVQTLVYIYGDMLSNVGAAEKV 443
Cdd:cd18583 232 TLGLlagcflaaYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
191-350 |
6.24e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 48.62 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 191 SAIFFM---CLFSFGSSLSAGCRGGCFTY---TMSRinlRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWL 264
Cdd:cd18604 41 SVLYYLgiyALISLLSVLLGTLRYLLFFFgslRASR---KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 265 PLNANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREiqDAVARAG--QVVREAVGGLQTV 342
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRL--ESVARSPilSHFGETLAGLVTI 195
|
....*...
gi 73747917 343 RSFGAEEH 350
Cdd:cd18604 196 RAFGAEER 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
467-639 |
6.81e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQvlldekpisqyehcylhsqv 546
Cdd:PRK11819 324 VIEAENLSKSFG---DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-------------------- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 547 VSVGQepvlfsgSVRnnIAYGLQSCE--DDKVMAAAQAAHADDFIQ----EMEHGIY--------TDVGEKGSQLAAGQK 612
Cdd:PRK11819 381 IKIGE-------TVK--LAYVDQSRDalDPNKTVWEEISGGLDIIKvgnrEIPSRAYvgrfnfkgGDQQKKVGVLSGGER 451
|
170 180
....*....|....*....|....*..
gi 73747917 613 QRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
468-639 |
6.90e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 6.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPNrPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TGGQVLLDEKPISQYEHCYLH- 543
Cdd:PRK09473 15 VKDLRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNk 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 ---SQVVSVGQEP----------------VL-----------FSGSVRNNIAYGLQscEDDKVMaaaqaahaddfiqeme 593
Cdd:PRK09473 94 lraEQISMIFQDPmtslnpymrvgeqlmeVLmlhkgmskaeaFEESVRMLDAVKMP--EARKRM---------------- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 73747917 594 hGIYTdvgekgSQLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK09473 156 -KMYP------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDV 194
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
464-638 |
8.51e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 47.70 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 464 LQGVVKFQDVSFAYPNRPdrpVLKGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLyqptGGQVLLDEKPISQYEhcYLH 543
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQ---ALHAVDLNIHHGEMVALLGPSGSGKST---LLRHL----SGLITGDKSAGSHIE--LLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQepvlFSGSVRN------------NIAYGLQSCEDDKVMAAAQAAHADD----FIQEMEHGIY---TDVG--- 601
Cdd:PRK09984 69 RTVQREGR----LARDIRKsrantgyifqqfNLVNRLSVLENVLIGALGSTPFWRTcfswFTREQKQRALqalTRVGmvh 144
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 73747917 602 ---EKGSQLAAGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK09984 145 fahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
219-414 |
8.80e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 47.90 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 219 SRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTL---MSNWLplnANVLLRSLVKVVgLYGFMLSISPRLTLL 295
Cdd:cd18783 71 TRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIrqfLTGQL---FGTLLDATSLLV-FLPVLFFYSPTLALV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 296 ----SLLHMPFTIAAEKVYNTRHQEVLReiqdAVARAGQVVREAVGGLQTVRSFgaeehevcrykeALEQCRQLYWRRDL 371
Cdd:cd18783 147 vlafSALIALIILAFLPPFRRRLQALYR----AEGERQAFLVETVHGIRTVKSL------------ALEPRQRREWDERV 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 372 ERAlyllVRRVLHLG------------VQMLM----LSCGLQQMQDGELTQGSLLSFMI 414
Cdd:cd18783 211 ARA----IRARFAVGrlsnwpqtltgpLEKLMtvgvIWVGAYLVFAGSLTVGALIAFNM 265
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
467-652 |
1.36e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.47 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPI--------SQYE 538
Cdd:TIGR01257 1937 ILRLNELTKVYSGT-SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIltnisdvhQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 539 HCYLHSQV--VSVGQEPVLFSGSVRnniayGLQSCEDDKVMAAAqaahaddfIQEMEHGIYTDvgEKGSQLAAGQKQRLA 616
Cdd:TIGR01257 2016 YCPQFDAIddLLTGREHLYLYARLR-----GVPAEEIEKVANWS--------IQSLGLSLYAD--RLAGTYSGGNKRKLS 2080
|
170 180 190
....*....|....*....|....*....|....*.
gi 73747917 617 IARALVRDPRVLILDEATSALDVQCEqaKTLWKFMI 652
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQAR--RMLWNTIV 2114
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
485-643 |
1.44e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.54 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 485 VLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQyeHCYLHSQVVSVGQEPV---------- 554
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD--KKNNHELITNPYSKKIknfkelrrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 555 ----------LFSGSVRNNIAYGLQSCeddKVMAAAQAAHADDFIQEMehGIYTDVGEKGS-QLAAGQKQRLAIARALVR 623
Cdd:PRK13631 119 smvfqfpeyqLFKDTIEKDIMFGPVAL---GVKKSEAKKLAKFYLNKM--GLDDSYLERSPfGLSGGQKRRVAIAGILAI 193
|
170 180
....*....|....*....|
gi 73747917 624 DPRVLILDEATSALDVQCEQ 643
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEH 213
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
156-429 |
2.97e-05 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. 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, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, 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.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 46.47 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 156 FFFLVLAVLGETLIPHYSGRVIDILGGDFDPHAFASAIFFMCLFSFGSSLSAGCRGG--------------CFTYTMSRI 221
Cdd:cd18581 2 LLLLAAGRVVNVLVPILYKKIVDSLTPDSADSPLAFPWALILLYVFLKFLQGGGSGSvgllsnlrsflwipVQQFTTREI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 222 NLRireqLFSSLLRQDLGFFQETKTGE----LNSRLSSDTTLMS----NWLPLNANVllrslvkVVGLYGFMLSISPRLT 293
Cdd:cd18581 82 SVK----LFAHLHSLSLRWHLSRKTGEvlrvMDRGTSSINSLLSyvlfNIGPTIADI-------IIAIIYFAIAFNPWFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 294 LLSL----LHMPFTIAAEKvYNTRHQEVLREiQDAVARAgqvvrEAVGGL---QTVRSFGAEEHEVCRYKEALEQCRQLY 366
Cdd:cd18581 151 LIVFvtmaLYLILTIIITE-WRTKFRREMNK-LDNEKRA-----KAVDSLlnfETVKYYNAERFEVERYRRAIDDYQVAE 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73747917 367 WRRDLERALYLLVRRVL-HLGVQMLMLSCGlQQMQDGELTqgsllsfmiyqesVGSYVQTLVYI 429
Cdd:cd18581 224 WKSNASLNLLNTAQNLIiTIGLLAGSLLCA-YFVVEGKLT-------------VGDFVLFLTYI 273
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
467-535 |
3.01e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 3.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73747917 467 VVKFQDVSfaYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPIS 535
Cdd:COG3845 257 VLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT 323
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
468-638 |
3.84e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 468 VKFQDVSFAYPnrpDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKpisqyehcylhsqvv 547
Cdd:PRK15064 320 LEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--------------- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 548 svgqepvlfsgsvrNNIAYGLQSCEDD--------KVMAAAQAAHADD-----------FIQEmehgiytDVGEKGSQLA 608
Cdd:PRK15064 382 --------------ANIGYYAQDHAYDfendltlfDWMSQWRQEGDDEqavrgtlgrllFSQD-------DIKKSVKVLS 440
|
170 180 190
....*....|....*....|....*....|
gi 73747917 609 AGQKQRLAIARALVRDPRVLILDEATSALD 638
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
490-639 |
7.86e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 490 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISqyehcyLHSQVVSVGQEPVL------FSG----- 558
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIRAGIMLcpedrkAEGiipvh 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 559 SVRNNIAYglqSCE----------DDKvmaaAQAAHADDFIQEMEhgIYTDVGE-KGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:PRK11288 347 SVADNINI---SARrhhlragcliNNR----WEAENADRFIRSLN--IKTPSREqLIMNLSGGNQQKAILGRWLSEDMKV 417
|
170
....*....|..
gi 73747917 628 LILDEATSALDV 639
Cdd:PRK11288 418 ILLDEPTRGIDV 429
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
478-639 |
9.36e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 9.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 478 PNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQptG---GQVLLDEKPIS--------QYEHCYL---- 542
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP--GrweGEIFIDGKPVKirnpqqaiAQGIAMVpedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 543 --HSQV--VSVGQE---PVL--FSGSVRNNIAYGLQSceddkvmaaaqaahADDFIQEMEhgIYTDVGE-KGSQLAAGQK 612
Cdd:PRK13549 348 krDGIVpvMGVGKNitlAALdrFTGGSRIDDAAELKT--------------ILESIQRLK--VKTASPElAIARLSGGNQ 411
|
170 180
....*....|....*....|....*..
gi 73747917 613 QRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
187-414 |
9.64e-05 |
|
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: 44.80 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 187 HAFASAIFFMCLFSFGSSlsaGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLmSNWLPL 266
Cdd:cd18588 42 DVLAIGLLVVALFEAVLS---GLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRELESI-RQFLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 267 NANVLLRSLVKVVGLYGFMLSISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFG 346
Cdd:cd18588 118 SALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 347 AE-------EHEVCRYKEA----------LEQCRQLywrrdLERALYLLvrrVLHLGVQMLMlscglqqmqDGELTQGSL 409
Cdd:cd18588 198 VEpqfqrrwEELLARYVKAsfktanlsnlASQIVQL-----IQKLTTLA---ILWFGAYLVM---------DGELTIGQL 260
|
....*.
gi 73747917 410 LSF-MI 414
Cdd:cd18588 261 IAFnML 266
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
467-639 |
1.16e-04 |
|
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: 45.20 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 467 VVKFQDVSFAYPNRPDRPVLKGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPTGGQVLLDEKPISqYEHCY--LH 543
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVD-IRNPAqaIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 544 SQVVSVGQE-------PVLfsgSVRNNIAYG-LQS-CEDDKVMAAAQAAHADDFIQEMEHGIYTDVGEKGSqLAAGQKQR 614
Cdd:TIGR02633 336 AGIAMVPEDrkrhgivPIL---GVGKNITLSvLKSfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQK 411
|
170 180
....*....|....*....|....*
gi 73747917 615 LAIARALVRDPRVLILDEATSALDV 639
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
491-643 |
1.30e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 491 FTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqptggqVLLDEKPISQYEHCYLhsqvVSVGQEPVLFSGSVRNNIAYGLQ 569
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALArALAGEL-------PLLSGERQSQFSHITR----LSFEQLQKLVSDEWQRNNTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 570 SCEDDkvmaaaQAAHADDFIQEMEH------------GIYTDVGEKGSQLAAGQKQRLAIARALVRDPRVLILDEATSAL 637
Cdd:PRK10938 93 PGEDD------TGRTTAEIIQDEVKdparceqlaqqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
|
....*.
gi 73747917 638 DVQCEQ 643
Cdd:PRK10938 167 DVASRQ 172
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
606-639 |
4.03e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 4.03e-04
10 20 30
....*....|....*....|....*....|....
gi 73747917 606 QLAAGQKQRLAIARALVRDPRVLILDEATSALDV 639
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDV 186
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
491-638 |
4.08e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 491 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDEKPISQYEHC------YLhSQVVSVGQEpvLfsgSVRNNI 564
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAtrrrvgYM-SQAFSLYGE--L---TVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 565 A-----YGLqscEDDKVmaaaqaahaDDFIQEMEHGIytDVGEKGSQLAA----GQKQRLAIARALVRDPRVLILDEATS 635
Cdd:NF033858 361 ElharlFHL---PAAEI---------AARVAEMLERF--DLADVADALPDslplGIRQRLSLAVAVIHKPELLILDEPTS 426
|
...
gi 73747917 636 ALD 638
Cdd:NF033858 427 GVD 429
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
501-639 |
4.76e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 501 LVGPNGSGKSTVAALLQNLYQPTGGQVLLD--EK--PISQ----YEHCYL-------HSQVVSVGQEpvlfsgsvRNNIa 565
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpnERlgKLRQdqfaFEEFTVldtvimgHTELWEVKQE--------RDRI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 566 YGLQSCEDDKVMAAAQAahaddfiqEM---EHGIYTDVGEKG-----------------SQLAAGQKQRLAIARALVRDP 625
Cdd:PRK15064 103 YALPEMSEEDGMKVADL--------EVkfaEMDGYTAEARAGelllgvgipeeqhyglmSEVAPGWKLRVLLAQALFSNP 174
|
170
....*....|....
gi 73747917 626 RVLILDEATSALDV 639
Cdd:PRK15064 175 DILLLDEPTNNLDI 188
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
470-638 |
9.31e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.01 E-value: 9.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 470 FQDVSFAYPNRpdrpVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQVlldekpisqyehcYLHSQVVSV 549
Cdd:PRK13541 4 LHQLQFNIEQK----NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNI-------------YYKNCNINN 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 550 GQEPvlFSGSVRNNIAYGLQ-SCEDDKVMAAAQAAHADDFIQEMEHGIYTD-VGEKGSQLAAGQKQRLAIARALVRDPRV 627
Cdd:PRK13541 67 IAKP--YCTYIGHNLGLKLEmTVFENLKFWSEIYNSAETLYAAIHYFKLHDlLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170
....*....|.
gi 73747917 628 LILDEATSALD 638
Cdd:PRK13541 145 WLLDEVETNLS 155
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
198-349 |
1.05e-03 |
|
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: 41.69 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 198 LFSFGSSLSAGCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRSLVK 277
Cdd:cd18606 43 GLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSS 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 73747917 278 VVGLYGFMLSISPRLTLLsllhMPFTIAAEKVYNTRHQEVLREIQ--DAVARAGQVVR--EAVGGLQTVRSFGAEE 349
Cdd:cd18606 123 IIGTFILIIIYLPWFAIA----LPPLLVLYYFIANYYRASSRELKrlESILRSFVYANfsESLSGLSTIRAYGAQD 194
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
488-516 |
1.09e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 1.09e-03
10 20 30
....*....|....*....|....*....|...
gi 73747917 488 GLTFTLRPGEVTALVGPNGSGKST----VAALL 516
Cdd:pfam13555 14 GHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
496-640 |
1.81e-03 |
|
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: 39.86 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 496 GEVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDekpisqyehcylhsqvvsvgqepvlfsgsvRNNIAYGLQsceddk 575
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------------------------GITPVYKPQ------ 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 73747917 576 vmaaaqaahaddfiqemehgiYTDvgekgsqLAAGQKQRLAIARALVRDPRVLILDEATSALDVQ 640
Cdd:cd03222 69 ---------------------YID-------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
480-527 |
1.83e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 1.83e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 73747917 480 RPDRPVLKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQV 527
Cdd:PRK10636 11 RGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSY 58
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
208-414 |
3.05e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 40.26 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 208 GCRGGCFTYTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLmSNWLPLNANVLLRSLVKVVGLYGFMLS 287
Cdd:cd18566 60 LLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQI-REFLTGQALLALLDLPFVLIFLGLIWY 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 288 ISPRLTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRqlyw 367
Cdd:cd18566 139 LGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAA---- 214
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 73747917 368 RRDLERALYLLV----RRVLHLGVQMLMLSCGLQQMQDGELTQGSLLSFMI 414
Cdd:cd18566 215 YAGFKVAKINAVaqtlGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
486-531 |
4.88e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 4.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 73747917 486 LKGLTFTLRPGeVTALVGPNGSGKSTVAALLQNLYQPTGGQVLLDE 531
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKFDEE 58
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
491-512 |
5.02e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 39.53 E-value: 5.02e-03
10 20
....*....|....*....|..
gi 73747917 491 FTLRPGEVTALVGPNGSGKSTV 512
Cdd:COG4637 16 LELPLGPLTVLIGANGSGKSNL 37
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
486-527 |
5.33e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 5.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 73747917 486 LKGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTGGQV 527
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
216-364 |
5.59e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 39.19 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 216 YTMSRINLRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDT----TLMSNWLPlnanVLLRSLVKVVGLYGFMLSISPR 291
Cdd:cd18561 62 RAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVealeAYYGRYLP----QLLVALLGPLLILIYLFFLDPL 137
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 73747917 292 LTLLSLLHMPFTIAAEKVYNTRHQEVLREIQDAVARAGQVVREAVGGLQTVRSFGAEEHEVCRYKEALEQCRQ 364
Cdd:cd18561 138 VALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQ 210
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
486-520 |
8.00e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 8.00e-03
10 20 30
....*....|....*....|....*....|....*.
gi 73747917 486 LKGLTFTLRPGeVTALVGPNGSGKST-VAALLQNLY 520
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
198-349 |
8.24e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 38.74 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 198 LFSFGSSLS---AGCRGGCftytmsrinlRIREQLFSSLLRQDLGFFQETKTGELNSRLSSDTTLMSNWLPLNANVLLRS 274
Cdd:cd18602 65 ILSLVTNLAgelAGLRAAR----------RLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRF 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73747917 275 LVKVVGLYGFMLSISPRLTLLSLlhmpFTIAAEKVYNTRHQEVLREIQ--DAVARaGQVV---REAVGGLQTVRSFGAEE 349
Cdd:cd18602 135 LLLCLSAIIVNAIVTPYFLIALI----PIIIVYYFLQKFYRASSRELQrlDNITK-SPVFshfSETLGGLTTIRAFRQQA 209
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