|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-716 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 1007.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 21 RPMLPGIFSLLVP-EVPLLRVWVVGLSRWAILGLGVRGVLGVTAGahGWLAALQPLVAALSLALPGLALFRELAAWGTLR 99
Cdd:TIGR00958 21 RDLLQGIFGLLLPfEKGLYVLWLEGTLRLGVLWLGALGILLNKAG--GLLAAVKPLVAALCLATPSLSSLRALAFWEALD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 100 EGDSAGLLYWNsrpdAFAISYVAALPAAALWHKLGSLWAP-----SGNRDAGDMLCRMLGFLGPKKRRLYLVLVLLILSC 174
Cdd:TIGR00958 99 PAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETADLLFRLLGLSGRDWPWLISAFVFLTLSS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 175 LGEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLK 254
Cdd:TIGR00958 175 LGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 255 NPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQE 334
Cdd:TIGR00958 255 NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 335 SLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGA 414
Cdd:TIGR00958 335 AVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGK 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 415 VSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPCSPLSGSLAPSNMKGLVEFQDVSFAYPNQPKV 494
Cdd:TIGR00958 415 VSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFREN 574
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVREN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 575 IAYGLNRTPtMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAgnq 654
Cdd:TIGR00958 575 IAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA--- 650
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239835765 655 lRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMV 716
Cdd:TIGR00958 651 -ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
142-718 |
9.37e-148 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 443.07 E-value: 9.37e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 142 NRDAGDMLCRMLGFLGPKKRRLYLVLVLLILSCLGEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFAS 221
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 222 DGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSP 301
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 302 YLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEA 381
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 382 LAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRT 461
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 462 P-CSPLSGSLAPSNMKGLVEFQDVSFAYPNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL 540
Cdd:COG1132 322 PeIPDPPGAVPLPPVRGEIEFENVSFSYPGDR--PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 541 DGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLS 620
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYG-RPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLS 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYEspKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQG 700
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALER--LMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570
....*....|....*...
gi 239835765 701 THLQLMKRGGCYRAMVEA 718
Cdd:COG1132 557 THEELLARGGLYARLYRL 574
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
176-454 |
3.44e-139 |
|
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: 410.32 E-value: 3.44e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 176 GEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKN 255
Cdd:cd18589 11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 256 PAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQES 335
Cdd:cd18589 91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 336 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAV 415
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 239835765 416 SSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
468-696 |
4.47e-119 |
|
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: 356.01 E-value: 4.47e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 468 GSLAPSNMKGLVEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQ 547
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 548 YDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLNRTPtMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 627
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRasRTVLLITQQLSLAEQAHHILFLREGSV 696
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
178-717 |
2.27e-118 |
|
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: 371.47 E-value: 2.27e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVPSftrnIWLMSILTIASTALEFASDGIYNITMGHMHGRV----HREVFRAVLRQETGFFL 253
Cdd:COG2274 173 LATPLFTQVVIDRVLPNQDLST----LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIdlrlSSRFFRHLLRLPLSFFE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 254 KNPAGSITSRVTeDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQ 333
Cdd:COG2274 249 SRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREES 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 334 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKK-EALAYVAEVWTTSVSGMLLkVGILYLGGQLVIR 412
Cdd:COG2274 328 EASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKlRRLSNLLSTLSGLLQQLAT-VALLWLGAYLVID 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 413 GAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTP-CSPLSGSLAPSNMKGLVEFQDVSFAYPNQ 491
Cdd:COG2274 407 GQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGD 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 492 PKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSF 571
Cdd:COG2274 487 SP-PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTI 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 RENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:COG2274 566 RENITLG-DPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 652 GNQLRVQRLLYEspKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVE 717
Cdd:COG2274 645 ETEAIILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
238-717 |
6.29e-98 |
|
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: 313.95 E-value: 6.29e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 238 REVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLL 317
Cdd:TIGR02204 95 RAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 318 PKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealAYVAEVWTTSVSGML 397
Cdd:TIGR02204 175 ILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQ---RIRTRALLTAIVIVL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 398 L---KVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTP--CSPLSGSLAP 472
Cdd:TIGR02204 252 VfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKTLP 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 473 SNMKGLVEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHY 552
Cdd:TIGR02204 332 VPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LHTQVAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARA 632
Cdd:TIGR02204 412 LRARMALVPQDPVLFAASVMENIRYG-RPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARA 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCY 712
Cdd:TIGR02204 491 ILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLY 568
|
....*
gi 239835765 713 RAMVE 717
Cdd:TIGR02204 569 ARLAR 573
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
479-718 |
9.09e-94 |
|
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: 290.98 E-value: 9.09e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVA 558
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGRSFRENIAYGLNRtPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPL 638
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVEA 718
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
238-712 |
2.70e-90 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 293.55 E-value: 2.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 238 REVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLL 317
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 318 PKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGML 397
Cdd:TIGR02203 171 MRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 398 LKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPcSPLSGSLAPSNMKG 477
Cdd:TIGR02203 251 ALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP-EKDTGTRAIERARG 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQV 557
Cdd:TIGR02203 330 DVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQV 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFGRSFRENIAYGLNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKP 637
Cdd:TIGR02203 409 ALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 638 LLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCY 712
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
176-454 |
4.78e-81 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 259.78 E-value: 4.78e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 176 GEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKN 255
Cdd:cd18572 11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 256 PAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQES 335
Cdd:cd18572 91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 336 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAV 415
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 239835765 416 SSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18572 251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
207-712 |
2.29e-79 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 267.76 E-value: 2.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 207 MSILTIASTAL---EFASDGIYNITMGHMHGRVHREV----FRAVLRQETGFFLKNPAGSITSRVTEdTANVCESISGTL 279
Cdd:TIGR01846 178 LSVLALAMLAVaifEPALGGLRTYLFAHLTSRIDVELgarlYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 280 SLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANE 359
Cdd:TIGR01846 257 LTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 360 EGEAQKFRQKLEemktlnkkealAYVAEVWTTSVSGMLLKVGI-----------LYLGGQLVIRGAVSSGNLVSFVLYQL 428
Cdd:TIGR01846 337 PQFQNRWDRQLA-----------AYVAASFRVTNLGNIAGQAIeliqkltfailLWFGAHLVIGGALSPGQLVAFNMLAG 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 429 QFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDrTPCSPLSGSLAP-SNMKGLVEFQDVSFAY-PNQPkvQVLQGLTFTLHP 506
Cdd:TIGR01846 406 RVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAAlPELRGAITFENIRFRYaPDSP--EVLSNLNLDIKP 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 507 GTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlNRTPTME 586
Cdd:TIGR01846 483 GEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALC-NPGAPFE 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 587 EITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPK 666
Cdd:TIGR01846 562 HVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR 641
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 239835765 667 raSRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCY 712
Cdd:TIGR01846 642 --GRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
344-710 |
1.27e-76 |
|
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: 256.99 E-value: 1.27e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 344 LEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKTLnkKEAL--AYVAEVWTT-SVSGMLLKVGILYLGGQLVIRGAV 415
Cdd:COG4988 201 LDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtMKVL--RVAFlsSAVLEFFASlSIALVAVYIGFRLLGGSLTLFAAL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 416 ssgnlvsFVL------YQ--LQFTQAVQVllslypSMQkAVGSSEKIFEYLDRTPCSPLSGSLAPSNMKGL-VEFQDVSF 486
Cdd:COG4988 279 -------FVLllapefFLplRDLGSFYHA------RAN-GIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPsIELEDVSF 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 487 AYPNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLL 566
Cdd:COG4988 345 SYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 567 FGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:COG4988 423 FAGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPT 501
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 647 SALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGG 710
Cdd:COG4988 502 AHLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
352-715 |
1.28e-74 |
|
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: 252.82 E-value: 1.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 352 TVRSFANEEGEAQKFRQKLEEMKTLNKKealayvaevwtTSVSGMLLKVG-----------ILYLGGQLVIRGAVSSGNL 420
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVK-----------SQTSLALLNFGqaliialgltaMMLMAAQGVVAGTMTVGDF 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 421 VSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPC---SPLSGSLAPSnmKGLVEFQDVSFAYpnQPKVQVL 497
Cdd:COG5265 299 VLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEvadAPDAPPLVVG--GGEVRFENVSFGY--DPERPIL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 498 QGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAY 577
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAY 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 578 GlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRV 657
Cdd:COG5265 455 G-RPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 658 QRLLyespKRAS--RTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAM 715
Cdd:COG5265 534 QAAL----REVArgRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
477-710 |
2.46e-74 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 239.82 E-value: 2.46e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 477 GLVEFQDVSFAYpnQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQ 556
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 636
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 637 PLLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGG 710
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
479-715 |
3.49e-73 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 237.13 E-value: 3.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYpnQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVA 558
Cdd:cd03253 1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPL 638
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAM 715
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
176-454 |
6.35e-73 |
|
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: 238.36 E-value: 6.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 176 GEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKN 255
Cdd:cd18784 11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 256 PAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQES 335
Cdd:cd18784 91 KTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 336 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAV 415
Cdd:cd18784 171 LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 239835765 416 SSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18784 251 SGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
479-713 |
3.68e-72 |
|
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: 234.43 E-value: 3.68e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVA 558
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPL 638
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESPKRasRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYR 713
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
176-454 |
3.71e-71 |
|
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: 233.61 E-value: 3.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 176 GEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKN 255
Cdd:cd18557 11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 256 PAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQES 335
Cdd:cd18557 91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 336 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAV 415
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 239835765 416 SSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
323-717 |
6.57e-70 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 238.90 E-value: 6.57e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 323 KVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEA-LAYVAEVWTTSVSGMLLkVG 401
Cdd:COG4987 178 RLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLArLSALAQALLQLAAGLAV-VA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 402 ILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPCSPLSGSLAPSNMKGLVEF 481
Cdd:COG4987 257 VLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLEL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 482 QDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVG 561
Cdd:COG4987 337 EDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVP 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 562 QEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLI 641
Cdd:COG4987 416 QRPHLFDTTLRENLRLA-RPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILL 494
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 642 LDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVE 717
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEA--LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
232-712 |
2.76e-69 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 237.61 E-value: 2.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 232 MHGRvhREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINL 311
Cdd:PRK11176 98 MTMR--RRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 312 PLLFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEalayvaeVWTT 391
Cdd:PRK11176 176 PIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKM-------VSAS 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 392 SVSGMLLK-------VGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPcS 464
Cdd:PRK11176 249 SISDPIIQliaslalAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ-E 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 465 PLSGSLAPSNMKGLVEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQC 544
Cdd:PRK11176 328 KDEGKRVIERAKGDIEFRNVTFTYPGKEV-PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 545 LVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQR 624
Cdd:PRK11176 407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 625 QAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQ 704
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
....*...
gi 239835765 705 LMKRGGCY 712
Cdd:PRK11176 565 LLAQNGVY 572
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
479-717 |
8.91e-67 |
|
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: 220.05 E-value: 8.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAY-PNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQV 557
Cdd:cd03252 1 ITFEHVRFRYkPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKP 637
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 638 LLLILDDATSALDAGNQLRVQRLLYESPkrASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVE 717
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
343-718 |
1.59e-64 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 224.84 E-value: 1.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 343 ALEALSAMPTVRSFANEEGEAQKFRQ---KLEE--MKTLNKkEALAYVAevwtTSVSGMLLKVGILYLGGQLVIRGAVSS 417
Cdd:PRK13657 198 VSDAIGNVSVVQSYNRIEAETQALRDiadNLLAaqMPVLSW-WALASVL----NRAASTITMLAILVLGAALVQKGQLRV 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 418 GNLVSFV-LYQL------QFTQAVQVLLSLYPSMQKavgssekIFEYLDRTPCSPLSGSLA-PSNMKGLVEFQDVSFAYP 489
Cdd:PRK13657 273 GEVVAFVgFATLligrldQVVAFINQVFMAAPKLEE-------FFEVEDAVPDVRDPPGAIdLGRVKGAVEFDDVSFSYD 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 490 NqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGR 569
Cdd:PRK13657 346 N--SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNR 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 570 SFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSAL 649
Cdd:PRK13657 424 SIEDNIRVG-RPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 650 DAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVEA 718
Cdd:PRK13657 503 DVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
479-694 |
7.73e-64 |
|
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: 209.93 E-value: 7.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVA 558
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGRSFRENIayglnrtptmeeitavavesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPL 638
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESPKRasRTVLLITQQLSLAEQAHHILFLREG 694
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
176-434 |
1.15e-59 |
|
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: 202.49 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 176 GEMAIPFFTGRITDWILQDKTVPSF--TRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFL 253
Cdd:pfam00664 14 ISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 254 KNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQ 333
Cdd:pfam00664 94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 334 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRG 413
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
|
250 260
....*....|....*....|.
gi 239835765 414 AVSSGNLVSFVLYQLQFTQAV 434
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
251-718 |
1.41e-58 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 211.14 E-value: 1.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 251 FFLKNPAGSITSRVTeDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAV 330
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNH 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 331 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMktLNKKEALAYVAEVWTT--SVSGMLLKVGILYLGGQ 408
Cdd:TIGR01193 325 DAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDY--LNKSFKYQKADQGQQAikAVTKLILNVVILWTGAY 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 409 LVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFE-YLDRTPCSPLSGSLAPSNMKGLVEFQDVSFA 487
Cdd:TIGR01193 403 LVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINKKKRTELNNLNGDIVINDVSYS 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 488 YPNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLF 567
Cdd:TIGR01193 483 YGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 GRSFRENIAYGLNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATS 647
Cdd:TIGR01193 561 SGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 648 ALDAgnqLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVEA 718
Cdd:TIGR01193 641 NLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
477-694 |
3.01e-57 |
|
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: 193.96 E-value: 3.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 477 GLVEFQDVSFAYPNQPKVqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQ 556
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 636
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLG-APLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 637 PLLLILDDATSALDAGNQLRVQRLLYESPkrASRTVLLITQQLSLAEQAHHILFLREG 694
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
400-718 |
6.89e-54 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 195.49 E-value: 6.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 400 VGILYLGGQLVIRGAVSSGNLVSFVLY-QL---QFTQAVQVLLSLYPSMQKAvgssEKIFEYLDRTPCSPLSGSLAP-SN 474
Cdd:TIGR01192 255 MCILVIGTVLVIKGELSVGEVIAFIGFaNLligRLDQMSGFITQIFEARAKL----EDFFDLEDSVFQREEPADAPElPN 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLH 554
Cdd:TIGR01192 331 VKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALI 634
Cdd:TIGR01192 409 KSIATVFQDAGLFNRSIRENIRLG-REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAIL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 635 RKPLLLILDDATSALDAGNQLRVQRLLyeSPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRA 714
Cdd:TIGR01192 488 KNAPILVLDEATSALDVETEARVKNAI--DALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYK 565
|
....
gi 239835765 715 MVEA 718
Cdd:TIGR01192 566 LLRR 569
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
396-708 |
7.63e-54 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 194.97 E-value: 7.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 396 MLLKVGILYLGGQLVIRGAVSSGN------LVSFVLyqlqftQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPCSPLSGS 469
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAmiaasiLMGRAL------APIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 470 L-APsnmKGLVEFQDVSFAYPNQPKVqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQY 548
Cdd:COG4618 324 LpRP---KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 549 DHHYLHTQVAAVGQEPLLFGRSFRENIAyglnR--TPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQA 626
Cdd:COG4618 400 DREELGRHIGYLPQDVELFDGTIAENIA----RfgDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQR 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLM 706
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
..
gi 239835765 707 KR 708
Cdd:COG4618 555 AR 556
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
239-723 |
2.04e-52 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 191.47 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 239 EVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLP 318
Cdd:PRK10790 103 DVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVM 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 319 KKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVrsfaneegeaQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLL 398
Cdd:PRK10790 183 VIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVI----------QQFRQQARFGERMGEASRSHYMARMQTLRLDGFLL 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 399 K-----VGILYLGGQLVI-----RGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRtPCSPLSG 468
Cdd:PRK10790 253 RpllslFSALILCGLLMLfgfsaSGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDG-PRQQYGN 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 469 SLAPSNmKGLVEFQDVSFAYPNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQY 548
Cdd:PRK10790 332 DDRPLQ-SGRIDIDNVSFAYRDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 549 DHHYLHTQVAAVGQEPLLFGRSFRENIAYGlnRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVA 628
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLA 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKR 708
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
490 500
....*....|....*....|.
gi 239835765 709 GGCYRAMV------EALAAPA 723
Cdd:PRK10790 565 QGRYWQMYqlqlagEELAASV 585
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
238-691 |
1.44e-51 |
|
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: 187.88 E-value: 1.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 238 REVFRAVLRQETGFFLKNPAGSITSRVTEDTanvcESISGTLSLLLWYLGRA----LCLLVFMFWGSPYLTLVTLINLPL 313
Cdd:TIGR02857 81 ERLLEAVAALGPRWLQGRPSGELATLALEGV----EALDGYFARYLPQLVLAvivpLAILAAVFPQDWISGLILLLTAPL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 314 LFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKTLNKKEALAYVAEV 388
Cdd:TIGR02857 157 IPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEyrertMRVLRIAFLSSAVLEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 389 WTT-SVSGMLLKVGILYLGGQLVIRGAVssgnlvsFVLYQL-QFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRT--PCS 464
Cdd:TIGR02857 237 FATlSVALVAVYIGFRLLAGDLDLATGL-------FVLLLApEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAprPLA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 465 PLSGSLAPSNMKglVEFQDVSFAYPNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQC 544
Cdd:TIGR02857 310 GKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 545 LVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLnRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQR 624
Cdd:TIGR02857 386 LADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR-PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQA 464
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 625 QAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRasRTVLLITQQLSLAEQAHHILFL 691
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
176-454 |
8.81e-51 |
|
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: 178.69 E-value: 8.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 176 GEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKN 255
Cdd:cd18590 11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 256 PAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQES 335
Cdd:cd18590 91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 336 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAV 415
Cdd:cd18590 171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 239835765 416 SSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18590 251 TTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
238-715 |
5.58e-49 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 181.45 E-value: 5.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 238 REVF-RAVLRQETGFFLKNPAGSITSRVTEDTANVCESI-SGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLF 315
Cdd:PRK10789 72 REDFyRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAgEGVLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 316 LLPKKLG-KVHQ--SLAVKVQESLAKSTQvalEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNkkealAYVAEVWTTS 392
Cdd:PRK10789 152 IMIKRYGdQLHErfKLAQAAFSSLNDRTQ---ESLTSIRMIKAFGLEDRQSALFAADAEDTGKKN-----MRVARIDARF 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 393 VSGMLLKVGILYL-----GGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPCSpLS 467
Cdd:PRK10789 224 DPTIYIAIGMANLlaiggGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVV-KD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 468 GSLAPSNMKGLVEFQDVSFAYPnQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQ 547
Cdd:PRK10789 303 GSEPVPEGRGELDVNIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 548 YDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 627
Cdd:PRK10789 382 LQLDSWRSRLAVVSQTPFLFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRI 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 628 ALARALIRKPLLLILDDATSALDAgnQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMK 707
Cdd:PRK10789 461 SIARALLLNAEILILDDALSAVDG--RTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
....*...
gi 239835765 708 RGGCYRAM 715
Cdd:PRK10789 539 QSGWYRDM 546
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
396-707 |
6.23e-49 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 180.62 E-value: 6.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 396 MLLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPCSPLSGSLApsNM 475
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLP--EP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 476 KGLVEFQDVSFAYPNQPKVqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHT 555
Cdd:TIGR01842 314 EGHLSVENVTIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGRSFRENIAYgLNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIR 635
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 636 KPLLLILDDATSALD-AGNQLRVQRLLyeSPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMK 707
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDeEGEQALANAIK--ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
477-701 |
1.45e-44 |
|
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: 1.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 477 GLVEFQDVSFAY-PNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHT 555
Cdd:cd03244 1 GDIEFKNVSLRYrPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGRSFRENIAyglnrtP----TMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALAR 631
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLYEspKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
441-715 |
3.78e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 161.94 E-value: 3.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 441 YPSMQKAVGSSEKIFEYLDRTPCSPLSGSLAPSNMKGL-VEFQDVSFAYPNQpkvQVLQG-LTFTLHPGTVTALVGPNGS 518
Cdd:PRK11174 311 YHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDPVtIEAEDLEILSPDG---KTLAGpLNFTLPAGQRIALVGPSGA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 519 GKST-VAALLQNL-YQptgGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESG 596
Cdd:PRK11174 388 GKTSlLNALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG-NPDASDEQLQQALENAW 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 597 AHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpkRASRTVLLIT 676
Cdd:PRK11174 464 VSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVT 541
|
250 260 270
....*....|....*....|....*....|....*....
gi 239835765 677 QQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAM 715
Cdd:PRK11174 542 HQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-647 |
3.59e-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: 147.41 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGR-SFRENI 575
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 576 AYGLNrtptMEEITAVAVESGAHDFISGFPQGY--DTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATS 647
Cdd:pfam00005 81 RLGLL----LKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
361-719 |
7.21e-41 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 158.06 E-value: 7.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 361 GEAQKFRQKLE--EMKTLNKKEALAYV---AEVWTTSVSGMLLkVGILYLGGQLViRGAVSSGNLVS-FVLYQLQFTQAV 434
Cdd:PRK11160 217 GAEDRYRQQLEqtEQQWLAAQRRQANLtglSQALMILANGLTV-VLMLWLAAGGV-GGNAQPGALIAlFVFAALAAFEAL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 435 QVLLSLYPSMQKAVGSSEKIFEYLDRTPCSPLSGSLAPSNMKGLVEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVG 514
Cdd:PRK11160 295 MPVAGAFQHLGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 515 PNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLNrTPTMEEITAVAVE 594
Cdd:PRK11160 374 RTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEVLQQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 595 SGAHDFISGfPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLL 674
Cdd:PRK11160 453 VGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLM 529
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 239835765 675 ITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVEAL 719
Cdd:PRK11160 530 ITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
480-694 |
1.07e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAA 559
Cdd:COG4619 2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQEPLLFGRSFRENIAYGL---NRTPTMEEITAVAVEsgahdFisGFPQGY-DTEVgetgNQLSGGQRQAVALARALIR 635
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFqlrERKFDRERALELLER-----L--GLPPDIlDKPV----ERLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREG 694
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
394-679 |
1.36e-40 |
|
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: 156.37 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 394 SGMLLKVGILYLGGQLVIRGAVSSGN-----LVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPCSPLSG 468
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRlapvtLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 469 SLAPSNM---KGLVEFQDVSFAYPNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCL 545
Cdd:TIGR02868 322 APAAGAVglgKPTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 546 VQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQ 625
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQ 478
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQL 679
Cdd:TIGR02868 479 RLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHHL 530
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
178-454 |
9.85e-40 |
|
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: 148.05 E-value: 9.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVP-----SFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFF 252
Cdd:cd18573 13 MSVPFAIGKLIDVASKESGDIeifglSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 253 LKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKV 332
Cdd:cd18573 93 DKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 333 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIR 412
Cdd:cd18573 173 QDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVAS 252
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 239835765 413 GAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18573 253 GELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
203-717 |
1.30e-39 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 157.88 E-value: 1.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 203 NIWLMSILTIASTAleFASDGI---YNITMGH-MHGRVHREVFRAVLRQETGFFL--KNPAGSITSRVTEDTANVCESIS 276
Cdd:PTZ00265 866 NKYSLYILVIAIAM--FISETLknyYNNVIGEkVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLV 943
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 277 GTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAKSTQVAL------------ 344
Cdd:PTZ00265 944 NNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYnsddeifkdpsf 1023
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 345 ---EALSAMPTVRSFANEEGEAqKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVI-RGAVSSGNL 420
Cdd:PTZ00265 1024 liqEAFYNMNTVIIYGLEDYFC-NLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIrRGTILVDDF 1102
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 421 VSfVLYQLQFTQA-VQVLLSLYPSMQKAVGSSEKIFEYLDRTPCSPL--SGSLAPSN---MKGLVEFQDVSFAYPNQPKV 494
Cdd:PTZ00265 1103 MK-SLFTFLFTGSyAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIRIKNkndIKGKIEIMDVNFRYISRPNV 1181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY------------QPTG--------------------------- 535
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneqdyqgdeeqnvgmknvnefslt 1261
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 536 ---------------GQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlNRTPTMEEITAVAVESGAHDF 600
Cdd:PTZ00265 1262 keggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACKFAAIDEF 1340
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 601 ISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS 680
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1420
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 239835765 681 LAEQAHHILFL----REGS-VGEQGTHLQLMK-RGGCYRAMVE 717
Cdd:PTZ00265 1421 SIKRSDKIVVFnnpdRTGSfVQAHGTHEELLSvQDGVYKKYVK 1463
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
479-701 |
1.54e-39 |
|
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: 145.55 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVA 558
Cdd:COG1122 1 IELENLSFSYPGG--TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPL--LFGRSFRENIAYGL-NRTPTMEEITAVAVES----GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 631
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPeNLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRaSRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
177-454 |
2.43e-39 |
|
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: 146.93 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 177 EMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNP 256
Cdd:cd07346 15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 257 AGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESL 336
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 337 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLN-KKEALAYVAEVWTTSVSGMLLkVGILYLGGQLVIRGAV 415
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANlRAARLSALFSPLIGLLTALGT-ALVLLYGGYLVLQGSL 253
|
250 260 270
....*....|....*....|....*....|....*....
gi 239835765 416 SSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd07346 254 TIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
178-454 |
2.95e-39 |
|
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: 147.01 E-value: 2.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVPSFTRN-------IWLMSILTIASTAlEFASDGIYNITMGHMHGRVHREVFRAVLRQETG 250
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGEEALralnqavLILLGVVLIGSIA-TFLRSWLFTLAGERVVARLRKRLFSAIIAQEIA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 251 FFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAV 330
Cdd:cd18780 92 FFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 331 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLV 410
Cdd:cd18780 172 KFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLV 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 239835765 411 IRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18780 252 IDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
475-708 |
5.06e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 151.59 E-value: 5.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQPkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGQCLVQYDHH 551
Cdd:COG1123 1 MTPLLEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 YLHTQVAAVGQEPL--LFGRSFRENIAYGL-NRTPTMEEITAVAVES----GAHDFISGFPQgydtevgetgnQLSGGQR 624
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALeNLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 625 QAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSL-AEQAHHILFLREGSVGEQGTHL 703
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPE 228
|
....*
gi 239835765 704 QLMKR 708
Cdd:COG1123 229 EILAA 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
478-701 |
5.85e-39 |
|
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: 144.80 E-value: 5.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQV 557
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLL-FGRSFRENIAYGlnRTPTM----------EEITAVAVES-GAHDFIsgfpqgyDTEVgetgNQLSGGQRQ 625
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALG--RYPHLglfgrpsaedREAVEEALERtGLEHLA-------DRPV----DELSGGERQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
478-700 |
1.74e-38 |
|
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: 142.64 E-value: 1.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHH---YL 553
Cdd:cd03257 1 LLEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQEPLL-------FGRSFRE--NIAYGLNRTPTMEEITAVAVESG--AHDFISGFPqgydtevgetgNQLSGG 622
Cdd:cd03257 81 RKEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVglPEEVLNRYP-----------HELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 623 QRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
479-695 |
3.18e-38 |
|
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: 141.07 E-value: 3.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYP--NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTV-AALLQNLyQPTGGQLlldgqclvqydhhYLHT 555
Cdd:cd03250 1 ISVEDASFTWDsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGRSFRENIAYGLnrtpTMEE------ITAVAVESgahDfISGFPQGYDTEVGETGNQLSGGQRQAVAL 629
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFGK----PFDEeryekvIKACALEP---D-LEILPDGDLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 630 ARALIRKPLLLILDDATSALDAgnqlRVQRLLYES----PKRASRTVLLITQQLSLAEQAHHILFLREGS 695
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDA----HVGRHIFENcilgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
480-694 |
4.56e-38 |
|
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: 140.68 E-value: 4.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAA 559
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQEP--LLFGRSFRENIAYGL-NRTPTMEEITAVAVESGAHDFISGFpQGYDTEvgetgnQLSGGQRQAVALARALIRK 636
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLeNLGLPEEEIEERVEEALELVGLEGL-RDRSPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 637 PLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLS-LAEQAHHILFLREG 694
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
235-715 |
1.25e-37 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 151.64 E-value: 1.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 235 RVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVtlINLPLL 314
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVI--IPPLGL 1116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 315 FLLPKKLGKVHQSLAVKVQESLAKSTQVAL--EALSAMPTVRSFANEEGEAQKFRQKLEEmktlNKKEALAYVaevwtts 392
Cdd:TIGR00957 1117 LYFFVQRFYVASSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSI------- 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 393 VSGMLLKVGILYLGGQLVI---------RGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRTPC 463
Cdd:TIGR00957 1186 VANRWLAVRLECVGNCIVLfaalfavisRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 464 SP--LSGSLAPSNM--KGLVEFQDVSFAYpnQPKVQ-VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL 538
Cdd:TIGR00957 1266 APwqIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 539 LLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI-AYGlnrTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGN 617
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGE 1420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 618 QLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQ---RLLYESPkrasrTVLLITQQLSLAEQAHHILFLREG 694
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQstiRTQFEDC-----TVLTIAHRLNTIMDYTRVIVLDKG 1495
|
490 500
....*....|....*....|.
gi 239835765 695 SVGEQGTHLQLMKRGGCYRAM 715
Cdd:TIGR00957 1496 EVAEFGAPSNLLQQRGIFYSM 1516
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
478-701 |
2.00e-37 |
|
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: 140.32 E-value: 2.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPK-VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQ 556
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLL-------FGRSFRENIAyGLNRTPTMEEITAVAVESG-AHDFISGFPqgydtevgetgNQLSGGQRQAVA 628
Cdd:COG1124 81 VQMVFQDPYAslhprhtVDRILAEPLR-IHGLPDREERIAELLEQVGlPPSFLDRYP-----------HQLSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
479-676 |
4.13e-37 |
|
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: 138.37 E-value: 4.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPN-QPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQydhhyLHTQV 557
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFG-RSFRENIAYGLN-RTPTMEEITAVAVES----GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 631
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLElQGVPKAEARERAEELlelvGLSGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVT 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
449-701 |
4.93e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 145.82 E-value: 4.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 449 GSSEKIFEYLDRTPCSPLSGSLAPSNMKG------LVEFQDVSFAYPNQPK--VQVLQGLTFTLHPGTVTALVGPNGSGK 520
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAaaaaepLLEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 521 STVAALLQNLYQPTGGQLLLDGQCLVQYDH---HYLHTQVAAVGQEPL--LFGR-SFRENIAYGL--NRTPTMEEITAVA 592
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNPRmTVGDIIAEPLrlHGLLSRAERRERV 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 593 VES----G-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKR 667
Cdd:COG1123 385 AELlervGlPPDLADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRE 453
|
250 260 270
....*....|....*....|....*....|....*
gi 239835765 668 ASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG1123 454 LGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
239-695 |
9.78e-37 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 148.64 E-value: 9.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 239 EVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTL-VTLINLPLLFLL 317
Cdd:PTZ00265 135 EFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLcITCVFPLIYICG 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 318 PKKLGKVHqslaVKVQESLA---KSTQVALEALSAMPTVRSFANEEGEAQKFrqKLEEmkTLNKKEALA--YVAEVWTTS 392
Cdd:PTZ00265 215 VICNKKVK----INKKTSLLynnNTMSIIEEALVGIRTVVSYCGEKTILKKF--NLSE--KLYSKYILKanFMESLHIGM 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 393 VSGMLL---KVGILYlGGQLVIRGAVSS--------GNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLDRT 461
Cdd:PTZ00265 287 INGFILasyAFGFWY-GTRIIISDLSNQqpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRK 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 462 PcsplsgsLAPSNMKG-------LVEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPT 534
Cdd:PTZ00265 366 P-------LVENNDDGkklkdikKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 535 GGQLLL-DGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLNRTPTMEEITAVAVESGA---------------- 597
Cdd:PTZ00265 439 EGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEALSNYYNEDGNdsqenknkrnscrakc 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 598 ----------------------------------------HDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKP 637
Cdd:PTZ00265 519 agdlndmsnttdsneliemrknyqtikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNP 598
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 638 LLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFL--REGS 695
Cdd:PTZ00265 599 KILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLsnRERG 658
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
479-708 |
1.90e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.12 E-value: 1.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQyDHHYLHTQVA 558
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGR-SFRENI-----AYGLNRTPTMEEITAVAVESGAHDFIsgfpqgyDTEVGetgnQLSGGQRQAVALARA 632
Cdd:COG1131 77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQLMKR 708
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
480-696 |
4.48e-36 |
|
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: 133.88 E-value: 4.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPKVqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAA 559
Cdd:cd03246 2 EVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQEPLLFGRSFRENIayglnrtptmeeitavavesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPLL 639
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 640 LILDDATSALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQAHHILFLREGSV 696
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
479-694 |
1.75e-35 |
|
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: 133.77 E-value: 1.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDH----HYL 553
Cdd:cd03255 1 IELKNLSKTYGGGGeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQEP-LLFGRSFRENIAYGL----NRTPTMEEITAVAVES-GAHDFISGFPqgydtevgetgNQLSGGQRQAV 627
Cdd:cd03255 81 RRHIGFVFQSFnLLPDLTALENVELPLllagVPKKERRERAEELLERvGLGDRLNHYP-----------SELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREG 694
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
478-701 |
2.73e-35 |
|
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: 133.83 E-value: 2.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLhTQV 557
Cdd:COG4555 1 MIEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFGR-SFRENI-----AYGLNRtptmeEITAVAVESGAHDFisGFPQGYDTEVGEtgnqLSGGQRQAVALAR 631
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIryfaeLYGLFD-----EELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREIL-RALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGS 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
480-700 |
6.79e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 130.63 E-value: 6.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAA 559
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQepllfgrsfreniayglnrtpTMEEItavavesGAHDFIsgfPQGYDTevgetgnqLSGGQRQAVALARALIRKPLL 639
Cdd:cd03214 78 VPQ---------------------ALELL-------GLAHLA---DRPFNE--------LSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239835765 640 LILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
473-676 |
8.78e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 132.91 E-value: 8.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 473 SNMKGLVEFQDVSFAYPNQPK-VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQydhh 551
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 yLHTQVAAVGQEPLLFG-RSFRENIAYGLN-RTPTMEEITAVAVES----GAHDFISGFPqgydtevgetgNQLSGGQRQ 625
Cdd:COG1116 78 -PGPDRGVVFQEPALLPwLTVLDNVALGLElRGVPKAERRERARELlelvGLAGFEDAYP-----------HQLSGGMRQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVT 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
480-694 |
1.60e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 125.82 E-value: 1.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAA 559
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQepllfgrsfreniayglnrtptmeeitavavesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPLL 639
Cdd:cd00267 78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 640 LILDDATSALDAGNQLRVQRLLYESPKRAsRTVLLITQQLSLAEQA-HHILFLREG 694
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
475-699 |
1.82e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 128.24 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPN-QPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHhyl 553
Cdd:COG1136 1 MSPLLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 hTQVAA--------VGQEPLLFGR-SFRENIAY-----GLNRTPTMEEITAVAVESGAHDFISGFPqgydtevgetgNQL 619
Cdd:COG1136 78 -RELARlrrrhigfVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRP-----------SQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 620 SGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQ 699
Cdd:COG1136 146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
178-454 |
6.17e-33 |
|
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: 128.76 E-value: 6.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPA 257
Cdd:cd18576 13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 258 GSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLA 337
Cdd:cd18576 93 GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 338 KSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAVSS 417
Cdd:cd18576 173 EANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTA 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 239835765 418 GNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18576 253 GDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
204-724 |
6.33e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 137.03 E-value: 6.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 204 IWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSL-- 281
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMfm 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 282 -LLWYLgralcLLVFMFWGSpyLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQ--ESLAKSTQVAL--EALSAMPTVRSF 356
Cdd:PLN03232 1033 nQLWQL-----LSTFALIGT--VSTISLWAIMPLLILFYAAYLYYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 357 aneegeaqkfrQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLV-------IRGAVSSGNLVSF------ 423
Cdd:PLN03232 1106 -----------KAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIwltatfaVLRNGNAENQAGFastmgl 1174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 424 -VLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIFEYLD------------RTPCS-PLSGSlapsnmkglVEFQDVSFAY- 488
Cdd:PLN03232 1175 lLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDlpseataiiennRPVSGwPSRGS---------IKFEDVHLRYr 1245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 489 PNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFG 568
Cdd:PLN03232 1246 PGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 RSFRENIayglnrTPTMEEITAVAVES--GAH--DFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDD 644
Cdd:PLN03232 1324 GTVRFNI------DPFSEHNDADLWEAleRAHikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 645 ATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKR-GGCYRAMVEAlAAPA 723
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIREEFK--SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRdTSAFFRMVHS-TGPA 1474
|
.
gi 239835765 724 D 724
Cdd:PLN03232 1475 N 1475
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
479-700 |
6.81e-33 |
|
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: 125.12 E-value: 6.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHyLHTQVA 558
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGRSFRENIayglnrtptmeeitavavesgahdfisgfpqgydtevgetGNQLSGGQRQAVALARALIRKPL 638
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQAHHILFLREGSVGEQG 700
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
479-700 |
2.95e-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: 124.60 E-value: 2.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY-----QPTGGQLLLDGQ--CLVQYDHH 551
Cdd:cd03260 1 IELRDLNVYYGD---KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKdiYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 YLHTQVAAVGQEPLLFGRSFRENIAYGLN-----RTPTMEEITAVAVESGahdfisgfpqGYDTEVGE--TGNQLSGGQR 624
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKA----------ALWDEVKDrlHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 625 QAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
479-700 |
1.25e-31 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 122.63 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYLHTQ-- 556
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-----DVTGVPPErr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 -VAAVGQEPLLF-GRSFRENIAYGL-NRTPTMEEITAVAVESGAHDFISGFPQGYDTEvgetgnqLSGGQRQAVALARAL 633
Cdd:cd03259 73 nIGMVFQDYALFpHLTVAENIAFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 634 IRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSVGEQG 700
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEAlALADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
479-709 |
1.56e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 124.08 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHY-LHTQV 557
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEP--LLFGRSFRENIAYGL-NR---TPTMEEITAVAVES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALA 630
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLeNLgvpREEMRKRVDEALKLvGMEDFRDREPH-----------LLSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 631 RALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRG 709
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
474-709 |
6.97e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 122.43 E-value: 6.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 474 NMKGLVEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYL 553
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQEP--LLFGRSFRENIAYGL--NRTPTMEEITAV--AVES-GAHDFISGFPqgydtevgetgNQLSGGQRQA 626
Cdd:PRK13635 80 RRQVGMVFQNPdnQFVGATVQDDVAFGLenIGVPREEMVERVdqALRQvGMEDFLNREP-----------HRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 627 VALARALIRKPLLLILDDATSALD-AGNQ--LRVQRLLyespKRASR-TVLLITQQLSLAEQAHHILFLREGSVGEQGTH 702
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDpRGRRevLETVRQL----KEQKGiTVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
....*..
gi 239835765 703 LQLMKRG 709
Cdd:PRK13635 225 EEIFKSG 231
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
479-696 |
1.01e-30 |
|
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: 118.65 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHtQVA 558
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGR-SFRENIayglnrtptmeeitavavesgahdfisgfpqgydtevgetgnQLSGGQRQAVALARALIRKP 637
Cdd:cd03230 77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 638 LLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSV 696
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
479-694 |
1.60e-30 |
|
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: 118.06 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHY--LHTQ 556
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLF-GRSFRENIAYGLnrtptmeeitavavesgahdfisgfpqgydtevgetgnqlSGGQRQAVALARALIR 635
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALGL----------------------------------------SGGQQQRVALARALAM 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREG 694
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
178-454 |
3.35e-30 |
|
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: 121.04 E-value: 3.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFT---GRITD----WILQDKTVPSF----TRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLR 246
Cdd:cd18577 13 AALPLMTivfGDLFDaftdFGSGESSPDEFlddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 247 QETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQ 326
Cdd:cd18577 93 QDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 327 SLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLG 406
Cdd:cd18577 173 KYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYG 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 239835765 407 GQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18577 253 SRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
478-708 |
8.80e-30 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 118.07 E-value: 8.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQ 556
Cdd:cd03258 1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVG----QEPLLFGRSFRENIAYGLN--RTPtMEEITAVAVE----SGAHDFISGFPqgydtevgetgNQLSGGQRQA 626
Cdd:cd03258 81 RRRIGmifqHFNLLSSRTVFENVALPLEiaGVP-KAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQL 705
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 239835765 706 MKR 708
Cdd:cd03258 229 FAN 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
479-708 |
1.67e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 118.75 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGQCLVQYDHHYLHT 555
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEP--LLFGRSFRENIAYGL-NRT---PTMEEITA-VAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 628
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLeNRAvprPEMIKIVRdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKR 708
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
474-696 |
1.87e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.11 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 474 NMKGLVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKST-VAALLqNLYQPTGGQLLLDGQCLVQYDHHy 552
Cdd:COG1121 2 MMMPAIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 lhtqVAAVGQEpLLFGRSF----RENIAYGLN------RTPTMEEITAV--AVES-GAHDFIsgfpqgyDTEVGEtgnqL 619
Cdd:COG1121 77 ----IGYVPQR-AEVDWDFpitvRDVVLMGRYgrrglfRRPSRADREAVdeALERvGLEDLA-------DRPIGE----L 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 620 SGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSV 696
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
474-707 |
1.97e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 474 NMKGLVEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYL 553
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQEP--LLFGRSFRENIAYGL-NRTPTMEE----ITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQA 626
Cdd:PRK13632 82 RKKIGIIFQNPdnQFIGATVEDDIAFGLeNKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLM 706
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
.
gi 239835765 707 K 707
Cdd:PRK13632 231 N 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
478-688 |
1.38e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 113.73 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYlHTQV 557
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFGR-SFRENIAY---GLNRTPTMEEITAVAVESGAHDFIsgfpqgyDTEVGetgnQLSGGQRQAVALARAL 633
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRFwaaLYGLRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 634 IRKPLLLILDDATSALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQAHHI 688
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELI-AAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
179-454 |
1.50e-28 |
|
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: 115.98 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTvpsfTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRV----HREVFRAVLRQETGFFLK 254
Cdd:cd18552 17 ALAWLLKPLLDDIFVEKD----LEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVvrdlRNDLFDKLLRLPLSFFDR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 255 NPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQE 334
Cdd:cd18552 93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 335 SLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealAYVAEVWTTSVS---GMLLKVGILYLGGQLVI 411
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMK---IARARALSSPLMellGAIAIALVLWYGGYQVI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 239835765 412 RGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18552 250 SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
483-697 |
2.65e-28 |
|
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: 112.74 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 483 DVSFAYPNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDhhyLHTQVAAVGQ 562
Cdd:cd03226 4 NISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 EP--LLFGRSFRENIAYGLNRTPTMEEITAVAVES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPLL 639
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 640 LILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLS-LAEQAHHILFLREGSVG 697
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
479-701 |
1.27e-27 |
|
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: 111.82 E-value: 1.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQC---LVQYDHHYLHT 555
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGR-SFRENIAYGLNRTPTM--EEITAVAVE-------SGAHDFisgFPqgydtevgetgNQLSGGQRQ 625
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREIVLEkleavglRGAEDL---YP-----------AELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
479-696 |
3.33e-27 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 110.14 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLY---QPTGGQLLLDGQCLVQYDHH---Y 552
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LHTQVAAVGQE-PLLFGRSFRENIAY-----GLNRTPTMEEITAVAVESGAHDFISGFPqgydtevgetgNQLSGGQRQA 626
Cdd:COG2884 77 LRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQAHH-ILFLREGSV 696
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
475-701 |
3.53e-27 |
|
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: 110.45 E-value: 3.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLH 554
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVG---QEPLLFGrSF--RENIAYGLNRTPTM--EEITAVAVE-------SGAHDFisgFPqgydtevgetgNQLS 620
Cdd:COG1127 79 ELRRRIGmlfQGGALFD-SLtvFENVAFPLREHTDLseAEIRELVLEklelvglPGAADK---MP-----------SELS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQL-SLAEQAHHILFLREGSVGEQ 699
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLdSAFAIADRVAVLADGKIIAE 223
|
..
gi 239835765 700 GT 701
Cdd:COG1127 224 GT 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
475-701 |
4.73e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 113.27 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLvqydhhylh 554
Cdd:COG3842 2 AMPALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAA----VG---QEPLLFG-RSFRENIAYGL-NRTPTMEEITAVA------VEsgahdfISGF----Pqgydtevget 615
Cdd:COG3842 70 TGLPPekrnVGmvfQDYALFPhLTVAENVAFGLrMRGVPKAEIRARVaellelVG------LEGLadryP---------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 616 gNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT--QQ--LSLaeqAHHILFL 691
Cdd:COG3842 134 -HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVThdQEeaLAL---ADRIAVM 209
|
250
....*....|
gi 239835765 692 REGSVGEQGT 701
Cdd:COG3842 210 NDGRIEQVGT 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
479-701 |
1.31e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.78 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQcLVQYDHHYLHTQVA 558
Cdd:COG1118 3 IEVRNISKRFGS---FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR-DLFTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFgR--SFRENIAYGL-NRTPTMEEITAVAVE----SGAHDFISGFPqgydtevgetgNQLSGGQRQAVALAR 631
Cdd:COG1118 79 FVFQHYALF-PhmTVAENIAFGLrVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 632 ALIRKPLLLILDDATSALDAgnQLRVQ--RLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSVGEQGT 701
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDA--KVRKElrRWLRRLHDELGGTTVFVTHDQEEAlELADRVVVMNQGRIEQVGT 217
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
478-701 |
2.25e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 109.07 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYpNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQV 557
Cdd:PRK13648 7 IIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEP--LLFGRSFRENIAYGL--NRTPT--MEEITAVAVES-GAHDFISGFPQGydtevgetgnqLSGGQRQAVALA 630
Cdd:PRK13648 86 GIVFQNPdnQFVGSIVKYDVAFGLenHAVPYdeMHRRVSEALKQvDMLERADYEPNA-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 631 RALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
477-701 |
2.29e-26 |
|
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: 107.11 E-value: 2.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 477 GLVEFQDVSFAY-PNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHT 555
Cdd:cd03369 5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGRSFRENI-AYGLNrtpTMEEITAVavesgahdfisgfpqgydTEVGETGNQLSGGQRQAVALARALI 634
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEY---SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 635 RKPLLLILDDATSALDAGNQLRVQRLLYESPKRAsrTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
479-694 |
3.34e-26 |
|
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: 106.85 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQ--YDHHYLHTQ 556
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLFG-RSFRENIAYGLNRTPTMEEITAVAV------ESGAHDFISGFPqgydtevgetgNQLSGGQRQAVAL 629
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERalelleKVGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 630 ARALIRKPLLLILDDATSALD---AGNQLRVQRLLYESpkraSRTVLLITQQLSLA-EQAHHILFLREG 694
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDG 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
235-721 |
5.55e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.84 E-value: 5.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 235 RVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLllwYLGRALCLL-VFMFWGspYLTLVTLINLPL 313
Cdd:PLN03130 987 RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNM---FLGQIFQLLsTFVLIG--IVSTISLWAIMP 1061
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 314 LFLLPKKLGKVHQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFaneegeaqkfrQKLEEMKTLNKKEALAYVAEVW 389
Cdd:PLN03130 1062 LLVLFYGAYLYYQSTAreVKRLDSITRSPVYAQfgEALNGLSTIRAY-----------KAYDRMAEINGRSMDNNIRFTL 1130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 390 TTSVSGMLLKVGILYLGGQLV-------IRGAVSSGNLVSF-------VLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIF 455
Cdd:PLN03130 1131 VNMSSNRWLAIRLETLGGLMIwltasfaVMQNGRAENQAAFastmgllLSYALNITSLLTAVLRLASLAENSLNAVERVG 1210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 456 EYLDRTPCSPL--SGSLAPSN--MKGLVEFQDVSFAY-PNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNL 530
Cdd:PLN03130 1211 TYIDLPSEAPLviENNRPPPGwpSSGSIKFEDVVLRYrPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI 1288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 531 YQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIayglnrTPTMEEITAVAVES--GAH--DFISGFPQ 606
Cdd:PLN03130 1289 VELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLWESleRAHlkDVIRRNSL 1362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 607 GYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQAH 686
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK--SCTMLIIAHRLNTIIDCD 1440
|
490 500 510
....*....|....*....|....*....|....*.
gi 239835765 687 HILFLREGSVGEQGTHLQL-MKRGGCYRAMVEALAA 721
Cdd:PLN03130 1441 RILVLDAGRVVEFDTPENLlSNEGSAFSKMVQSTGA 1476
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
240-717 |
5.74e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 114.69 E-value: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 240 VFRAVLRQeTGFFLKN-PAGSITSRVTEDtANVCESIsgtlslllwylgralCLLVFMFWGSPYLTLVTLINLPLLFLLP 318
Cdd:PLN03232 380 IFHKSLRL-THEARKNfASGKVTNMITTD-ANALQQI---------------AEQLHGLWSAPFRIIVSMVLLYQQLGVA 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 319 KKLGKV-------HQSLAVKVQESLAKS------TQVAL--EALSAMPTVRSFANE---EGEAQKFRQklEEMKTLNKKE 380
Cdd:PLN03232 443 SLFGSLilfllipLQTLIVRKMRKLTKEglqwtdKRVGIinEILASMDTVKCYAWEksfESRIQGIRN--EELSWFRKAQ 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 381 ALAYVAE--VWTTSVSGMLLKVGI-LYLGGQLVIRGAVSSGNLVSFVLYQLQ-----FTQAVQVLLSLyPSMQKAVGSSE 452
Cdd:PLN03232 521 LLSAFNSfiLNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLFAVLRSPLNmlpnlLSQVVNANVSL-QRIEELLLSEE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 453 KIFeyldrTPCSPLSGSlAPSnmkglVEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGK-STVAALLQNLY 531
Cdd:PLN03232 600 RIL-----AQNPPLQPG-APA-----ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELS 668
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 532 QPTGGQLLLDGQclvqydhhylhtqVAAVGQEPLLFGRSFRENIAYGLNRTPTmEEITAVAVESGAHDfISGFPqGYD-T 610
Cdd:PLN03232 669 HAETSSVVIRGS-------------VAYVPQVSWIFNATVRENILFGSDFESE-RYWRAIDVTALQHD-LDLLP-GRDlT 732
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 611 EVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAgnqlRVQRLLYESPKR---ASRTVLLITQQLSLAEQAHH 687
Cdd:PLN03232 733 EIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA----HVAHQVFDSCMKdelKGKTRVLVTNQLHFLPLMDR 808
|
490 500 510
....*....|....*....|....*....|
gi 239835765 688 ILFLREGSVGEQGTHLQLMKRGGCYRAMVE 717
Cdd:PLN03232 809 IILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
238-454 |
8.07e-26 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 107.96 E-value: 8.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 238 REVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLwylgRALCL----LVFMFWGSPYLTLVTLINLPL 313
Cdd:cd18575 73 KAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL----RNLLLliggLVMLFITSPKLTLLVLLVIPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 314 LFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkTLNKkeALAYV-AEVWTTS 392
Cdd:cd18575 149 VVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA--AFAA--ALRRIrARALLTA 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 393 VS---GMLLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18575 225 LViflVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
506-700 |
1.51e-25 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 105.07 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 506 PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHH-YLHTQVAAVG---QEPLLFGR-SFRENIAYGLN 580
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGlvfQQYALFPHlNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 581 RTPTMEEITAVAVESGAHDfISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRL 660
Cdd:cd03297 102 RKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 239835765 661 LYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
240-717 |
1.79e-25 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.29 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 240 VFRAVLRQETGFFLKNPAGSITSRVTEDT---ANVCES----------ISGTLSLLLWYLGRA----LCLLVFMFwgsPY 302
Cdd:PLN03130 380 VFRKSLRLTHEGRKKFTSGKITNLMTTDAealQQICQQlhtlwsapfrIIIAMVLLYQQLGVAsligSLMLVLMF---PI 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 303 LTLVTlinlpllfllpkklgKVHQSLAvkvQESLAKS-TQVAL--EALSAMPTVRSFANEegeaQKFRQKL-----EEMK 374
Cdd:PLN03130 457 QTFII---------------SKMQKLT---KEGLQRTdKRIGLmnEVLAAMDTVKCYAWE----NSFQSKVqtvrdDELS 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 375 TLNKKEALAYVAEVWTTSVSGM--LLKVGIL-YLGGQLVIRGAVSSGNLVS---FVLYQLQ--FTQAVQVLLSLyPSMQK 446
Cdd:PLN03130 515 WFRKAQLLSAFNSFILNSIPVLvtVVSFGVFtLLGGDLTPARAFTSLSLFAvlrFPLFMLPnlITQAVNANVSL-KRLEE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 447 AVGSSEKIFeyldrTPCSPLSGSLAPSNMKglvefqDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGK-STVAA 525
Cdd:PLN03130 594 LLLAEERVL-----LPNPPLEPGLPAISIK------NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISA 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 526 LLQNLYQPTGGQLLLDGQclvqydhhylhtqVAAVGQEPLLFGRSFRENIAYGLNRTPTMEEiTAVAVESGAHDfISGFP 605
Cdd:PLN03130 663 MLGELPPRSDASVVIRGT-------------VAYVPQVSWIFNATVRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLP 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 606 QGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAgnqlRVQRLLYESPKR---ASRTVLLITQQLSLA 682
Cdd:PLN03130 728 GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA----HVGRQVFDKCIKdelRGKTRVLVTNQLHFL 803
|
490 500 510
....*....|....*....|....*....|....*
gi 239835765 683 EQAHHILFLREGSVGEQGTHLQLMKRGGCYRAMVE 717
Cdd:PLN03130 804 SQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
480-691 |
1.83e-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: 104.92 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHhylhtQVAA 559
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQEpLLFGRSF----RENIAYGLN------RTPTMEEITAV--AVES-GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQA 626
Cdd:cd03235 73 VPQR-RSIDRDFpisvRDVVLMGLYghkglfRRLSKADKAKVdeALERvGLSELA-------DRQIGE----LSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRLLyESPKRASRTVLLITQQL-SLAEQAHHILFL 691
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLgLVLEYFDRVLLL 205
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
177-454 |
2.35e-25 |
|
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: 106.83 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 177 EMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRV----HREVFRAVLRQETGFF 252
Cdd:cd18563 15 GLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERItadlRRDLYEHLQRLSLSFF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 253 LKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKV 332
Cdd:cd18563 95 DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 333 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealayVAEVWTT--SVSGMLLKVG---ILYLGG 407
Cdd:cd18563 175 WRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR-----AEKLWATffPLLTFLTSLGtliVWYFGG 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 239835765 408 QLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18563 250 RQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
179-454 |
2.56e-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: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKtvpSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPAG 258
Cdd:cd18551 17 AQPLLVKNLIDALSAGG---SSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 259 SITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAK 338
Cdd:cd18551 94 DLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 339 STQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEAL--AYVAEVWTTSVSGMLLkvGILYLGGQLVIRGAVS 416
Cdd:cd18551 174 LSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKieALIGPLMGLAVQLALL--VVLGVGGARVASGALT 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 239835765 417 SGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18551 252 VGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
479-701 |
2.93e-25 |
|
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: 105.11 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQydHHYLHTQVA 558
Cdd:cd03296 3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGR-SFRENIAYGLNRTPTMEEITAVAVESGAHDFI-----SGFPQGYDtevgetgNQLSGGQRQAVALARA 632
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSVGEQGT 701
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGT 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
480-701 |
3.16e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.84 E-value: 3.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPkvqvlqgLTFTLH--PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYLHTQ- 556
Cdd:COG3840 3 RLDDLTYRYGDFP-------LRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-----DLTALPPAe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 --VAAVGQEPLLFGR-SFRENIAYGLNrtPTM-------EEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQA 626
Cdd:COG3840 71 rpVSMLFQENNLFPHlTVAQNIGLGLR--PGLkltaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 627 VALARALIR-KPLLLiLDDATSALDAGnqLRVQ--RLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG3840 138 VALARCLVRkRPILL-LDEPFSALDPA--LRQEmlDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
178-454 |
4.01e-25 |
|
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: 105.98 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKtvpsFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREV----FRAVLRQETGFFL 253
Cdd:cd18542 16 LLIPLLIRRIIDSVIGGG----LRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLrndlYDHLQRLSFSFHD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 254 KNPAGSITSRVTEDTanvcESISGTLSLLLWYLGRALCLLVF----MFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLA 329
Cdd:cd18542 92 KARTGDLMSRCTSDV----DTIRRFLAFGLVELVRAVLLFIGaliiMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 330 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealayVAEVW-----TTSVSGMLLKVGILY 404
Cdd:cd18542 168 EEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIK-----LAKLLakywpLMDFLSGLQIVLVLW 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 239835765 405 LGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18542 243 VGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
478-651 |
4.44e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.72 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYLHTQ- 556
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE-----PVRFRSPRd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 -----VAAVGQEPLLF-GRSFRENIAygLNRTPT---------MEEITAVAVES-GAHdfISgfPqgyDTEVGEtgnqLS 620
Cdd:COG1129 76 aqaagIAIIHQELNLVpNLSVAENIF--LGREPRrgglidwraMRRRARELLARlGLD--ID--P---DTPVGD----LS 142
|
170 180 190
....*....|....*....|....*....|.
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTE 173
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
475-705 |
5.34e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.56 E-value: 5.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLH 554
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQEP--LLFGRSFRENIAYGLN-----RTPTMEEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAV 627
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQL 705
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
478-700 |
9.69e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 103.63 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLV--QYDHHYLHT 555
Cdd:PRK09493 1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGR-SFRENIAYGLNRT----------PTMEEITAVAVESGAHDFISgfpqgydtevgetgnQLSGGQR 624
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPLRVrgaskeeaekQARELLAKVGLAERAHHYPS---------------ELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 625 QAVALARALIRKPLLLILDDATSALDA---GNQLRVQRLLYESpkraSRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPelrHEVLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDG 218
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
478-701 |
1.78e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 102.76 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHH--YLHT 555
Cdd:COG1126 1 MIEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFG-RSFRENIAYG----LNRTPtmEEITAVAVES----GAHDFISGFPqgydtevgetgNQLSGGQRQA 626
Cdd:COG1126 78 KVGMVFQQFNLFPhLTVLENVTLApikvKKMSK--AEAEERAMELlervGLADKADAYP-----------AQLSGGQQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 627 VALARALIRKPLLLILDDATSALD---AGNQLRVQRLLyespKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG1126 145 VAIARALAMEPKVMLFDEPTSALDpelVGEVLDVMRDL----AKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
478-689 |
1.98e-24 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 104.75 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYP-NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGQCLVQYDH--- 550
Cdd:COG0444 1 LLEVRNLKVYFPtRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 551 -HYLHTQVAAVGQEPL-----LF--GRSFRENIAY--GLNRtptmEEITAVAVE-------SGAHDFISGFPqgydtevg 613
Cdd:COG0444 81 rKIRGREIQMIFQDPMtslnpVMtvGDQIAEPLRIhgGLSK----AEARERAIEllervglPDPERRLDRYP-------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 614 etgNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHIL 689
Cdd:COG0444 149 ---HELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEiADRVA 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
480-696 |
1.99e-24 |
|
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: 102.65 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHT---Q 556
Cdd:cd03256 2 EVENLSKTYPNG--KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLFGR-SFRENIAYG-LNRTPTM--------EEITAVAVES----GAHDFISgfpqgydTEVGetgnQLSGG 622
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGrLGRRSTWrslfglfpKEEKQRALAAlervGLLDKAY-------QRAD----QLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 623 QRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSV 696
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
479-708 |
2.82e-24 |
|
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: 102.38 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVA 558
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLF-GRSFRENIAYglnrTPTMEEITAVAVESGAHDFISGF---PQGYdteVGETGNQLSGGQRQAVALARALI 634
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIAL----VPKLLKWPKEKIRERADELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 635 RKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSVGEQGTHLQLMKR 708
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
495-701 |
4.10e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.16 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLL-FGRSFRE 573
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 574 NIAYGL-----NRTPTMEEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIR------KPLLLIL 642
Cdd:PRK13548 96 VVAMGRaphglSRAEDDALVAAALAQVDLAHLAGRDYP-----------QLSGGEQQRVQLARVLAQlwepdgPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 643 DDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGT 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
495-701 |
5.78e-24 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 101.73 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYL---------HTQVAA---VgQ 562
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarrravlpqHSSLAFpftV-E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 EPLLFGRsfrenIAYGLNRTPTMEEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALI-------R 635
Cdd:COG4559 94 EVVALGR-----APHGSSAAQDRQIVREALALVGLAHLAGRSYQ-----------TLSGGEQQRVQLARVLAqlwepvdG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG4559 158 GPRWLFLDEPTSALDLAHQHAVLRLARQL-ARRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQGT 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
478-694 |
5.89e-24 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 100.97 E-value: 5.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYP-NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylhtQ 556
Cdd:COG4181 8 IIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED----A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAA-----VG----QEPLLFGRSFRENIAYGLN-------RTPTMEEITAVAVESGAHDFisgfPqgydtevgetgNQLS 620
Cdd:COG4181 84 RARlrarhVGfvfqSFQLLPTLTALENVMLPLElagrrdaRARARALLERVGLGHRLDHY----P-----------AQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREG 694
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
475-710 |
8.66e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 8.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLH 554
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQEP--LLFGRSFRENIAYGL-NRTPTMEEITAVAVES----GAHDFISGFPQgydtevgetgnQLSGGQRQAV 627
Cdd:PRK13650 81 HKIGMVFQNPdnQFVGATVEDDVAFGLeNKGIPHEEMKERVNEAlelvGMQDFKEREPA-----------RLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMK 707
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
...
gi 239835765 708 RGG 710
Cdd:PRK13650 230 RGN 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
479-696 |
1.66e-23 |
|
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: 97.50 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqydhhylhtqva 558
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 avgqePLLFgRSFRENIAYGlnrtptmeeITAVavesgaHdfisgfpqgydtevgetgnQLSGGQRQAVALARALIRKPL 638
Cdd:cd03216 63 -----EVSF-ASPRDARRAG---------IAMV------Y-------------------QLSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239835765 639 LLILDDATSALD---AGNQLRVQRLLyespKRASRTVLLITQQLS-LAEQAHHILFLREGSV 696
Cdd:cd03216 103 LLILDEPTAALTpaeVERLFKVIRRL----RAQGVAVIFISHRLDeVFEIADRVTVLRDGRV 160
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
478-708 |
1.79e-23 |
|
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: 105.15 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQ--------PKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVA-ALLQnLyQPTGGQLLLDGQCLVQY 548
Cdd:COG4172 275 LLEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 549 DHHYL-----HTQVaaVGQEPllFG-----RSFRENIAYGL---NRTPTMEEITAVAVESGAhdfisgfpqgydtEVG-- 613
Cdd:COG4172 353 SRRALrplrrRMQV--VFQDP--FGslsprMTVGQIIAEGLrvhGPGLSAAERRARVAEALE-------------EVGld 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 614 -ETGN----QLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHH 687
Cdd:COG4172 416 pAARHryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAlAHR 495
|
250 260
....*....|....*....|.
gi 239835765 688 ILFLREGSVGEQGTHLQLMKR 708
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
478-701 |
1.82e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLvQYDHHYL---H 554
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQEP--LLFGRSFRENIAYG-LNRTPTMEEITAVAVESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALAR 631
Cdd:PRK13639 78 KTVGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFEN-------KPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASrTVLLITQQLSLAE-QAHHILFLREGSVGEQGT 701
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGI-TIIISTHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
479-696 |
2.03e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 99.02 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHH---YLHT 555
Cdd:cd03292 1 IEFINVTKTYPNG--TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQE-PLLFGRSFRENIAYGLN---------RTPTMEEITAVAVESGAHDFisgfpqgydtevgetGNQLSGGQRQ 625
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEvtgvppreiRKRVPAALELVGLSHKHRAL---------------PAELSGGEQQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASrTVLLITQQLSLAEQ-AHHILFLREGSV 696
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGT-TVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
482-706 |
2.04e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.09 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 482 QDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVG 561
Cdd:PRK11231 6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 562 QEPLL-FGRSFRENIAYGlnRTPTM----------EEITAVAVEsgahdfisgfpqgyDTEVGETGNQ----LSGGQRQA 626
Cdd:PRK11231 83 QHHLTpEGITVRELVAYG--RSPWLslwgrlsaedNARVNQAME--------------QTRINHLADRrltdLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQL 705
Cdd:PRK11231 147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEV 225
|
.
gi 239835765 706 M 706
Cdd:PRK11231 226 M 226
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
178-426 |
2.43e-23 |
|
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: 100.95 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDK-TVPSFTRNIWLMSILTIASTALEFasdgIYNITMGHMHGRVHREV----FRAVLRQETGFF 252
Cdd:cd18541 16 LLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRF----LWRYLIFGASRRIEYDLrndlFAHLLTLSPSFY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 253 LKNPAGSITSRVTEDTANVCESIS-GTLslllwYLGRALCL----LVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQS 327
Cdd:cd18541 92 QKNRTGDLMARATNDLNAVRMALGpGIL-----YLVDALFLgvlvLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 328 LAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealayVAEVWTTSVSGMLLKVGI----- 402
Cdd:cd18541 167 RFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR-----LARVDALFFPLIGLLIGLsfliv 241
|
250 260
....*....|....*....|....
gi 239835765 403 LYLGGQLVIRGAVSSGNLVSFVLY 426
Cdd:cd18541 242 LWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
177-454 |
2.68e-23 |
|
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: 100.54 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 177 EMAIPFFTGRITDWILqdKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRV----HREVFRAVLRQETGFF 252
Cdd:cd18544 15 ELLGPLLIKRAIDDYI--VPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIiydlRRDLFSHIQRLPLSFF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 253 LKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKV 332
Cdd:cd18544 93 DRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 333 QESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVI 411
Cdd:cd18544 173 REKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVL 251
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 239835765 412 RGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18544 252 SGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
479-701 |
3.08e-23 |
|
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: 98.85 E-value: 3.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylHTQVA 558
Cdd:cd03300 1 IELENVSKFYGGF---VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGR-SFRENIAYGLNRTPT---------MEEITAVAVESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 628
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGLRLKKLpkaeikervAEALDLVQLEGYANRKPS---------------QLSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 629 LARALIRKPLLLILDDATSALDAgnQLR--VQRLLYESPKRASRTVLLIT--QQ--LSLAEQahhILFLREGSVGEQGT 701
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDL--KLRkdMQLELKRLQKELGITFVFVThdQEeaLTMSDR---IAVMNKGKIQQIGT 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
479-700 |
3.63e-23 |
|
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: 98.33 E-value: 3.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPkvqvlqgLTF--TLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYLHTQ 556
Cdd:cd03298 1 VRLDKIRFSYGEQP-------MHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAPPA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 ---VAAVGQEPLLFGR-SFRENIAYGLNRTPTMEEITAVAVESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARA 632
Cdd:cd03298 69 drpVSMLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
479-705 |
6.53e-23 |
|
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: 97.58 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKVqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqclvqydhHYLHTQVA 558
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--------YSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQE--------PLLFGRSFRENIAY-----GLNRTPTMEEITAVAVESGAHDFIsgfpqgyDTEVGetgnQLSGGQRQ 625
Cdd:cd03263 72 AARQSlgycpqfdALFDELTVREHLRFyarlkGLPKSEIKEEVELLLRVLGLTDKA-------NKRAR----TLSGGMKR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAgnqlRVQRLLYESPK--RASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTH 702
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDP----ASRRAIWDLILevRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSP 216
|
...
gi 239835765 703 LQL 705
Cdd:cd03263 217 QEL 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
476-658 |
7.21e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.18 E-value: 7.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 476 KGLVEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCL--VQYDHHYL 553
Cdd:PRK09452 12 SPLVELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTqvaaVGQEPLLFGR-SFRENIAYGL--NRTP-------TMEEITAVAVEsgahDFISGFPQgydtevgetgnQLSGGQ 623
Cdd:PRK09452 89 NT----VFQSYALFPHmTVFENVAFGLrmQKTPaaeitprVMEALRMVQLE----EFAQRKPH-----------QLSGGQ 149
|
170 180 190
....*....|....*....|....*....|....*
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAgnQLRVQ 658
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALDY--KLRKQ 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
479-701 |
7.32e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 100.54 E-value: 7.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYP-NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQV 557
Cdd:COG1135 2 IELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVG----QEPLLFGRSFRENIAY-----GLNRtptmEEITAVAVE-------SGAHDFisgFPqgydtevgetgNQLSG 621
Cdd:COG1135 82 RKIGmifqHFNLLSSRTVAENVALpleiaGVPK----AEIRKRVAEllelvglSDKADA---YP-----------SQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 622 GQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLyespKRASR----TVLLITQQLSLAEQ-AHHILFLREGSV 696
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLL----KDINRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 239835765 697 GEQGT 701
Cdd:COG1135 220 VEQGP 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
493-706 |
1.31e-22 |
|
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: 96.73 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLvqyDHHYLHTQVAA----VGQEPLLFG 568
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPPHERARAgigyVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 R-SFRENI---AYGLNR---TPTMEEITAVavesgahdfisgFP---QGYDTEVGetgnQLSGGQRQAVALARALIRKPL 638
Cdd:cd03224 89 ElTVEENLllgAYARRRakrKARLERVYEL------------FPrlkERRKQLAG----TLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 639 LLILDDATSAL---------DAgnqlrVQRLlyespKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQLM 706
Cdd:cd03224 153 LLLLDEPSEGLapkiveeifEA-----IREL-----RDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
482-707 |
1.75e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 97.55 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 482 QDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVG 561
Cdd:PRK10575 15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 562 QE-PLLFGRSFRENIAYG-------------LNRTPTMEEITAVAVESGAHDFIsgfpqgydtevgetgNQLSGGQRQAV 627
Cdd:PRK10575 92 QQlPAAEGMTVRELVAIGrypwhgalgrfgaADREKVEEAISLVGLKPLAHRLV---------------DSLSGGERQRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQLM 706
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 239835765 707 K 707
Cdd:PRK10575 237 R 237
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
501-724 |
2.13e-22 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 97.33 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 501 TFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYL----HTQVAAVGQEPLLF-GRSFRENI 575
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 AYGLN-RTPTMEEITAVAVES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPLLLILDDATSALD 650
Cdd:cd03294 124 AFGLEvQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 651 AGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQLmkrggcyramveaLAAPAD 724
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEI-------------LTNPAN 254
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
479-658 |
2.79e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.99 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQydhhyLHTQ-- 556
Cdd:COG3839 4 LELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD-----LPPKdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 -VAAVGQEPLLF-GRSFRENIAYGL-NRTPTMEEItavavesgahdfisgfpqgyDTEVGETG-------------NQLS 620
Cdd:COG3839 76 nIAMVFQSYALYpHMTVYENIAFPLkLRKVPKAEI--------------------DRRVREAAellgledlldrkpKQLS 135
|
170 180 190
....*....|....*....|....*....|....*...
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDAgnQLRVQ 658
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDA--KLRVE 171
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
229-719 |
2.93e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.93 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 229 MGHMHGRVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLtLVTL 308
Cdd:PTZ00243 1026 MRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFV-LVAL 1104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 309 InlpllfllpkKLGKVHQSLAV---------KVQESLAKSTQVAL--EALSAMPTVRSFaneeGEAQKFRQkleemktln 377
Cdd:PTZ00243 1105 V----------PCGYLYYRLMQfynsanreiRRIKSVAKSPVFTLleEALQGSATITAY----GKAHLVMQ--------- 1161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 378 kkEALAYVAEVWTTS----VSGMLLKVGILYLGGQLV-------IRGAVSSGNLVSFVLYQLQFTQAVQV------LLSL 440
Cdd:PTZ00243 1162 --EALRRLDVVYSCSylenVANRWLGVRVEFLSNIVVtvialigVIGTMLRATSQEIGLVSLSLTMAMQTtatlnwLVRQ 1239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 441 YPSMQKAVGSSEKIFEYLDR--------------------------------TPCSPLSGslAPSNMK-GLVEFQDVSFA 487
Cdd:PTZ00243 1240 VATVEADMNSVERLLYYTDEvphedmpeldeevdalerrtgmaadvtgtvviEPASPTSA--APHPVQaGSLVFEGVQMR 1317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 488 YPNQPKVqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLF 567
Cdd:PTZ00243 1318 YREGLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLF 1396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 GRSFRENIAYGLNRTPtmEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLIL-DDAT 646
Cdd:PTZ00243 1397 DGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEAT 1474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 647 SALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQL-MKRGGCYRAMVEAL 719
Cdd:PTZ00243 1475 ANIDPALDRQIQATVMSA--FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMVEAL 1546
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
479-696 |
3.20e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.40 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYL---HT 555
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-----DVTDLppkDR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGR-SFRENIAYGLNRTPTMEEITAVAVESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALI 634
Cdd:cd03301 73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELL------QIEHLLDRKPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 635 RKPLLLILDDATSALDAgnQLRVQ------RLLyespKRASRTVLLITQ-QLSLAEQAHHILFLREGSV 696
Cdd:cd03301 147 REPKVFLMDEPLSNLDA--KLRVQmraelkRLQ----QRLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
179-454 |
7.32e-22 |
|
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: 96.70 E-value: 7.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTVPS------FTRNIWLMSILTIASTALEFasdgIYNITMGHMhgrVHREVFRavLRQET--- 249
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGGGgvdfsgLLRILLLLLGLYLLSALFSY----LQNRLMARV---SQRTVYD--LRKDLfek 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 250 ------GFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGK 323
Cdd:cd18547 88 lqrlplSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 324 VHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMktlnkkealaYVAEVWTTSVSGM------- 396
Cdd:cd18547 168 RSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEEL----------YKASFKAQFYSGLlmpimnf 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 397 ---LLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18547 238 innLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
476-676 |
1.01e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 476 KGLVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHT 555
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPLLFGRSFRENIAYGL---NRTPTMEEITAvavesGAHDFisGFPqgyDTEVGETGNQLSGGQRQAVALARA 632
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIFPWqirNQQPDPAIFLD-----DLERF--ALP---DTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVT 195
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
479-700 |
1.08e-21 |
|
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: 93.80 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkvQVLQGLTFTLHPGtVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQyDHHYLHTQVA 558
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGR-SFRENIAY-----GLNRTPTMEEITAVAVESGAHDFisgfpqgYDTEVGetgnQLSGGQRQAVALARA 632
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPkrASRTVLLITQQLS-LAEQAHHILFLREGSVGEQG 700
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELG--EDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
496-701 |
1.55e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQ-----------------YDHHYLHTQVA 558
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaelrnqklgfiYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQ--EPLLFGRSFRENIayglnRTPTMEEITAVAVESGAHDFISgfpqgydtevgetgnQLSGGQRQAVALARALIRK 636
Cdd:PRK11629 104 ALENvaMPLLIGKKKPAEI-----NSRALEMLAAVGLEHRANHRPS---------------ELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 637 PLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
480-676 |
2.60e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.16 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPN-QPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCL--------VQYDH 550
Cdd:COG4525 5 TVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrgVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 551 HylhtqvaavgqePLLFGRSFRENIAYGLN-RTPTMEEITAVAVES----GAHDFISGFPQgydtevgetgnQLSGGQRQ 625
Cdd:COG4525 85 D------------ALLPWLNVLDNVAFGLRlRGVPKAERRARAEELlalvGLADFARRRIW-----------QLSGGMRQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLIT 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
493-700 |
2.68e-21 |
|
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: 92.67 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVqyDHHYLHTQVAAVGQEPLLFG-RSF 571
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPnLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 RENI-----AYGLNRTPTMEEITAVAVESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:cd03268 90 RENLrllarLLGIRKKRIDEVLDVVGLKDSAKKKVKGF---------------SLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 647 SALDAGNQLRVQRLLYESPKRAsRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQG-ITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
466-718 |
3.00e-21 |
|
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: 93.82 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 466 LSGSLaPSNMKGL---VEFQDVSFAYPNQPKvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG 542
Cdd:cd03288 5 ISGSS-NSGLVGLggeIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 543 QCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLNRT-PTMEEITAVAvesGAHDFISGFPQGYDTEVGETGNQLSG 621
Cdd:cd03288 83 IDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTdDRLWEALEIA---QLKNMVKSLPGGLDAVVTEGGENFSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 622 GQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:cd03288 160 GQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVECDT 237
|
250
....*....|....*...
gi 239835765 702 HLQLM-KRGGCYRAMVEA 718
Cdd:cd03288 238 PENLLaQEDGVFASLVRT 255
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
478-701 |
3.46e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQ------PKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYD-- 549
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNra 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 550 -HHYLHTQVAAVGQEPL-------LFGRSFRENIAY--GLNRTPTMEEITAV--AVESGAHDfISGFPQgydtevgetgn 617
Cdd:PRK10419 83 qRKAFRRDIQMVFQDSIsavnprkTVREIIREPLRHllSLDKAERLARASEMlrAVDLDDSV-LDKRPP----------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 618 QLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSV 696
Cdd:PRK10419 151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
....*
gi 239835765 697 GEQGT 701
Cdd:PRK10419 231 VETQP 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
479-700 |
3.98e-21 |
|
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: 92.34 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHH------- 551
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 ----YLHTQVaavgQEPLLFGRSFReniayGLNRTPTMEEITavavesgahDFISGFpqgydtEVGETGN----QLSGGQ 623
Cdd:cd03269 78 erglYPKMKV----IDQLVYLAQLK-----GLKKEEARRRID---------EWLERL------ELSEYANkrveELSKGN 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03269 134 QQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
494-701 |
4.52e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.03 E-value: 4.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHY---LHTQVAAVGQ-------- 562
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQnpygslnp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 ---------EPLLfgrsfrenIAYGLNRTPTMEEITAVAVESGAHdfisgfPQGYDtevgETGNQLSGGQRQAVALARAL 633
Cdd:PRK11308 108 rkkvgqileEPLL--------INTSLSAAERREKALAMMAKVGLR------PEHYD----RYPHMFSGGQRQRIAIARAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 634 IRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:PRK11308 170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
497-712 |
4.62e-21 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 98.86 E-value: 4.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKST-VAALLQNLYQPTGgqllldgqclvqydHHYLHTQVAAVGQEPLLFGRSFRENI 575
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 AYG--LNRTPTMEEITAVAVESGahdfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAgn 653
Cdd:TIGR00957 720 LFGkaLNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-- 793
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 654 qlRVQRLLYES---PK--RASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQLMKRGGCY 712
Cdd:TIGR00957 794 --HVGKHIFEHvigPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
203-462 |
6.42e-21 |
|
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: 94.06 E-value: 6.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 203 NIWLMSILTIAstALEFASDGIYNITMG----HMHGRVHREVFRAVLRQETGFF--LKNPAGSITSRVTEDTANVCESIS 276
Cdd:cd18578 52 NFWALMFLVLA--IVAGIAYFLQGYLFGiageRLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 277 GTLSLLLwylgRALCLLVF-MFWGSPY---LTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPT 352
Cdd:cd18578 130 DRLGLIL----QAIVTLVAgLIIAFVYgwkLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 353 VRSFANEEGEAQKFRQKLEEMKTLNKKEALayvaevwttsVSGMLLKVG----------ILYLGGQLVIRGAVSSGN-LV 421
Cdd:cd18578 206 VASLTLEDYFLEKYEEALEEPLKKGLRRAL----------ISGLGFGLSqsltffayalAFWYGGRLVANGEYTFEQfFI 275
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 239835765 422 SFVLyqLQFT-QAVQVLLSLYPSMQKAVGSSEKIFEYLDRTP 462
Cdd:cd18578 276 VFMA--LIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
178-454 |
6.93e-21 |
|
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: 93.69 E-value: 6.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVPSftrnIWLMSILTIASTALEFASDGIYNITMGHMHGRV----HREVFRAVLRQETGFFL 253
Cdd:cd18545 17 LAGPYLIKIAIDEYIPNGDLSG----LLIIALLFLALNLVNWVASRLRIYLMAKVGQRIlydlRQDLFSHLQKLSFSFFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 254 KNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQ 333
Cdd:cd18545 93 SRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 334 ESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKeALAYVAEVW----TTSVSGMLLkvgILYLGGQ 408
Cdd:cd18545 173 KKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWplveLISALGTAL---VYWYGGK 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 239835765 409 LVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18545 248 LVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
478-700 |
9.13e-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: 91.28 E-value: 9.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAY-PNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqclvqYDhhyLHTQ 556
Cdd:cd03266 1 MITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FD---VVKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLFGRSF--------RENIAY-----GLNRTPTMEEITAVAVESGAHDFIsgfpqgyDTEVGEtgnqLSGGQ 623
Cdd:cd03266 73 PAEARRRLGFVSDSTglydrltaRENLEYfaglyGLKGDELTARLEELADRLGMEELL-------DRRVGG----FSTGM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALD--AGNQLR--VQRLlyespKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGE 698
Cdd:cd03266 142 RQKVAIARALVHDPPVLLLDEPTTGLDvmATRALRefIRQL-----RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVY 216
|
..
gi 239835765 699 QG 700
Cdd:cd03266 217 EG 218
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
495-700 |
1.20e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.12 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL-----LLDG-------QCLVQYdhhyLHTQVAAVGQ 562
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarslsqqKGLIRQ----LRQHVGFVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 EPLLF-GRSFRENIAYG---LNRTPTmEEITAVAVESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPL 638
Cdd:PRK11264 93 NFNLFpHRTVLENIIEGpviVKGEPK-EEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 639 LLILDDATSALD---AGNQLRVQRLLYESpkraSRTVLLITQQLSLA-EQAHHILFLREGSVGEQG 700
Cdd:PRK11264 165 VILFDEPTSALDpelVGEVLNTIRQLAQE----KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
178-454 |
1.27e-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: 92.93 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASdGIYNITMGH--MHG-RVhrEVFRAVLRQETGFFLK 254
Cdd:cd18550 16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQ-TYLSARIGQgvMYDlRV--QLYAHLQRMSLAFFTR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 255 NPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQE 334
Cdd:cd18550 93 TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 335 SLAKSTQVALEALSA--MPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALayvAEVWTTSVSGMLLKVG---ILYLGGQL 409
Cdd:cd18550 173 KLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQAL---AGRWFFAALGLFTAIGpalVYWVGGLL 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 239835765 410 VIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18550 250 VIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
478-700 |
1.70e-20 |
|
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: 91.30 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQnlyqptggqlLLDGqclvqyDHHylhtqv 557
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKST---LLS----------LITG------DLP------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFGRSF--------RENIAY-------GLNRTPTMEEItavaVESGAHDFIsGFPQGYDTE----------- 611
Cdd:COG1119 55 PTYGNDVRLFGERRggedvwelRKRIGLvspalqlRFPRDETVLDV----VLSGFFDSI-GLYREPTDEqrerarellel 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 612 ------VGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS-LAEQ 684
Cdd:COG1119 130 lglahlADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPG 209
|
250
....*....|....*.
gi 239835765 685 AHHILFLREGSVGEQG 700
Cdd:COG1119 210 ITHVLLLKDGRVVAAG 225
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
487-691 |
1.89e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 487 AYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQydhhYLHTQVAAVGQEPLl 566
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVA----YVPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 567 fgrSFRENIAYG------LNRTPTMEEITAV--AVES-GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALIRKP 637
Cdd:NF040873 73 ---TVRDLVAMGrwarrgLWRRLTRDDRAAVddALERvGLADLA-------GRQLGE----LSGGQRQRALLAQGLAQEA 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 239835765 638 LLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQAHHILFL 691
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
478-701 |
2.11e-20 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 90.81 E-value: 2.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylhtQV 557
Cdd:COG0410 3 MLEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH----RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVG-----QEPLLFGR-SFRENI---AYGLNRTP----TMEEITAVavesgahdfisgFPqgydtEVGE----TGNQLS 620
Cdd:COG0410 76 ARLGigyvpEGRRIFPSlTVEENLllgAYARRDRAevraDLERVYEL------------FP-----RLKErrrqRAGTLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSAL------DAGNQLRvqRLlyespKRASRTVLLITQQLSLAEQ-AHHILFLRE 693
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPSLGLapliveEIFEIIR--RL-----NREGVTILLVEQNARFALEiADRAYVLER 211
|
....*...
gi 239835765 694 GSVGEQGT 701
Cdd:COG0410 212 GRIVLEGT 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
478-701 |
2.80e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 91.40 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYpnQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQV 557
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEP--LLFGRSFRENIAYGLNRTPTMEEITAVAVESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR 635
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSL-AEQAHHILFLREGSVGEQGT 701
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRIVAYGT 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
469-678 |
3.01e-20 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.87 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 469 SLAPSNMKGLVEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNL--------YQPTGGQLLL 540
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 541 DGQCLvqYDHHY----LHTQVAAVGQEPLLFGRSFRENIAYGL------NRTpTMEEItavaVES---GAH--Dfisgfp 605
Cdd:COG1117 76 DGEDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgikSKS-ELDEI----VEEslrKAAlwD------ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 606 qgydtEV----GETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRasRTVLLIT---QQ 678
Cdd:COG1117 143 -----EVkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVThnmQQ 215
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
494-650 |
3.28e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.49 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYL---HTQVAAVGQEPllfgrs 570
Cdd:COG4608 31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP------ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 571 freniaYG-LNRTPTMEEITAVAVEsgAHDFISGfpQGYDTEVGET----G----------NQLSGGQRQAVALARALIR 635
Cdd:COG4608 105 ------YAsLNPRMTVGDIIAEPLR--IHGLASK--AERRERVAELlelvGlrpehadrypHEFSGGQRQRIGIARALAL 174
|
170
....*....|....*
gi 239835765 636 KPLLLILDDATSALD 650
Cdd:COG4608 175 NPKLIVCDEPVSALD 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
478-676 |
3.58e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPKVQvlqGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylHTQV 557
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFGR-SFRENIAYGL--NRTPTmEEITAVAVESGAHDFISGFpqgydteVGETGNQLSGGQRQAVALARALI 634
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNIAFGLkqDKLPK-AEIASRVNEMLGLVHMQEF-------AKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 239835765 635 RKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVT 207
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
495-697 |
4.07e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.51 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQY-DHHYLHTQVAAvgqepLLFGRSFRE 573
Cdd:PRK11247 26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEArEDTRLMFQDAR-----LLPWKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 574 NIAYGLN---RTPTMEEITAVAVESGAHDFISGfpqgydtevgetgnqLSGGQRQAVALARALIRKPLLLILDDATSALD 650
Cdd:PRK11247 101 NVGLGLKgqwRDAALQALAAVGLADRANEWPAA---------------LSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 239835765 651 AGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSVG 697
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAvAMADRVLLIEEGKIG 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-700 |
4.79e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.36 E-value: 4.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGQCLVQYDHHYL 553
Cdd:PRK14247 4 IEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQEP-LLFGRSFRENIAYG--LNR----TPTMEEITAVAVESGahdfisgfpQGYD---TEVGETGNQLSGGQ 623
Cdd:PRK14247 81 RRRVQMVFQIPnPIPNLSIFENVALGlkLNRlvksKKELQERVRWALEKA---------QLWDevkDRLDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
232-454 |
7.39e-20 |
|
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: 90.68 E-value: 7.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 232 MHGRVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINL 311
Cdd:cd18574 73 VAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIV 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 312 PLLFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKeaLAYVAEVWT- 390
Cdd:cd18574 153 PVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK--LGLGIGIFQg 230
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 391 ---TSVSGMLLkvGILYLGGQLVIRGAVSSGNLVSFVLYqlqfTQAVQVLLS----LYPSMQKAVGSSEKI 454
Cdd:cd18574 231 lsnLALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLVA----TQTIQRSLAqlsvLFGQYVKGKSAGARV 295
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
483-688 |
7.58e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 89.26 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 483 DVSFAYPNQPkvqvlqgLTFTLH--PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYL---HTQV 557
Cdd:PRK10771 6 DITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEPLLFGR-SFRENIAYGLNrtPTM-------EEITAVAVESGAHDFISGFPqgydtevgetgNQLSGGQRQAVAL 629
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNIGLGLN--PGLklnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 630 ARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLslaEQAHHI 688
Cdd:PRK10771 141 ARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSL---EDAARI 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
473-696 |
1.24e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 473 SNMKGLVEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqclvqydHHY 552
Cdd:PRK15439 6 TTAPPLLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG-------NPC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LH-TQVAA-------VGQEPLLF-GRSFRENIAYGLNRTP-TMEEITAVAVESGAHdfisgfpqgYDTEVgeTGNQLSGG 622
Cdd:PRK15439 76 ARlTPAKAhqlgiylVPQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ---------LDLDS--SAGSLEVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 623 QRQAVALARALIRKPLLLILDDATSALDAG--NQL--RVQRLLYEspkraSRTVLLITQQLSLAEQ-AHHILFLREGSV 696
Cdd:PRK15439 145 DRQIVEILRGLMRDSRILILDEPTASLTPAetERLfsRIRELLAQ-----GVGIVFISHKLPEIRQlADRISVMRDGTI 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
495-700 |
1.38e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVA-ALLQNLyqPTGGQLLLDGQCLVQYDHHYL---HTQVAAVGQEP--LLFG 568
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 R-SFRENIAYGLN-RTPTM------EEITAVAVESG-----AHDFISGFpqgydtevgetgnqlSGGQRQAVALARALIR 635
Cdd:PRK15134 378 RlNVLQIIEEGLRvHQPTLsaaqreQQVIAVMEEVGldpetRHRYPAEF---------------SGGQRQRIAIARALIL 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
478-694 |
1.60e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 1.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHH---YLH 554
Cdd:PRK10908 1 MIRFEHVSKAYLGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQE-PLLFGRSFRENIAY-----GLNRTPTMEEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 628
Cdd:PRK10908 79 RQIGMIFQDhHLLMDRTVYDNVAIpliiaGASGDDIRRRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRlLYESPKRASRTVLLITQQLSL-AEQAHHILFLREG 694
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLiSRRSYRMLTLSDG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
483-700 |
3.37e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 483 DVSFAypnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQ 562
Cdd:PRK09536 10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 E-PLLFGRSFRENIAYGlnRTP------TMEEITAVAVESGAHDfiSGFPQGYDTEVGEtgnqLSGGQRQAVALARALIR 635
Cdd:PRK09536 85 DtSLSFEFDVRQVVEMG--RTPhrsrfdTWTETDRAAVERAMER--TGVAQFADRPVTS----LSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 636 KPLLLILDDATSALDAGNQLR----VQRLLYEspkraSRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRtlelVRRLVDD-----GKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-679 |
3.68e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.78 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG-----GQLLLDGQCLVQ--YDHH 551
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 YLHTQVAAVGQEPLLFGRSFRENIAYGLNRT---PTMEeITAVaVESGAHDfiSGFPQGYDTEVGETGNQLSGGQRQAVA 628
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrPKLE-IDDI-VESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQL 679
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
493-651 |
4.24e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 89.39 E-value: 4.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQ-----CLVQYDhhylhtqVAAVGQEPLLF 567
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrSIQQRD-------ICMVFQSYALF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 GR-SFRENIAYGLNrtptM-----EEITAVAVESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPLLLI 641
Cdd:PRK11432 91 PHmSLGENVGYGLK----MlgvpkEERKQRVKEALELVDLAGFEDRYV-------DQISGGQQQRVALARALILKPKVLL 159
|
170
....*....|
gi 239835765 642 LDDATSALDA 651
Cdd:PRK11432 160 FDEPLSNLDA 169
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
475-700 |
4.28e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLH 554
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQEP--LLFGRSFRENIAYG-LNRTPTMEEITAVAVES----GAHDFISGFPQgydtevgetgnQLSGGQRQAV 627
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRAsRTVLLITQQLSLA-EQAHHILFLREGSVGEQG 700
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQG-KTVIVATHDVDLAaEWADQVIVLKEGRVLAEG 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
502-708 |
4.43e-19 |
|
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: 89.39 E-value: 4.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 502 FTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDH-HYLHT---QVAAVGQEPLLFG-RSFRENIA 576
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgIFLPPhrrRIGYVFQEARLFPhLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 577 YGLNRTPT------MEEITAVAvesGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPLLLILDDATSALD 650
Cdd:COG4148 100 YGRKRAPRaerrisFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 651 AGnqlRVQRLLyesP--KRASRT----VLLITQqlSLAEQAH---HILFLREGSVGEQGTHLQLMKR 708
Cdd:COG4148 166 LA---RKAEIL---PylERLRDEldipILYVSH--SLDEVARladHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
493-701 |
7.13e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.99 E-value: 7.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYLHT---QVAAVGQEPLLFGR 569
Cdd:PRK10851 14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHArdrKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 570 -SFRENIAYGLNRTPTMEEITAVAVESGAHDFI-----SGFPQGYDTevgetgnQLSGGQRQAVALARALIRKPLLLILD 643
Cdd:PRK10851 89 mTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 644 DATSALDAgnQLRVQ-----RLLYESPKRASrtVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK10851 162 EPFGALDA--QVRKElrrwlRQLHEELKFTS--VFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
481-651 |
8.36e-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: 8.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 481 FQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQClvqydhhylhtQVAAV 560
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 561 GQEPLLF-GRSFRENIAYGLNRTPTME---------------------EITAVAVESGAHDFIS---------GFPQG-Y 608
Cdd:COG0488 67 PQEPPLDdDLTVLDTVLDGDAELRALEaeleeleaklaepdedlerlaELQEEFEALGGWEAEAraeeilsglGFPEEdL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 239835765 609 DTEVGEtgnqLSGGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL 185
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
496-708 |
9.63e-19 |
|
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: 85.85 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQY--DHHylhtQVAAVGQEPLLFGR-SFR 572
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKR----DISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 573 ENIAYGL-NRTPTMEEITAVAVEsgahdfISGFpQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:cd03299 90 KNIAYGLkKRKVDKKEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 652 GNQLRVQRLLYESPKRASRTVLLITQQL----SLAEQahhILFLREGSVGEQGTHLQLMKR 708
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFeeawALADK---VAIMLNGKLIQVGKPEEVFKK 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
475-696 |
1.24e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPN-QPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYL 553
Cdd:PRK10535 1 MTALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 htqvAAVGQEPllFGRSFREniaYGLNRTPTME---EITAVAVESG-------AHDFISGFpqGYDTEVGETGNQLSGGQ 623
Cdd:PRK10535 81 ----AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAVYAGLErkqrllrAQELLQRL--GLEDRVEYQPSQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRAsRTVLLITQQLSLAEQAHHILFLREGSV 696
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRG-HTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
177-446 |
1.71e-18 |
|
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: 86.74 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 177 EMAIPFFTGRITDWILQDKTVpsftRNIWLMSILTIASTALEFASDgiYNIT-MGHMHG-RVH----REVFRAVLRQETG 250
Cdd:cd18549 18 DLVFPLIVRYIIDDLLPSKNL----RLILIIGAILLALYILRTLLN--YFVTyWGHVMGaRIEtdmrRDLFEHLQKLSFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 251 FFLKNPAGSITSRVTEDTANVCE--------------SISGTLSLLL---WYLgrALCLLVFMfwgsPYLTLVTLInlpl 313
Cdd:cd18549 92 FFDNNKTGQLMSRITNDLFDISElahhgpedlfisiiTIIGSFIILLtinVPL--TLIVFALL----PLMIIFTIY---- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 314 lfllpkKLGKVHQSLAvKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealAYVAEVWTTS 392
Cdd:cd18549 162 ------FNKKMKKAFR-RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK---AYKAMAYFFS 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 393 VSGM---LLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQK 446
Cdd:cd18549 231 GMNFftnLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
479-701 |
1.81e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.55 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYP-NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHT-- 555
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 -QVAAVGQE-PLLFGRSFRENIAYGL--NRTPTmEEITAVAVE-------SGAHDFisgFPQgydtevgetgnQLSGGQR 624
Cdd:PRK11153 82 rQIGMIFQHfNLLSSRTVFDNVALPLelAGTPK-AEIKARVTEllelvglSDKADR---YPA-----------QLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 625 QAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
479-696 |
2.19e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 83.75 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQP---KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGQclvQYDHHYL 553
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGR---PLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQEPLLFGR-SFRENIAYGLNrtptmeeitavavesgahdfISGfpqgydtevgetgnqLSGGQRQAVALARA 632
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMFAAK--------------------LRG---------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRaSRTVLLITQQLS--LAEQAHHILFLREGSV 696
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLSQGRV 190
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
494-675 |
2.87e-18 |
|
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: 85.09 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylhtQVAAVG-----QEPLLFG 568
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRLFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 R-SFRENIA------------YGLNRTP----TMEEITAVAVES----GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAV 627
Cdd:COG0411 93 ElTVLENVLvaaharlgrgllAALLRLPrarrEEREARERAEELlervGLADRA-------DEPAGN----LSYGQQRRL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLI 675
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLI 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
480-693 |
3.18e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 83.69 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTV-AALLQNLYQP--TGGQLLLDGQCLvqydhHYLHTQ 556
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRRL-----TALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVG---QEPLLFGR-SFRENIAYGLNRTPTMEE----ITAVAVESGAHDFISGFPqgydtevgetgNQLSGGQRQAVA 628
Cdd:COG4136 75 QRRIGilfQDDLLFPHlSVGENLAFALPPTIGRAQrrarVEQALEEAGLAGFADRDP-----------ATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLRE 693
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
494-701 |
3.70e-18 |
|
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: 84.41 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylhtQVAAVG-----QEPLLFG 568
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 R-SFREN--IAYGLNRTPTMEEITAVAVESGAH-------DFIsGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRKPL 638
Cdd:cd03219 89 ElTVLENvmVAAQARTGSGLLLARARREEREAReraeellERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELI-RELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
478-705 |
5.39e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPKV-QVLQGLTFTLHPGTVTALVGPNGSGKSTVA-ALLQNLYQP----TGGQLLLDGQCLVQYDHH 551
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 YLH----TQVAAVGQEPLL-------FGRSFRENIAY--GLNRTPTMEEITAVAVESG---AHDFISGFPqgydtevget 615
Cdd:PRK15134 85 TLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYP---------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 616 gNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREG 694
Cdd:PRK15134 155 -HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|.
gi 239835765 695 SVGEQGTHLQL 705
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
478-701 |
7.62e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.79 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAY-PNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGQCLV-----QYDH 550
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVsstskQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 551 HYLHTQVAAVGQEP--LLFGRSFRENIAYG-LNRTPTMEEITAVAVESGAHdfisgfpQGYDTEVGETGN-QLSGGQRQA 626
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGpQNFGIPKEKAEKIAAEKLEM-------VGLADEFWEKSPfELSGGQMRR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRlLYESPKRASRTVLLITQQL-SLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGT 227
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
178-447 |
1.01e-17 |
|
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: 84.42 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFasdgIYNITMGHMHGRVHREV----FRAVLRQETGFFL 253
Cdd:cd18570 19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSY----IRSYLLLKLSQKLDIRLilgyFKHLLKLPLSFFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 254 KNPAGSITSRVTeDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQ 333
Cdd:cd18570 95 TRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 334 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEA-LAYVAEVWTTSVSGmLLKVGILYLGGQLVIR 412
Cdd:cd18570 174 ESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGkLSNLQSSIKGLISL-IGSLLILWIGSYLVIK 252
|
250 260 270
....*....|....*....|....*....|....*..
gi 239835765 413 GAVSSGNLVSFvlYQLQ--FTQAVQVLLSLYPSMQKA 447
Cdd:cd18570 253 GQLSLGQLIAF--NALLgyFLGPIENLINLQPKIQEA 287
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
494-701 |
1.12e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.69 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPllfGRSF-- 571
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 RENIAYGLN---RTPTmeEITAVAVESGAH----------DFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPL 638
Cdd:PRK15112 103 RQRISQILDfplRLNT--DLEPEQREKQIIetlrqvgllpDHASYYP-----------HMLAPGQKQRLGLARALILRPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:PRK15112 170 VIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
478-701 |
1.51e-17 |
|
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: 86.28 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPK-VQVLQGLTFTLHPGTVTALVGPNGSGKS-TVAALLQNLYQP---TGGQLLLDGQCLVQYDHHY 552
Cdd:COG4172 6 LLSVEDLSVAFGQGGGtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LHT----QVAAVGQEPL-----LF--GRSFRENIA--YGLNRTPTMEEITAVAVESG---AHDFISGFPqgydtevgetg 616
Cdd:COG4172 86 LRRirgnRIAMIFQEPMtslnpLHtiGKQIAEVLRlhRGLSGAAARARALELLERVGipdPERRLDAYP----------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 617 NQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGS 695
Cdd:COG4172 155 HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGE 234
|
....*.
gi 239835765 696 VGEQGT 701
Cdd:COG4172 235 IVEQGP 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
478-676 |
2.10e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqydhhylhtQV 557
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK------------PV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVG--------QEPLLFGRSFRENIAYGLN-RTPTMEEITAVAVESGAHDFISGFPQGYDTevgetgnQLSGGQRQAVA 628
Cdd:PRK11248 66 EGPGaergvvfqNEGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-701 |
2.56e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.40 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCL------VQYDHHYLHTQVAAVGQEPLLFGR 569
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkdiFQIDAIKLRKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 570 -SFRENIAYGLNRTPTME--EITAVAVESGAHdfISGFPQGYDtEVGETGNQLSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEkrEIKKIVEECLRK--VGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 647 SALDAGNQLRVQRLLYESPKRASrTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIA-IVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
479-711 |
5.06e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHyLHTQVA 558
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQ----EP--------LLFGRSFRENIAYGLNRTPTMEEITavAVESGAhdfisgfpqgyDTEVGEtgnqLSGGQRQA 626
Cdd:PRK13537 84 VVPQfdnlDPdftvrenlLVFGRYFGLSAAAARALVPPLLEFA--KLENKA-----------DAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 627 VALARALIRKPLLLILDDATSALDAgnQLRvqRLLYESPKR---ASRTVLLITQQLSLAEQ-AHHILFLREG-SVGEQGT 701
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDP--QAR--HLMWERLRSllaRGKTILLTTHFMEEAERlCDRLCVIEEGrKIAEGAP 222
|
250
....*....|
gi 239835765 702 HLQLMKRGGC 711
Cdd:PRK13537 223 HALIESEIGC 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
497-682 |
6.60e-17 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 80.59 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqydhhylhtQVAAVGQE--------PLLFG 568
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK------------QITEPGPDrmvvfqnySLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 RSFRENIAYGLNRT-PTM--EEITAVAVEsgaHDFISGFPQGYDTEVGetgnQLSGGQRQAVALARALIRKPLLLILDDA 645
Cdd:TIGR01184 69 LTVRENIALAVDRVlPDLskSERRAIVEE---HIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
170 180 190
....*....|....*....|....*....|....*..
gi 239835765 646 TSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA 682
Cdd:TIGR01184 142 FGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEA 178
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
477-698 |
6.81e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 6.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 477 GLVEFQDVSFAYPN-QPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQ-----------NLYQPTGGQLLLdgqc 544
Cdd:COG4178 361 GALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKST---LLRaiaglwpygsgRIARPAGARVLF---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 545 lvqydhhylhtqvaaVGQEPLLFGRSFRENIAY-GLNRTPTMEEITAVAVESGAHDFISGFpqgyDTEVgETGNQLSGGQ 623
Cdd:COG4178 431 ---------------LPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERL----DEEA-DWDQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRAsrTVLLITQQLSLAEQAHHILFLREGSVGE 698
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT--TVISVGHRSTLAAFHDRVLELTGDGSWQ 563
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
478-701 |
8.37e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDH-HYLHTQ 556
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEP--LLFGRSFRENIAYG-----LNRTPTMEEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAVAL 629
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 630 ARALIRKPLLLILDDATSALD--AGNQL--RVQRLlyespKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDpdSGIAVleRIKKL-----HEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
488-679 |
9.03e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 488 YPNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLL 566
Cdd:COG1101 12 NPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 567 fGRSFR----EN--IAY------GLNRTPTMEEITAVavesgaHDFISGFPQGY----DTEVGetgnQLSGGQRQAVALA 630
Cdd:COG1101 92 -GTAPSmtieENlaLAYrrgkrrGLRRGLTKKRRELF------RELLATLGLGLenrlDTKVG----LLSGGQRQALSLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 239835765 631 RALIRKPLLLILDDATSALDagnqlrvqrllyesPKRASRtVLLITQQL 679
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALD--------------PKTAAL-VLELTEKI 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
493-700 |
9.32e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 9.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEPLLFGR-SF 571
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 RENIAYGlnRTPTM--------EEITAVAVESGAHDFISGFPQGYDTevgetgnqLSGGQRQAVALARALIRKPLLLILD 643
Cdd:PRK10253 99 QELVARG--RYPHQplftrwrkEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 644 DATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSVGEQG 700
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIVAQG 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
479-701 |
9.60e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.22 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAY-PNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGQCLV-----QYDHH 551
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVItagkkNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 YLHTQVAAVGQ--EPLLFGRSFRENIAYG-LNRTPTMEEITAVAVESGAhdfISGFPQGYDTEvgeTGNQLSGGQRQAVA 628
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGpMNFGVSEEDAKQKAREMIE---LVGLPEELLAR---SPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS-LAEQAHHILFLREGSVGEQGT 701
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGT 229
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
492-695 |
1.12e-16 |
|
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: 79.68 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 492 PKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQ----VAAVGQEPLLF 567
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 GRSFRENIAYG--LNRTPTMEEITAVAVESGahdfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDA 645
Cdd:cd03290 92 NATVEENITFGspFNKQRYKAVTDACSLQPD----IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 239835765 646 TSALDA--GNQLrVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGS 695
Cdd:cd03290 168 FSALDIhlSDHL-MQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
479-660 |
1.16e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.20 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQcLVqydhhylhTQV- 557
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGR-VV--------NELe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 ------AAVGQEPLLFGR-SFRENIAYGL-NRTPTMEEI------TAVAVESGAhdFISGFPQgydtevgetgnQLSGGQ 623
Cdd:PRK11650 73 padrdiAMVFQNYALYPHmSVRENMAYGLkIRGMPKAEIeervaeAARILELEP--LLDRKPR-----------ELSGGQ 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAgnQLRVQ-RL 660
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDA--KLRVQmRL 175
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
493-723 |
1.17e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqclvqydhhylhtqvaavgqEPLlfGRSFR 572
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG--------------------EPL--DPEDR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 573 ENIAY-----GLNRTPTMEE----------ITAVAVESGAHDFISGFpqgydtEVGETGN----QLSGGQRQAVALARAL 633
Cdd:COG4152 71 RRIGYlpeerGLYPKMKVGEqlvylarlkgLSKAEAKRRADEWLERL------GLGDRANkkveELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 634 IRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQLMKRGGCY 712
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRN 223
|
250
....*....|.
gi 239835765 713 RAMVEALAAPA 723
Cdd:COG4152 224 TLRLEADGDAG 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
235-696 |
1.25e-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: 84.58 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 235 RVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTL----SLLLWYLGrALCLLVFMfwgSPYLTLVTLIN 310
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLfdfiQLTLIVLG-AIFVVSVL---QPYIFIAAIPV 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 311 LPLLFLLPKKLGKVHQSLavKVQESLAKSTQVA--LEALSAMPTVRSFAneegeaqkfRQKLEEM---KTLNKKEALAYV 385
Cdd:TIGR01271 1035 AVIFIMLRAYFLRTSQQL--KQLESEARSPIFShlITSLKGLWTIRAFG---------RQSYFETlfhKALNLHTANWFL 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 386 aevWTTSVSGMLLKVGILYLggqlVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSS----------EKIF 455
Cdd:TIGR01271 1104 ---YLSTLRWFQMRIDIIFV----FFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSidvdglmrsvSRVF 1176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 456 EYLDRTPCSP-LSGSLAPSNMKG--LVEFQDVSFAYPNQPKVQV--------------LQGLTFTLHPGTVTALVGPNGS 518
Cdd:TIGR01271 1177 KFIDLPQEEPrPSGGGGKYQLSTvlVIENPHAQKCWPSGGQMDVqgltakyteagravLQDLSFSVEGGQRVGLLGRTGS 1256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 519 GKSTV-AALLQNLyqPTGGQLLLDGqclVQYDHHYLHTQVAAVG---QEPLLFGRSFRENIayglnrTP----TMEEITA 590
Cdd:TIGR01271 1257 GKSTLlSALLRLL--STEGEIQIDG---VSWNSVTLQTWRKAFGvipQKVFIFSGTFRKNL------DPyeqwSDEEIWK 1325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 591 VAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpkRASR 670
Cdd:TIGR01271 1326 VAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS--FSNC 1403
|
490 500
....*....|....*....|....*.
gi 239835765 671 TVLLITQQLSLAEQAHHILFLREGSV 696
Cdd:TIGR01271 1404 TVILSEHRVEALLECQQFLVIEGSSV 1429
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
475-701 |
1.31e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYP-------------------NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQ---NLYQ 532
Cdd:COG1134 1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 533 PTGGQLLLDGqclvqydhhylhtQVAAvgqePLLFGRSF------RENI-----AYGLNRtptmEEITAVAvesgahDFI 601
Cdd:COG1134 78 PTSGRVEVNG-------------RVSA----LLELGAGFhpeltgRENIylngrLLGLSR----KEIDEKF------DEI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 602 SGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQ 677
Cdd:COG1134 131 VEF-----AELGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSH 204
|
250 260
....*....|....*....|....*
gi 239835765 678 QLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:COG1134 205 SMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
475-688 |
2.17e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 79.43 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLYQ--------PTGGQLLLDGQCLV 546
Cdd:PRK14239 2 TEPILQVSDLSVYYN---KKKALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 547 --QYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLNRTPTME-EITAVAVES---GAHDFISGFPQGYDTEVGetgnqLS 620
Cdd:PRK14239 76 spRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDkQVLDEAVEKslkGASIWDEVKDRLHDSALG-----LS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYEspKRASRTVLLITQQLslaEQAHHI 688
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG--LKDDYTMLLVTRSM---QQASRI 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
497-698 |
2.41e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 78.57 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQyDHHYLHTQVAAVGQEPLLFGR-SFRENI 575
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 A-----YGLNRTPTMEEITAVAvesgahDFIsgfpqgydtEVGETGNQL----SGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:cd03265 95 YiharlYGVPGAERRERIDELL------DFV---------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 647 SALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-------AHHILFLREGSVGE 698
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlcdrvaiIDHGRIIAEGTPEE 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
496-683 |
3.77e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.53 E-value: 3.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 574
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTlSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 575 IAY--GLNRTPTMEEITAVAVESGAHDFISgfpqgydtevgetgNQLSGGQRQAVALARALIRKPLLLILDDATSALDAG 652
Cdd:cd03231 94 LRFwhADHSDEQVEEALARVGLNGFEDRPV--------------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180 190
....*....|....*....|....*....|.
gi 239835765 653 NQLRVQRLLYESPKRASRTVLLITQQLSLAE 683
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
479-696 |
3.79e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.08 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPK-VQVLQGLTFTLHPGTVTALVGPNGSGKST----VAALLQNLYQpTGGQLLLDGQclvQYDHHYL 553
Cdd:cd03234 4 LPWWDVGLKAKNWNKyARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQ---PRKPDQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQ-EPLLFGRSFRENIAYGLN-RTP--TMEEITAVAVEsgahdfISGFPQGYDTEVGETG-NQLSGGQRQAVA 628
Cdd:cd03234 80 QKCVAYVRQdDILLPGLTVRETLTYTAIlRLPrkSSDAIRKKRVE------DVLLRDLALTRIGGNLvKGISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRaSRTVLL-ITQQLS-LAEQAHHILFLREGSV 696
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILtIHQPRSdLFRLFDRILLLSSGEI 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
475-710 |
4.19e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQPKVQ---VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHH 551
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 Y-LHTQVAAVGQEP--LLFGRSFRENIAYG---LNRTPtmEEITAVAVES----GAHDFISGFPqgydtevgetgNQLSG 621
Cdd:PRK13633 81 WdIRNKAGMVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRERVDESlkkvGMYEYRRHAP-----------HLLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 622 GQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
250
....*....|....*
gi 239835765 702 ------HLQLMKRGG 710
Cdd:PRK13633 228 pkeifkEVEMMKKIG 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
501-701 |
5.36e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 501 TFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLH----TQVAAVGQE-PLLFGRSFRENI 575
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 AYGLN---------RTPTMEEITAVAVESGAHdfisGFPqgydtevgetgNQLSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:PRK10070 128 AFGMElaginaeerREKALDALRQVGLENYAH----SYP-----------DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 647 SALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGT 701
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGT 248
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
495-700 |
6.71e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 78.09 E-value: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL-----------DGQCLVqYDHHYLH---TQVAAV 560
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkDGQLKV-ADKNQLRllrTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 561 GQEPLLFGR-SFRENI------AYGLNRTPTMEEitavAVESGAHDFISGFPQGydtevgETGNQLSGGQRQAVALARAL 633
Cdd:PRK10619 98 FQHFNLWSHmTVLENVmeapiqVLGLSKQEARER----AVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 634 IRKPLLLILDDATSALD---AGNQLRVQRLLYESPKrasrTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGK----TMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
483-710 |
7.32e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 7.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 483 DVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLvQYDHH---YLHTQVAA 559
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQEP--LLFGRSFRENIAYGLNRTPTMEEITAVAVESgAHDFISGfpQGYDTEVGETgnqLSGGQRQAVALARALIRKP 637
Cdd:PRK13638 82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDE-ALTLVDA--QHFRHQPIQC---LSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 638 LLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSV------GEQGTHLQLMKRGG 710
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIlthgapGEVFACTEAMEQAG 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
478-701 |
9.99e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.35 E-value: 9.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQClVQYDHH---YLH 554
Cdd:PRK13636 5 ILKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-IDYSRKglmKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQEP--LLFGRSFRENIAYG-LNRTPTMEEITAVAVESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALAR 631
Cdd:PRK13636 82 ESVGMVFQDPdnQLFSASVYQDVSFGaVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSL-AEQAHHILFLREGSVGEQGT 701
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGN 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
499-703 |
1.11e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 499 GLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylhtQVAAVG-----QEPLLFG----- 568
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIARMGvvrtfQHVRLFRemtvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 --------RSFRENIAYGLNRTPTMEEITAVAVESGAH--DFIsGFpqgydTEVG--ETGNqLSGGQRQAVALARALIRK 636
Cdd:PRK11300 99 enllvaqhQQLKTGLFSGLLKTPAFRRAESEALDRAATwlERV-GL-----LEHAnrQAGN-LAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 637 PLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILflregsVGEQGTHL 703
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIY------VVNQGTPL 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
464-711 |
1.58e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 78.72 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 464 SPLSGSLAPSnmkgLVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQ 543
Cdd:PRK13536 31 ASIPGSMSTV----AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 544 --------------CLVQYDHHYLHTQVaavgQEPLL-FGRSFRENiayglnrTPTMEEITAVAVEsgahdfISGFPQGY 608
Cdd:PRK13536 104 pvpararlararigVVPQFDNLDLEFTV----RENLLvFGRYFGMS-------TREIEAVIPSLLE------FARLESKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 609 DTEVGEtgnqLSGGQRQAVALARALIRKPLLLILDDATSALDA-GNQLRVQRLlyESPKRASRTVLLITQQLSLAEQAHH 687
Cdd:PRK13536 167 DARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPhARHLIWERL--RSLLARGKTILLTTHFMEEAERLCD 240
|
250 260
....*....|....*....|....*.
gi 239835765 688 ILFLREG--SVGEQGTHLQLMKRGGC 711
Cdd:PRK13536 241 RLCVLEAgrKIAEGRPHALIDEHIGC 266
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
479-689 |
2.01e-15 |
|
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: 74.50 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgqclvqydHHYLHTQVA 558
Cdd:cd03223 1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGRSFRENIAYglnrtPTMEEitavavesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPL 638
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLyespKRASRTVLLITQQLSLAEQAHHIL 689
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVL 158
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
201-454 |
2.04e-15 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 77.70 E-value: 2.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 201 TRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLS 280
Cdd:cd18558 59 TLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 281 LLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEE 360
Cdd:cd18558 139 VIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 361 GEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSL 440
Cdd:cd18558 219 KEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPS 298
|
250
....*....|....
gi 239835765 441 YPSMQKAVGSSEKI 454
Cdd:cd18558 299 IEAFANARGAAYHI 312
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
479-709 |
3.74e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 76.36 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAY----PNQpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQY--DHHY 552
Cdd:PRK13646 3 IRFDNVSYTYqkgtPYE--HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LHT--QVAAVGQ--EPLLFGRSFRENIAYG-LNRTPTMEEitavaVESGAHDFIS--GFPQGYdteVGETGNQLSGGQRQ 625
Cdd:PRK13646 81 RPVrkRIGMVFQfpESQLFEDTVEREIIFGpKNFKMNLDE-----VKNYAHRLLMdlGFSRDV---MSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 626 AVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS-LAEQAHHILFLREGSVGEQGTHLQ 704
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTSPKE 232
|
....*
gi 239835765 705 LMKRG 709
Cdd:PRK13646 233 LFKDK 237
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
497-706 |
4.23e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.65 E-value: 4.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGQCLVQYDHH-------YLHTQVAAVGQEPLLfgr 569
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFAMPVF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 570 sfrENIAYGLNRTPTMEEITAVaVESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR-------KPLLLIL 642
Cdd:COG4138 88 ---QYLALHQPAGASSEAVEQL-LAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 643 DDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLA-EQAHHILFLREGSVGEQGTHLQLM 706
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTlRHADRVWLLKQGKLVASGETAEVM 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
496-661 |
6.03e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDH----HYLHTQVAAvgqEPLLfgrSF 571
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLGHRNAM---KPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 RENIA-----YGLNRTPTMEEITAVAVESGAHdfisgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:PRK13539 91 AENLEfwaafLGGEELDIAAALEAVGLAPLAH-----LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170
....*....|....*
gi 239835765 647 SALDAGNQLRVQRLL 661
Cdd:PRK13539 156 AALDAAAVALFAELI 170
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
479-701 |
6.51e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 75.55 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPKVQ--VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCL----VQYDHHY 552
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LHTQVAAVGQ--EPLLFGRSFRENIAYG-LNRTPTMEEITAVAVESGAHDFISgfpqgyDTEVGETGNQLSGGQRQAVAL 629
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 630 ARALIRKPLLLILDDATSALDAGNQLRVQRlLYESPKRASRTVLLITQQL-SLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-454 |
7.95e-15 |
|
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: 75.65 E-value: 7.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMG-HMHGRVHREVFRAVLRQETGFFLKNPA 257
Cdd:cd18778 17 VPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEqKVVADLRSDLYDKLQRLSLRYFDDRQT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 258 GSITSRVTEDTANV----CESISGTLSLLLWYLGralcLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQ 333
Cdd:cd18778 97 GDLMSRVINDVANVerliADGIPQGITNVLTLVG----VAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 334 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealayVAEVWTTSVSGM-----LLKVGILYLGGQ 408
Cdd:cd18778 173 EALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLR-----AMKLWAIFHPLMefltsLGTVLVLGFGGR 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 239835765 409 LVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18778 248 LVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
479-676 |
9.39e-15 |
|
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: 71.71 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqclvqydhhylhtqva 558
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 avgqepllfgrsfRENIAYglnrtptmeeitavavesgahdfisgFPqgydtevgetgnQLSGGQRQAVALARALIRKPL 638
Cdd:cd03221 62 -------------TVKIGY--------------------------FE------------QLSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*...
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESPkrasRTVLLIT 676
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVS 124
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
475-681 |
9.52e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLH 554
Cdd:PRK09544 1 MTSLVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAvgqePLLFGRSFRenIAYGLNRT---PTMEEITAvavesgAHdfISGFPQgydtevgetgNQLSGGQRQAVALAR 631
Cdd:PRK09544 78 LDTTL----PLTVNRFLR--LRPGTKKEdilPALKRVQA------GH--LIDAPM----------QKLSGGETQRVLLAR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSL 681
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
493-675 |
9.61e-15 |
|
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: 74.01 E-value: 9.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLldgqclvqYDHHYLHTQVAAVGQEPLLFGRsfR 572
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDGGWVDLAQASPREILALR--R 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 573 ENIAY------GLNRTPTMEEITAVAVESG-----AHDfisgfpqgydtEVGETGNQL--------------SGGQRQAV 627
Cdd:COG4778 93 RTIGYvsqflrVIPRVSALDVVAEPLLERGvdreeARA-----------RARELLARLnlperlwdlppatfSGGEQQRV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLI 675
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGI 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
475-651 |
1.30e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHY-- 552
Cdd:PRK11288 1 SSPYLSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ-----EMRFas 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 ----LHTQVAAVGQE----PLLfgrSFRENIAYGlnRTPT------MEEITAVAVESGAHDFISGFPqgyDTEVGEtgnq 618
Cdd:PRK11288 73 ttaaLAAGVAIIYQElhlvPEM---TVAENLYLG--QLPHkggivnRRLLNYEAREQLEHLGVDIDP---DTPLKY---- 140
|
170 180 190
....*....|....*....|....*....|...
gi 239835765 619 LSGGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:PRK11288 141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
474-649 |
1.31e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 474 NMKGLVEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqyDHHYL 553
Cdd:COG3845 1 MMPPALELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK-----PVRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAA------VGQEPLLFGR-SFRENIAYGLNRTPTM--------EEITAVAVEsgahdfiSGFPQGYDTEVGetgnQ 618
Cdd:COG3845 73 SPRDAIalgigmVHQHFMLVPNlTVAENIVLGLEPTKGGrldrkaarARIRELSER-------YGLDVDPDAKVE----D 141
|
170 180 190
....*....|....*....|....*....|.
gi 239835765 619 LSGGQRQAVALARALIRKPLLLILDDATSAL 649
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
493-650 |
1.43e-14 |
|
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: 73.73 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylhtQVAAVG-----QEPLLF 567
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH----KRARLGigylpQEASIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 GR-SFRENIAYGLNRTPTMEEITAVAVESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:cd03218 88 RKlTVEENILAVLEIRGLSKKEREEKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
....
gi 239835765 647 SALD 650
Cdd:cd03218 162 AGVD 165
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
486-700 |
1.49e-14 |
|
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: 73.34 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 486 FAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqclvqydhhylhtQVAA-----V 560
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSllglgG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 561 GQEPLLFGrsfRENI-----AYGLNRtptmEEITAVAvesgahDFISGFpqgydTEVGETGNQ----LSGGQRQAVALAR 631
Cdd:cd03220 94 GFNPELTG---RENIylngrLLGLSR----KEIDEKI------DEIIEF-----SELGDFIDLpvktYSSGMKARLAFAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRL-RELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
496-696 |
1.51e-14 |
|
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: 74.51 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTV-AALLQNLYqpTGGQLLLDGqclVQYDHHYLHTQVAAVG---QEPLLFGRSF 571
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDG---VSWNSVPLQKWRKAFGvipQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 RENI-AYGLNRTptmEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALD 650
Cdd:cd03289 94 RKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 239835765 651 AGNQLRVQRLLYESpkRASRTVLLITQQLSLAEQAHHILFLREGSV 696
Cdd:cd03289 171 PITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
257-545 |
3.01e-14 |
|
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: 75.99 E-value: 3.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 257 AGSITSRVTEDTANVCESiSGTLSLLLWYLGRALCLLVFMFWGSP---YLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQ 333
Cdd:COG4615 104 AARLLAALTEDVRTISQA-FVRLPELLQSVALVLGCLAYLAWLSPplfLLTLVLLGLGVAGYRLLVRRARRHLRRAREAE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 334 ESLAKSTQVALE-----ALSAmPTVRSFANEEgeaqkFRQKLEEMKTLNKKEALAYV-AEVWTTSVsgMLLKVG-ILYLG 406
Cdd:COG4615 183 DRLFKHFRALLEgfkelKLNR-RRRRAFFDED-----LQPTAERYRDLRIRADTIFAlANNWGNLL--FFALIGlILFLL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 407 GQLvirGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKIfEYLDRTPCSPLSGSLAPSNMKGLVEFQ---- 482
Cdd:COG4615 255 PAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKI-EELELALAAAEPAAADAAAPPAPADFQtlel 330
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 483 -DVSFAYPNQ--PKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCL 545
Cdd:COG4615 331 rGVTYRYPGEdgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
483-681 |
3.85e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 71.90 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 483 DVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQClVQYDHHYLHTQVAAVGQ 562
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-IKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 E----PLLfgrSFRENIAYGLNRTPTMEEITAVAVESGAHDFISgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPL 638
Cdd:PRK13540 82 RsginPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSL 681
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPL 190
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
485-676 |
4.29e-14 |
|
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: 72.37 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 485 SFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqcLVQYDHH--YLHTQVAAVGQ 562
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVPWKRRkkFLRRIGVVFGQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 EPLLF-----GRSFRENIA-YG---------LNRTPTMEEITAVavesgahdfisgfpqgYDTEVgetgNQLSGGQRQAV 627
Cdd:cd03267 103 KTQLWwdlpvIDSFYLLAAiYDlpparfkkrLDELSELLDLEEL----------------LDTPV----RQLSLGQRMRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:cd03267 163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTS 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
495-702 |
6.10e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.97 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvQYDHHY---------LHTQVAAVGQE-- 563
Cdd:PRK11124 16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKtpsdkaireLRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 564 --PLLfgrSFRENI------AYGLNRTPTMEEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIR 635
Cdd:PRK11124 93 lwPHL---TVQQNLieapcrVLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTH 702
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
496-705 |
7.01e-14 |
|
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: 72.58 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqydhhylhtqVAAVGQEPLLFGRSFRENI 575
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 AYGLnrtpTMEE------ITAVAVESGahdfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSAL 649
Cdd:cd03291 119 IFGV----SYDEyryksvVKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 650 DagnqLRVQRLLYES---PKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQL 705
Cdd:cd03291 191 D----VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
496-705 |
8.13e-14 |
|
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: 75.72 E-value: 8.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvqydhhylhtqVAAVGQEPLLFGRSFRENI 575
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 AYGLnrtpTMEEI--TAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDagn 653
Cdd:TIGR01271 508 IFGL----SYDEYryTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD--- 580
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 654 qLRVQRLLYES---PKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGTHLQL 705
Cdd:TIGR01271 581 -VVTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
493-699 |
9.85e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 9.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylhtQVAAVGQEPLLF-GRSF 571
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE----ARAKLRAKHVGFvFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 --------RENIAY-----GLNRTPTMEEITAVAVESGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPL 638
Cdd:PRK10584 98 mliptlnaLENVELpallrGESSRQSRNGAKALLEQLGLGKRLDHLPA-----------QLSGGEQQRVALARAFNGRPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 639 LLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQ 699
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
495-721 |
1.19e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.25 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGQCLVQYDHHylhtQVAAVG-----QEPLLF 567
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPD----ERARAGiflafQYPVEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 -GRSFRE--NIAYGLNRTptmEEITAVAVESGAHDFIS--GFPQGY-DTEVGETgnqLSGGQRQAVALARALIRKPLLLI 641
Cdd:COG0396 90 pGVSVSNflRTALNARRG---EELSAREFLKLLKEKMKelGLDEDFlDRYVNEG---FSGGEKKRNEILQMLLLEPKLAI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 642 LDDATSALDAGNqLRVQRLLYESPKRASRTVLLITQQLSLAE--QAHHILFLREGSVGEQGTH---LQLMKRGgcYRAMV 716
Cdd:COG0396 164 LDETDSGLDIDA-LRIVAEGVNKLRSPDRGILIITHYQRILDyiKPDFVHVLVDGRIVKSGGKelaLELEEEG--YDWLK 240
|
....*
gi 239835765 717 EALAA 721
Cdd:COG0396 241 EEAAA 245
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
496-683 |
1.35e-13 |
|
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: 70.08 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 574
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 575 IayglnrtptmeeitavavesgahDFISGFPQGYD-------TEVGETG------NQLSGGQRQAVALARALIRKPLLLI 641
Cdd:TIGR01189 94 L-----------------------HFWAAIHGGAQrtiedalAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWI 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 239835765 642 LDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAE 683
Cdd:TIGR01189 151 LDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVE 192
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
478-650 |
1.53e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGQCLVQ-Y---DHHYL 553
Cdd:COG0488 315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgYfdqHQEEL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTqvaavgqepllfGRSFRENIAYGLnrtPTMEEITAVAVesgAHDFisGFPqGYD--TEVGEtgnqLSGGQRQAVALAR 631
Cdd:COG0488 391 DP------------DKTVLDELRDGA---PGGTEQEVRGY---LGRF--LFS-GDDafKPVGV----LSGGEKARLALAK 445
|
170
....*....|....*....
gi 239835765 632 ALIRKPLLLILDDATSALD 650
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLD 464
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
479-634 |
2.09e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.50 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVA 558
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQEPLLFGR-SFRENIAYGlnRTP------TMEEITAVA-------VESGAHDFIsgfpqgydtevgetgNQLSGGQR 624
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFG--RFPyskgrlTAEDREIIDeaiayldLEDLADRYL---------------DELSGGQR 141
|
170
....*....|
gi 239835765 625 QavalaRALI 634
Cdd:COG4604 142 Q-----RAFI 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
498-691 |
2.54e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 498 QGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYlHTQVAAVGQ----EPLLfgrSFRE 573
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHqpgiKTEL---TALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 574 NIAY--GLNRTPTMEEITAVAVESGahdfISGFPqgyDTEVGetgnQLSGGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:PRK13538 94 NLRFyqRLHGPGDDEALWEALAQVG----LAGFE---DVPVR----QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 239835765 652 GNQLRVQRLLYEspkRASR--TVLLIT-QQLSLAEQAHHILFL 691
Cdd:PRK13538 163 QGVARLEALLAQ---HAEQggMVILTThQDLPVASDKVRKLRL 202
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
479-694 |
2.86e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.01 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAY-PNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHY---- 552
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LHTQVAAVGQ--EPLLFGRSFRENIAYG-LNRTPTMEEITAVAVEsgahdFISGFpqGYDTEVGETGN-QLSGGQRQAVA 628
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpKNFGFSEDEAKEKALK-----WLKKV--GLSEDLISKSPfELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQL-SLAEQAHHILFLREG 694
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
479-707 |
2.96e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.85 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAY-PNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLV--QYDHHYLH 554
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVGQEP--LLFGRSFRENIAYGL-NRTPTMEEITAVAVESGAhdfISGFPqgYDTEVGETGNQLSGGQRQAVALAR 631
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPiNLGLSEEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 632 ALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS-LAEQAHHILFLREGSVGEQGTHLQLMK 707
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
496-696 |
3.16e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 68.61 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVqydhhylhtqvaavgqepllfGRSFRENI 575
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT---------------------RRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 AYGlnrtptmeeITAVAVESGAHDFISGFPqgydteVGE---TGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAG 652
Cdd:cd03215 74 RAG---------IAYVPEDRKREGLVLDLS------VAEniaLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 239835765 653 NQLRVQRLLYESpKRASRTVLLITQQLS-LAEQAHHILFLREGSV 696
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
491-708 |
3.32e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 491 QPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHY--LHTQ------------ 556
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVieLSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLL-------FGRSFRENIAY--GLNRTPTMEE----ITAVAVESgAHDFISGFPqgydtevgetgNQLSGGQ 623
Cdd:PRK10261 106 MAMIFQEPMTslnpvftVGEQIAESIRLhqGASREEAMVEakrmLDQVRIPE-AQTILSRYP-----------HQLSGGM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS-LAEQAHHILFLREGSVGEQGTH 702
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGSV 253
|
....*.
gi 239835765 703 LQLMKR 708
Cdd:PRK10261 254 EQIFHA 259
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
176-440 |
4.17e-13 |
|
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: 70.51 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 176 GEMAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASdGIYNITMGHMHGR-VHREVFRAVLRQETGFFLK 254
Cdd:cd18548 14 LELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILA-GYFAAKASQGFGRdLRKDLFEKIQSFSFAEIDK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 255 NPAGSITSRVTEDTANVCESISGTLSLLLwylgRALCLLVF----MFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAV 330
Cdd:cd18548 93 FGTSSLITRLTNDVTQVQNFVMMLLRMLV----RAPIMLIGaiimAFRINPKLALILLVAIPILALVVFLIMKKAIPLFK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 331 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKK-EALAYVAEVWTTSVSGMLLkVGILYLGGQL 409
Cdd:cd18548 169 KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKaGRLMALLNPLMMLIMNLAI-VAILWFGGHL 247
|
250 260 270
....*....|....*....|....*....|.
gi 239835765 410 VIRGAVSSGNLVSFVLYqlqftqAVQVLLSL 440
Cdd:cd18548 248 INAGSLQVGDLVAFINY------LMQILMSL 272
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
179-454 |
4.18e-13 |
|
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: 70.61 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPAG 258
Cdd:cd18588 20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 259 SITSRVTEdTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAK 338
Cdd:cd18588 100 DTVARVRE-LESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 339 STQVALEALSAMPTVRSFANEegeaQKFRQKLEEMKTlnkkealAYVAEVWTTSVSGM-----------LLKVGILYLGG 407
Cdd:cd18588 179 NQSFLVETVTGIETVKSLAVE----PQFQRRWEELLA-------RYVKASFKTANLSNlasqivqliqkLTTLAILWFGA 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 239835765 408 QLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18588 248 YLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
462-707 |
5.05e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 72.89 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 462 PCSPLSGSLAPSNMKGLVEFQDVSFAYPN-QPKVqVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLYqptggqlll 540
Cdd:PTZ00243 641 GGTGGGHEATPTSERSAKTPKMKTDDFFElEPKV-LLRDVSVSVPRGKLTVVLGATGSGKST---LLQSLL--------- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 541 dGQCLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYgLNRTPTMEEITAVAVESGAHDfISGFPQGYDTEVGETGNQLS 620
Cdd:PTZ00243 708 -SQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILF-FDEEDAARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLS 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQG 700
Cdd:PTZ00243 785 GGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLG-ALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
....*..
gi 239835765 701 THLQLMK 707
Cdd:PTZ00243 864 SSADFMR 870
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
470-679 |
9.18e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.14 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 470 LAPSNMKGLVEFQD--VSFAYPNQpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP---TGGQLLLDGQC 544
Cdd:PRK09473 4 LAQQQADALLDVKDlrVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 545 LVQYDHHYLHT----QVAAVGQEPLL-------FGRSFRENIAY--GLNRTPTMEE----ITAVAVESgAHDFISGFPqg 607
Cdd:PRK09473 83 ILNLPEKELNKlraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEEsvrmLDAVKMPE-ARKRMKMYP-- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239835765 608 ydtevgetgNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQL 679
Cdd:PRK09473 160 ---------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
471-698 |
9.83e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 9.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 471 APSNMKGLvEFQDVSFAYPNQpKVQVlQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDH 550
Cdd:PRK10522 316 AFPDWQTL-ELRNVTFAYQDN-GFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 551 HYLHTQVAAVGQEPLLFGRSFreniayglnrTPTMEEITAVAVESGAHdfISGFPQGYDTEVGETGN-QLSGGQRQAVAL 629
Cdd:PRK10522 393 EDYRKLFSAVFTDFHLFDQLL----------GPEGKPANPALVEKWLE--RLKMAHKLELEDGRISNlKLSKGQKKRLAL 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 630 ARALIRKPLLLILDDAtsALDAGNQLRvqRLLYES--P--KRASRTVLLITQQLSLAEQAHHILFLREGSVGE 698
Cdd:PRK10522 461 LLALAEERDILLLDEW--AADQDPHFR--REFYQVllPllQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
493-700 |
1.40e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.17 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNL--YQPTGGQLLLDGQCLVQYDHHylhtQVAAVG-----QEPl 565
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE----ERARLGiflafQYP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 566 lfgrsfreniayglnrtptmEEITAVAVEsgahDFISgfpqgydtEVGETgnqLSGGQRQAVALARALIRKPLLLILDDA 645
Cdd:cd03217 87 --------------------PEIPGVKNA----DFLR--------YVNEG---FSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 646 TSALDAGNqLRVQRLLYESPKRASRTVLLITQQLSLAE--QAHHILFLREGSVGEQG 700
Cdd:cd03217 132 DSGLDIDA-LRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
492-707 |
1.68e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 492 PKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNlYQPTG----GQLLLDGQ-----------CLVQYDHHYLHTQ 556
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMpidakemraisAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAavgQEPLLFGRSFR--ENIAYGLNRTPTMEEITAVAVESGAHdfisgfpqgydTEVGETGNQ--LSGGQRQAVALARA 632
Cdd:TIGR00955 115 TV---REHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCAN-----------TRIGVPGRVkgLSGGERKRLAFASE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS-LAEQAHHILFLREGSVGEQGTHLQLMK 707
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
475-649 |
2.13e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYD-HHYL 553
Cdd:PRK11614 2 EKVMLSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 HTQVAAVGQEPLLFGR-SFRENIAYG---LNRTPTMEEITAVavesgaHDFisgFPQGYDTEVGETGNqLSGGQRQAVAL 629
Cdd:PRK11614 79 REAVAIVPEGRRVFSRmTVEENLAMGgffAERDQFQERIKWV------YEL---FPRLHERRIQRAGT-MSGGEQQMLAI 148
|
170 180
....*....|....*....|
gi 239835765 630 ARALIRKPLLLILDDATSAL 649
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGL 168
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
177-454 |
2.37e-12 |
|
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: 68.28 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 177 EMAIPFFTGRITDWILQDKTvpsfTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVH----REVFRAVLRQETGFF 252
Cdd:cd18543 15 GLAIPLLTRRAIDGPIAHGD----RSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEhdlrTDLFAHLQRLDGAFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 253 LKNPAGSITSRVTEDTAnvceSISGTLSLLLWYLGRALCL---LVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLA 329
Cdd:cd18543 91 DRWQSGQLLSRATSDLS----LVQRFLAFGPFLLGNLLTLvvgLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 330 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNkkealayVAEVWTTSVSGMLLK-------VGI 402
Cdd:cd18543 167 RRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATR-------LRAARLRARFWPLLEalpelglAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 239835765 403 LYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
478-682 |
2.87e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.50 E-value: 2.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPKVQvlqGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQ--PTG---GQLLLDGQCLvqYDHHY 552
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNL--YAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 ----LHTQVAAVGQEPLLFGRSFRENIAYG---LNRTPTMEEITAVAVESGAHdfisgfpqgYDtEVG----ETGNQLSG 621
Cdd:PRK14243 85 dpveVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAAL---------WD-EVKdklkQSGLSLSG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 622 GQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRasRTVLLITQQLSLA 682
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQA 213
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
403-695 |
3.47e-12 |
|
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: 69.78 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 403 LYLGGQLVIRGAVSSGNLVSFV--LYQLQ-FTQAVQVLLSLYPSMQK------AVGSSEKIFEYLDRTPCSPLSGSLAps 473
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLMLAGrdMTRLAgFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIVE-- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 474 NMKGLVEFQDVSFAYPNQPKVqvLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYdhhyl 553
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPNGDVL--IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY----- 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 554 htqvaaVGQEPLLFGRSFRENIAYG------LNRTPTMEEITAVAVESGAHDFISGfPQGYDTeVGETGNQLSGGQRQAV 627
Cdd:TIGR00954 520 ------VPQRPYMTLGTLRDQIIYPdssedmKRRGLSDKDLEQILDNVQLTHILER-EGGWSA-VQDWMDVLSGGEKQRI 591
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 628 ALARALIRKPLLLILDDATSALdagnQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHIL-FLREGS 695
Cdd:TIGR00954 592 AMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLyMDGRGG 656
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-705 |
3.62e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.43 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGG-----QLLLDGQCLVQY-DHHYLHTQVAAVGQEPLLFGR 569
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 570 SFRENIAYGLN----------RTPTMEEITAVAVESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPLL 639
Cdd:PRK14271 116 SIMDNVLAGVRahklvprkefRGVAQARLTEVGLWDAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 640 LILDDATSALDAGNQLRVQRLLYESPKRAsrTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQL 705
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
179-454 |
3.72e-12 |
|
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: 67.59 E-value: 3.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTVPSFtrNIWL--MSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNP 256
Cdd:cd18568 20 ALPLFTQIILDRVLVHKNISLL--NLILigLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 257 AGSITSRVTED-------TANVCESISGTLSLLLwYLGralcllvFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLA 329
Cdd:cd18568 98 VGDIITRFQENqkirrflTRSALTTILDLLMVFI-YLG-------LMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 330 VKVQESLAKSTQVALEALSAMPTVRSFANEegeaQKFRQKLEE--MKTLN---KKEALAYVAEVwTTSVSGMLLKVGILY 404
Cdd:cd18568 170 REIFQANAEQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNtrfRGQKLSIVLQL-ISSLINHLGTIAVLW 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 239835765 405 LGGQLVIRGAVSSGNLVSF-VLYQLqFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18568 245 YGAYLVISGQLTIGQLVAFnMLFGS-VINPLLALVGLWDELQETRISVERL 294
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
618-707 |
3.75e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.23 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 618 QLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSL-AEQAHHILFLREGSV 696
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQV 232
|
90
....*....|.
gi 239835765 697 GEQGTHLQLMK 707
Cdd:PRK11022 233 VETGKAHDIFR 243
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
472-688 |
4.43e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.81 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 472 PSNMKGLVEFQD--VSF------AYPNQP--KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLD 541
Cdd:PRK15079 2 TEGKKVLLEVADlkVHFdikdgkQWFWQPpkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 542 GQCLVQYDHHYLHT---QVAAVGQEPL--LFGR-SFRENIAYGLnRT--PTM------EEITAVAVESG-AHDFISGFPq 606
Cdd:PRK15079 82 GKDLLGMKDDEWRAvrsDIQMIFQDPLasLNPRmTIGEIIAEPL-RTyhPKLsrqevkDRVKAMMLKVGlLPNLINRYP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 607 gydtevgetgNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEqah 686
Cdd:PRK15079 160 ----------HEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVK--- 226
|
..
gi 239835765 687 HI 688
Cdd:PRK15079 227 HI 228
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
187-454 |
4.49e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 67.54 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 187 ITDWILQDKTVPSFTRN-----------IWLMSILTIASTALEFASDGIYNITMG----HMHGRVHREVFRAVLRQETGF 251
Cdd:cd18564 25 VIDDVLGDKPLPGLLGLapllgpdplalLLLAAAALVGIALLRGLASYAGTYLTAlvgqRVVLDLRRDLFAHLQRLSLSF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 252 FLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVK 331
Cdd:cd18564 105 HDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASRE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 332 VQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQklEEMKTLNKKEALAYVAEVWTTSVSgMLLKVG---ILYLGGQ 408
Cdd:cd18564 185 QRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR--ENRKSLRAGLRAARLQALLSPVVD-VLVAVGtalVLWFGAW 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 239835765 409 LVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18564 262 LVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-454 |
7.56e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 66.73 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASdgIYN---ITMGHMHgRVHREVFRAVLRQETGFFLKN 255
Cdd:cd18540 20 VFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLF--IRLagkIEMGVSY-DLRKKAFEHLQTLSFSYFDKT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 256 PAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLInlpllfllpkklgkVHQSLAV----- 330
Cdd:cd18540 97 PVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLA--------------VVPVLAVvsiyf 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 331 ---------KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKeaLAYVAEVWTTSVSgMLLKVG 401
Cdd:cd18540 163 qkkilkayrKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVR--AARLSALFLPIVL-FLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 402 ---ILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18540 240 talVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
474-649 |
1.96e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 474 NMKGLVEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclvQYDH--H 551
Cdd:PRK09700 1 MATPYISMAGIGKSFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI---NYNKldH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 YLHTQ--VAAVGQEPLLFGR-SFRENIAYGlnRTPT-------------MEEITAVAVesgahdFISGFPQGYDTEVGEt 615
Cdd:PRK09700 75 KLAAQlgIGIIYQELSVIDElTVLENLYIG--RHLTkkvcgvniidwreMRVRAAMML------LRVGLKVDLDEKVAN- 145
|
170 180 190
....*....|....*....|....*....|....
gi 239835765 616 gnqLSGGQRQAVALARALIRKPLLLILDDATSAL 649
Cdd:PRK09700 146 ---LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
491-708 |
5.75e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.54 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 491 QPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQP----TGGQLLLDGQCLVQYD----HHYLHTQVAAVGQ 562
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSprerRKIIGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 EPL-------LFGRSFRENIA-----------YGLNRTPTMEEITAVAVESgaHDFI-SGFPqgydtevgetgNQLSGGQ 623
Cdd:COG4170 97 EPSscldpsaKIGDQLIEAIPswtfkgkwwqrFKWRKKRAIELLHRVGIKD--HKDImNSYP-----------HELTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 624 RQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQL-SLAEQAHHILFLREGSVGEQGTH 702
Cdd:COG4170 164 CQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLeSISQWADTITVLYCGQTVESGPT 243
|
....*.
gi 239835765 703 LQLMKR 708
Cdd:COG4170 244 EQILKS 249
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
479-705 |
7.61e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 64.28 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQ-------------CL 545
Cdd:PRK11000 4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergvgMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 546 VQYDHHYLHTQVAavgqepllfgrsfrENIAYGLNRTPTMEEITAVAVESGAhdfisgfpqgydtEVGETGN-------Q 618
Cdd:PRK11000 81 FQSYALYPHLSVA--------------ENMSFGLKLAGAKKEEINQRVNQVA-------------EVLQLAHlldrkpkA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 619 LSGGQRQAVALARALIRKPLLLILDDATSALDAGnqLRVQ------RLlyesPKRASRTVLLITQ-QLSLAEQAHHILFL 691
Cdd:PRK11000 134 LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA--LRVQmrieisRL----HKRLGRTMIYVTHdQVEAMTLADKIVVL 207
|
250
....*....|....
gi 239835765 692 REGSVGEQGTHLQL 705
Cdd:PRK11000 208 DAGRVAQVGKPLEL 221
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
496-722 |
7.77e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 63.31 E-value: 7.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTV----AALLQNLYQPTG----GQLLLDGQCLVQYDHHYLHTQVAAVGQ--EPl 565
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 566 LFGRSFRENIAYGlnRTPTMEEITAVAVESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARAL---------IRK 636
Cdd:PRK13547 95 AFAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 637 PLLLILDDATSALDAGNQLRvqrlLYESPKRASRT----VLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQLMKRG-- 709
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHR----LLDTVRRLARDwnlgVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPAhi 248
|
250
....*....|....
gi 239835765 710 -GCYRAMVEALAAP 722
Cdd:PRK13547 249 aRCYGFAVRLVDAG 262
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
178-454 |
1.12e-10 |
|
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: 63.38 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPA 257
Cdd:cd18782 19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 258 GSITSRVTEdTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLA 337
Cdd:cd18782 99 GELSTRISE-LDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 338 KSTQVALEALSAMPTVRSFANEEgeaqKFRQKLEEmktlnkkEALAYVAEVWTTSVSGMLL-----------KVGILYLG 406
Cdd:cd18782 178 KTQSYLVESLTGIQTVKAQNAEL----KARWRWQN-------RYARSLGEGFKLTVLGTTSgslsqflnklsSLLVLWVG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 239835765 407 GQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18782 247 AYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
475-700 |
1.42e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.17 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQ-----PTGGQLLLDGQCLVQYD 549
Cdd:PRK14267 1 MKFAIETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 550 HHYLHT--QVAAVGQEPLLFGR-SFRENIAYGL------NRTPTMEEITAVAVESGA-----HDFISGFPqgydtevget 615
Cdd:PRK14267 78 VDPIEVrrEVGMVFQYPNPFPHlTIYDNVAIGVklnglvKSKKELDERVEWALKKAAlwdevKDRLNDYP---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 616 gNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKraSRTVLLITQQLSLAEQ-AHHILFLREG 694
Cdd:PRK14267 148 -SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARvSDYVAFLYLG 224
|
....*.
gi 239835765 695 SVGEQG 700
Cdd:PRK14267 225 KLIEVG 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
482-676 |
1.47e-10 |
|
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: 64.19 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 482 QDVSFAYPnqPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYdhhylhtqvaaVG 561
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGY-----------LP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 562 QEPLL-FGRSFRENIAYGLNRTPTM----EEITAVAVE---------------------SGAHDFISGF---------PQ 606
Cdd:TIGR03719 75 QEPQLdPTKTVRENVEEGVAEIKDAldrfNEISAKYAEpdadfdklaaeqaelqeiidaADAWDLDSQLeiamdalrcPP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 607 GyDTEVgetgNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKrasrTVLLIT 676
Cdd:TIGR03719 155 W-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVT 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
506-677 |
1.65e-10 |
|
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: 59.69 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 506 PGTVTALVGPNGSGKSTVA-ALLQNLYQPTGGQLLLDGQCLVQYDHHYLHtqvaavgqepllfgrsfreniayglnrtpt 584
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLArALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 585 meeitavavesgahdfisgfpqgyDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQ-----R 659
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelR 106
|
170
....*....|....*...
gi 239835765 660 LLYESPKRASRTVLLITQ 677
Cdd:smart00382 107 LLLLLKSEKNLTVILTTN 124
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
204-454 |
1.78e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 62.97 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 204 IWLMSILTIASTALEFASDGIYNITMGHMHGRVHREV----FRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTL 279
Cdd:cd18565 53 LWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLrtdtYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 280 SLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAK-STQvaLE-ALSAMPTVRSFA 357
Cdd:cd18565 133 NSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNAR--LEnNLSGIAVIKAFT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 358 NEEGEAQKFRQKLEEMKTLNK---KEALAYVAEVWTTSVSGMLLkvgILYLGGQLVIRGAV------SSGNLVSFVLYQL 428
Cdd:cd18565 211 AEDFERERVADASEEYRDANWraiRLRAAFFPVIRLVAGAGFVA---TFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQ 287
|
250 260
....*....|....*....|....*.
gi 239835765 429 QFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18565 288 RLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
475-651 |
2.51e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEfqdvSFaypnqPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGQCLVQydHH 551
Cdd:PRK13549 8 MKNITK----TF-----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQA--SN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 YLHTQ---VAAVGQEPLLF-GRSFRENIAYGlnrtptmEEITavavESGAHDfisgFPQGY----------------DTE 611
Cdd:PRK13549 76 IRDTEragIAIIHQELALVkELSVLENIFLG-------NEIT----PGGIMD----YDAMYlraqkllaqlkldinpATP 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 239835765 612 VGETGnqlsGGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:PRK13549 141 VGNLG----LGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
491-700 |
3.06e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.25 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 491 QPKVQVLQGLTFTLHPGTVTALVGPNGSGKS-TVAALLQNL---YQPTGGQLLLDGQCLVQYDHHYLHtqVAAVGQEPll 566
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRK--IATIMQNP-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 567 fgRS-F----------RENIAyGLNRTPTMEEITAVAVESGAHDfISGFPQGYDTEvgetgnqLSGGQRQAVALARALIR 635
Cdd:PRK10418 89 --RSaFnplhtmhthaRETCL-ALGKPADDATLTAALEAVGLEN-AARVLKLYPFE-------MSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS-LAEQAHHILFLREGSVGEQG 700
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRIVEQG 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
496-694 |
3.45e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 63.36 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG--GQLLLDGQCLV-----------QYDHHYLHTQVaavgQ 562
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTkqilkrtgfvtQDDILYPHLTV----R 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 563 EPLLFGRSFReniaygLNRTPTMEEITAVAvESGAHDFisGFPQGYDTEVGETGNQ-LSGGQRQAVALARALIRKPLLLI 641
Cdd:PLN03211 159 ETLVFCSLLR------LPKSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 239835765 642 LDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQA-HHILFLREG 694
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMfDSVLVLSEG 283
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
494-676 |
4.63e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 4.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHtQVAAV-GQE-------PL 565
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfGQRsqlwwdlPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 566 LfgRSFRENIA-YGLNRT---PTMEEITAVAvesGAHDFIsgfpqgyDTEVgetgNQLSGGQRQAVALARALIRKPLLLI 641
Cdd:COG4586 114 I--DSFRLLKAiYRIPDAeykKRLDELVELL---DLGELL-------DTPV----RQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|....*
gi 239835765 642 LDDATSALDAGNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTS 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
497-700 |
9.13e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 9.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYD---------HHYLHTQVAAVGQEP--- 564
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDlyalseaerRRLLRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 565 LLFGRSFRENIA----------YGlnrtptmeEITAVA------VESGAhDFISGFPQGYdtevgetgnqlSGGQRQAVA 628
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYG--------DIRATAgdwlerVEIDA-ARIDDLPTTF-----------SGGMQQRLQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
473-644 |
1.04e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.78 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 473 SNMKGLVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHY 552
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 LHT---QVAAVGQEPLLF-GRSFRENIAYGLN----------RTPTMEEITAVAVESGAHDFISgfpqgydtevgetgnQ 618
Cdd:PRK11831 79 LYTvrkRMSMLFQSGALFtDMNVFDNVAYPLRehtqlpapllHSTVMMKLEAVGLRGAAKLMPS---------------E 143
|
170 180
....*....|....*....|....*.
gi 239835765 619 LSGGQRQAVALARALIRKPLLLILDD 644
Cdd:PRK11831 144 LSGGMARRAALARAIALEPDLIMFDE 169
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
479-650 |
1.09e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGQCLvqydhhylhtQVA 558
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 559 AVGQ--EPLLFGRSFRENIAYGLnrtptmEEITAVAVESGAHDFISGFP-QGYDTE--VGetgnQLSGGQRQAVALARAL 633
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGL------DIIKLGKREIPSRAYVGRFNfKGSDQQkkVG----QLSGGERNRVHLAKTL 458
|
170
....*....|....*..
gi 239835765 634 IRKPLLLILDDATSALD 650
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
500-707 |
1.09e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 500 LTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTGGQLLLDGQCLVQYDHHYLHTQVAAVGQEpllfgrsfreniaygl 579
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQ---------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 580 NRTPTMEEI-----------TAVAVESGAHDFISGFpQGYDTEVGETGNQLSGGQRQAVALARALIR-KPL------LLI 641
Cdd:PRK03695 78 QTPPFAMPVfqyltlhqpdkTRTEAVASALNEVAEA-LGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDinpagqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 642 LDDATSALDAGNQLRVQRLLYESPkRASRTVLLITQQLS-LAEQAHHILFLREGSVGEQGTHLQLMK 707
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
488-701 |
1.48e-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: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 488 YPNQPKVQVLQGLTFTLHPGT-----VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQClVQYDHHY---------- 552
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQYikadyegtvr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 --LHTQVAAVGQEPllfgrSFRENIAYGLNrtptMEEItavavesgahdfisgfpqgYDTEVgetgNQLSGGQRQAVALA 630
Cdd:cd03237 80 dlLSSITKDFYTHP-----YFKTEIAKPLQ----IEQI-------------------LDREV----PELSGGELQRVAIA 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 631 RALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAHHILFLREGSVGEQGT 701
Cdd:cd03237 128 ACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNGV 198
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
238-454 |
1.68e-09 |
|
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: 59.43 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 238 REVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLL 317
Cdd:cd18546 76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 318 PKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKeALAYVAEVW-TTSVSGM 396
Cdd:cd18546 156 TRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLR-AQRLVAIYFpGVELLGN 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 397 LLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18546 235 LATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
493-700 |
1.77e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQ---CLVQYDHHYLHTQVAAVGQEP----- 564
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 565 -----------------LLFGRSFRENIAYGLNRTPTMEEitavavesgaHDFisGFPqgydtevgetgNQLSGGQRQAV 627
Cdd:PRK10261 416 prqtvgdsimeplrvhgLLPGKAAAARVAWLLERVGLLPE----------HAW--RYP-----------HEFSGGQRQRI 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQG 700
Cdd:PRK10261 473 CIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
496-698 |
2.20e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVqydhhyLHTQVAAVGQ-----------EP 564
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDAIRAgiayvpedrkgEG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 565 LLFGRSFRENIA---------YGLNRTPTMEEITAvavesgahDFISGF---PQGYDTEVGetgnQLSGGQRQAVALARA 632
Cdd:COG1129 341 LVLDLSIRENITlasldrlsrGGLLDRRRERALAE--------EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQLS-LAEQAHHILFLREGS-VGE 698
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPeLLGLSDRILVMREGRiVGE 475
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
489-701 |
2.29e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 489 PNQpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL----LLDGQCLVQYDHHYLHTQ-------- 556
Cdd:PRK13631 36 ENE--LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYSkkiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 ----VAAVGQEP--LLFGRSFRENIAYGlnrtPTMEEITAVAVESGAHDFISGFPQGYD-TEVGETGnqLSGGQRQAVAL 629
Cdd:PRK13631 114 lrrrVSMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 630 ARALIRKPLLLILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQL-SLAEQAHHILFLREGSVGEQGT 701
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
495-696 |
2.37e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.87 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY---QPTGGQLLLDGQCL-----VQYDHHYLHTQVAAVGQEPLL 566
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVqregrLARDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 567 FGR-SFRENIAYG-LNRTP----------------TMEEITAVAVESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 628
Cdd:PRK09984 98 VNRlSVLENVLIGaLGSTPfwrtcfswftreqkqrALQALTRVGMVHFAHQRVS---------------TLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 629 LARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLA-EQAHHILFLREGSV 696
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHV 231
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
478-650 |
2.56e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQ-YDHHylHTQ 556
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvFSQH--HVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLFgrsfreniayglnrtptMEEITAVAVESGAHDFISGFpqgydtevGETGN-------QLSGGQRQAVAL 629
Cdd:PLN03073 584 GLDLSSNPLLY-----------------MMRCFPGVPEQKLRAHLGSF--------GVTGNlalqpmyTLSGGQKSRVAF 638
|
170 180
....*....|....*....|.
gi 239835765 630 ARALIRKPLLLILDDATSALD 650
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLD 659
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
482-676 |
2.66e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 482 QDVSFAYPnqPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQ-LLLDGqclvqydhhylhtqvAAV 560
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG---------------IKV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 561 G---QEPLL-FGRSFRENIAYG-------LNR---------TPtMEEITAVAVESG----------AHDFIS-------- 602
Cdd:PRK11819 73 GylpQEPQLdPEKTVRENVEEGvaevkaaLDRfneiyaayaEP-DADFDALAAEQGelqeiidaadAWDLDSqleiamda 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 603 -GFPQGyDTEVGetgnQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKrasrTVLLIT 676
Cdd:PRK11819 152 lRCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVT 217
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
493-545 |
3.06e-09 |
|
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: 58.04 E-value: 3.06e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGQCL 545
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDL 66
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
475-649 |
3.94e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 475 MKGLVEFQDVSFAYPNqpkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHylH 554
Cdd:PRK10762 1 MQALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVG---QEPLLFGR-SFRENIAYGLNRTPTMEEITAVAVESGAHDFIS--GFPQGYDTEVGEtgnqLSGGQRQAVA 628
Cdd:PRK10762 76 SQEAGIGiihQELNLIPQlTIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180
....*....|....*....|.
gi 239835765 629 LARALIRKPLLLILDDATSAL 649
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDAL 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
494-651 |
4.50e-09 |
|
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: 59.45 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGQCLVQydHHYLHTQ---VAAVGQEPLLF 567
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKA--SNIRDTEragIVIIHQELTLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 GR-SFRENIAYGLNRTPTMEEITAVAVESGAHDFISGFpQGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:TIGR02633 91 PElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
....*
gi 239835765 647 SALDA 651
Cdd:TIGR02633 170 SSLTE 174
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
494-679 |
4.77e-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: 59.43 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLL--------------DGQCLVQYDHHYLHtqvaa 559
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgpDGRGRAKRYIGILH----- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 vgQEPLLFG-RSFRENI--AYGLNRTPTMEEITAVAVESGAhdfisGFPQGYDTEVGET-GNQLSGGQRQAVALARALIR 635
Cdd:TIGR03269 372 --QEYDLYPhRTVLDNLteAIGLELPDELARMKAVITLKMV-----GFDEEKAEEILDKyPDELSEGERHRVALAQVLIK 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 239835765 636 KPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQL 679
Cdd:TIGR03269 445 EPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
496-676 |
4.97e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.28 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLY--QPTGGQL-LLDGQClvqydhhylhtqvaavGQE-PLLfgrsf 571
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVdVPDNQF----------------GREaSLI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 572 rENIAYGLNRTPTMEEITAVAVeSGAHDFISGFPqgydtevgetgnQLSGGQRQAVALARALIRKPLLLILDDATSALDA 651
Cdd:COG2401 104 -DAIGRKGDFKDAVELLNAVGL-SDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*
gi 239835765 652 GNQLRVQRLLYESPKRASRTVLLIT 676
Cdd:COG2401 170 QTAKRVARNLQKLARRAGITLVVAT 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
500-705 |
7.05e-09 |
|
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: 59.64 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 500 LTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDG-----------QCLVQYDHH---YLHTQVAavgqEPL 565
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGkdietnldavrQSLGMCPQHnilFHHLTVA----EHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 566 LF-----GRSFREniayglnrtpTMEEITAVAVESGAHDfisgfpqgydtEVGETGNQLSGGQRQAVALARALIRKPLLL 640
Cdd:TIGR01257 1025 LFyaqlkGRSWEE----------AQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 641 ILDDATSALDAGNQLRVQRLLYESpkRASRTVLLITQQLSLAE-QAHHILFLREGSVGEQGTHLQL 705
Cdd:TIGR01257 1084 VLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFL 1147
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
485-651 |
8.47e-09 |
|
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: 56.12 E-value: 8.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 485 SFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTG---GQLLLDGqclVQYD--HHYLHTQVAA 559
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNG---IPYKefAEKYPGEIIY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQE----PLLfgrsfreniayglnrtpTMEEITAVAVESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARALIR 635
Cdd:cd03233 88 VSEEdvhfPTL-----------------TVRETLDFALRCKGNEFVRGI---------------SGGERKRVSIAEALVS 135
|
170
....*....|....*.
gi 239835765 636 KPLLLILDDATSALDA 651
Cdd:cd03233 136 RASVLCWDNSTRGLDS 151
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
481-694 |
1.43e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.33 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 481 FQDVSFAYP-NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLYQPT-----GGQLLLDGQCLVQY------ 548
Cdd:cd03232 6 WKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDKNfqrstg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 549 --DHHYLHTQVAAVgQEPLLFGRSFREniayglnrtptmeeitavavesgahdfisgfpqgydtevgetgnqLSGGQRQA 626
Cdd:cd03232 83 yvEQQDVHSPNLTV-REALRFSALLRG---------------------------------------------LSVEQRKR 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 627 VALARALIRKPLLLILDDATSALDAGNQLRVQRLLyespKR---ASRTVLLITQQLS--LAEQAHHILFLREG 694
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL----KKladSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
494-708 |
1.76e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.50 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 494 VQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNL--YQPTGGQLL----LDGQCLVQYDHHYLHTQVAAVGQEPLLF 567
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvaLCEKCGYVERPSKVGEPCPVCGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 G-----------RSFRENIAYGLNRT--------------PTMEEITAVAVES--GAHDFISGFPQGYdtEVGETGNQLS 620
Cdd:TIGR03269 93 EvdfwnlsdklrRRIRKRIAIMLQRTfalygddtvldnvlEALEEIGYEGKEAvgRAVDLIEMVQLSH--RITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKrASRTVLLITQQLS--LAEQAHHILFLREGSVGE 698
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVK-ASGISMVLTSHWPevIEDLSDKAIWLENGEIKE 249
|
250
....*....|
gi 239835765 699 QGTHLQLMKR 708
Cdd:TIGR03269 250 EGTPDEVVAV 259
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
199-457 |
2.09e-08 |
|
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: 56.36 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 199 SFTRNIWLMSILTIASTALefasdgiynitmghmhgrvHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGT 278
Cdd:cd18580 56 VLLRWLLFVLAGLRASRRL-------------------HDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 279 LSLLLWYLGRALCLLVFMFWGSPYLTLVTLInlplLFLLPKKLGKVHQSLA--VKVQESLAKS---TQVaLEALSAMPTV 353
Cdd:cd18580 117 LLDFLQSLFSVLGSLIVIAIVSPYFLIVLPP----LLVVYYLLQRYYLRTSrqLRRLESESRSplySHF-SETLSGLSTI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 354 RSFANEEGEAQKFRQKLEE-------MKTLNkkEALAYVAEVwttSVSGMLLKVGILylggqLVIRGAVSSGNLVSFVLY 426
Cdd:cd18580 192 RAFGWQERFIEENLRLLDAsqrafylLLAVQ--RWLGLRLDL---LGALLALVVALL-----AVLLRSSISAGLVGLALT 261
|
250 260 270
....*....|....*....|....*....|..
gi 239835765 427 Q-LQFTQAVQVLLSLYPSMQKAVGSSEKIFEY 457
Cdd:cd18580 262 YaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
178-454 |
2.16e-08 |
|
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: 56.27 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 178 MAIPFFTGRITDWILQ-------DKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETG 250
Cdd:cd18554 16 LLLPLILKYIVDDVIQgssltldEKVYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 251 FFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTL-INLPLLFLLPKKLGKVHQSLA 329
Cdd:cd18554 96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLvIFPFYILAVKYFFGRLRKLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 330 VKVQEsLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEM--KTLNKKEALAY-VAEVWTTSVSGMLLKVGIlylG 406
Cdd:cd18554 176 ERSQA-LAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFltRALKHTRWNAKtFSAVNTITDLAPLLVIGF---A 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 239835765 407 GQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18554 252 AYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
483-705 |
2.50e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.17 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 483 DVSFAYPNQP--KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQ-----YDHHYLHT 555
Cdd:PRK13645 11 NVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEP--LLFGRSFRENIAYG-LNRTPTMEEITAVAVEsgAHDFISgFPQGYdteVGETGNQLSGGQRQAVALARA 632
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFGpVNLGENKQEAYKKVPE--LLKLVQ-LPEDY---VKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQL-SLAEQAHHILFLREGSVGEQGTHLQL 705
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFEI 238
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
240-441 |
3.47e-08 |
|
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: 55.55 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 240 VFRAVLRQETGFFLKNPAGSITSRVteDTANVCES------ISGTLSLLLwylgrALCLLVFMFWGSPYLTLVTLINLPL 313
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRF--GSLDEIQQtlttgfVEALLDGLM-----AILTLVMMFLYSPKLALIVLAAVAL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 314 LFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkTLNKKEALAYVaEVWTTSV 393
Cdd:cd18567 154 YALLRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVD--AINADIRLQRL-QILFSAA 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 239835765 394 SGMLL---KVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLY 441
Cdd:cd18567 231 NGLLFgleNILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKL 281
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
495-661 |
9.45e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 53.74 E-value: 9.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYD-HHYLHTQVAAVGQEPLLFGR-SFR 572
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 573 ENIAYGLNrtpTMEEITAVAVESGAHDFISGFPQGYDTEvgETGNQLSGGQRQAVALARALIRKPLLLILDDATSALDAG 652
Cdd:PRK10895 97 DNLMAVLQ---IRDDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
....*....
gi 239835765 653 NQLRVQRLL 661
Cdd:PRK10895 172 SVIDIKRII 180
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
492-649 |
1.03e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.12 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 492 PKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQcLVQY--DHHYLHTQVAAVGQE-PLLFG 568
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFksSKEALENGISMVHQElNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 569 RSFRENIAYGlnRTPTmeeiTAVAVESGA--HDFISGFPQ-GYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDA 645
Cdd:PRK10982 88 RSVMDNMWLG--RYPT----KGMFVDQDKmyRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
|
....
gi 239835765 646 TSAL 649
Cdd:PRK10982 162 TSSL 165
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
501-681 |
1.48e-07 |
|
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: 53.14 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 501 TFTLH------PGTVTALVGPNGSGKSTVAALLQNLYQPTGGQL--------LLD---GQCLVQYDHHYLHTQVAAVgQE 563
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVI-VK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 564 PL---LFGRSFRENIAYGLNRTPtmeeitavavESGAHDFIS---GFPQGYDTEVgetgNQLSGGQRQAVALARALIRKP 637
Cdd:cd03236 93 PQyvdLIPKAVKGKVGELLKKKD----------ERGKLDELVdqlELRHVLDRNI----DQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 239835765 638 LLLILDDATSALDAGNQLRVQRLLYESPKRAsRTVLLITQQLSL 681
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIRELAEDD-NYVLVVEHDLAV 201
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
495-565 |
1.61e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALL--QNLYQPTGGQLLLDGQCLV----------------QY-------- 548
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLelspedragegifmafQYpveipgvs 94
|
90 100
....*....|....*....|.
gi 239835765 549 DHHYLHTQVAAV----GQEPL 565
Cdd:PRK09580 95 NQFFLQTALNAVrsyrGQEPL 115
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
478-679 |
2.31e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.88 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSfaYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYD-HHYLHTQ 556
Cdd:COG3845 257 VLEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 557 VAAVGQEPLLFG----RSFRENIAYGLNRTPTM--------EEITAVAVEsgahdFISGF---PQGYDTEVGetgnQLSG 621
Cdd:COG3845 335 VAYIPEDRLGRGlvpdMSVAENLILGRYRRPPFsrggfldrKAIRAFAEE-----LIEEFdvrTPGPDTPAR----SLSG 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 239835765 622 GQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYEspKRASRT-VLLITQQL 679
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE--LRDAGAaVLLISEDL 462
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
501-652 |
3.30e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 501 TFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLV-QYDHHYLHTQVAAVGQEP----LLFGRSFRENI 575
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRkrdgLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 576 --------AYGLNRTPTMEEITAVAvesgahDFISGF----PqGYDTEVGEtgnqLSGGQRQAVALARALIRKPLLLILD 643
Cdd:PRK10762 352 sltalryfSRAGGSLKHADEQQAVS------DFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420
|
....*....
gi 239835765 644 DATSALDAG 652
Cdd:PRK10762 421 EPTRGVDVG 429
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
479-650 |
3.35e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPNQpkvqVL-QGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLdGQCLvqydhhylhtQV 557
Cdd:PRK11819 325 IEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQepllfgrsFRENIAYglNRTpTMEEItavaveSGAHDFIS---------------GFpQGYDTE--VGetgnQLS 620
Cdd:PRK11819 390 AYVDQ--------SRDALDP--NKT-VWEEI------SGGLDIIKvgnreipsrayvgrfNF-KGGDQQkkVG----VLS 447
|
170 180 190
....*....|....*....|....*....|
gi 239835765 621 GGQRQAVALARALIRKPLLLILDDATSALD 650
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
493-706 |
3.72e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTvaaLLQNLYQPTGGQLLLDGQCLV-----------------QYDhhyLHT 555
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVngrpldssfqrsigyvqQQD---LHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVgQEPLLFGRSFRENiayglNRTPTMEE-------ITAVAVESGAhdfisgfpqgyDTEVGETGNQLSGGQRQAVA 628
Cdd:TIGR00956 849 PTSTV-RESLRFSAYLRQP-----KSVSKSEKmeyveevIKLLEMESYA-----------DAVVGVPGEGLNVEQRKRLT 911
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 629 LARALIRKP-LLLILDDATSALDAGNQLRVQRLLYESPKrASRTVLLITQQLS--LAEQAHHILFLREGS----VGEQGT 701
Cdd:TIGR00956 912 IGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaiLFEEFDRLLLLQKGGqtvyFGDLGE 990
|
....*
gi 239835765 702 HLQLM 706
Cdd:TIGR00956 991 NSHTI 995
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
492-649 |
3.96e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 492 PKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYqPTG---GQLLLDGQcLVQY------DHH---YLHTQVAA 559
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGE-VCRFkdirdsEALgivIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VgqePLLfgrSFRENIAYG--------LNRTPTMEEITAVAVESGAHDfisgFPqgyDTEVGETGNqlsgGQRQAVALAR 631
Cdd:NF040905 90 I---PYL---SIAENIFLGnerakrgvIDWNETNRRARELLAKVGLDE----SP---DTLVTDIGV----GKQQLVEIAK 152
|
170
....*....|....*...
gi 239835765 632 ALIRKPLLLILDDATSAL 649
Cdd:NF040905 153 ALSKDVKLLILDEPTAAL 170
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
480-650 |
4.22e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.42 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 480 EFQDVSFAYPNQpkvQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLlldgQCLVQYDHHYLHTQVAA 559
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 560 VGQEpllfgRSFRENIAYGlnrtptMEEITAVAVESGAHDFISGF---PQGYDTEVgetgNQLSGGQRQAVALARALIRK 636
Cdd:PRK11147 394 LDPE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKP 458
|
170
....*....|....
gi 239835765 637 PLLLILDDATSALD 650
Cdd:PRK11147 459 SNLLILDEPTNDLD 472
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
235-454 |
4.65e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 52.13 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 235 RVHREVFRAVLRQETGFFLKNPAGSITSRVTEdTANVCESISGTL--SLLlwylgRALCLLVF---MFWGSPYLTLVTLI 309
Cdd:cd18783 76 RLALRTFDRLLSLPIDFFERTPAGVLTKHMQQ-IERIRQFLTGQLfgTLL-----DATSLLVFlpvLFFYSPTLALVVLA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 310 NLPLLFLLPKKLGKVHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkTLNKKEALAYVAeVW 389
Cdd:cd18783 150 FSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVAR--AIRARFAVGRLS-NW 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 390 TTSVSG---MLLKVGILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18783 227 PQTLTGpleKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
244-454 |
5.27e-07 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 52.09 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 244 VLRQETGFFLKNPAGSITSRVtEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGK 323
Cdd:cd18569 85 VLRLPVEFFSQRYAGDIASRV-QSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 324 VHQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGeaqkFRQKLEEM--KTLNKKEALAyVAEVWTTSVSGMLLKVG 401
Cdd:cd18569 164 KRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESD----FFSRWAGYqaKVLNAQQELG-RTNQLLGALPTLLSALT 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 239835765 402 ---ILYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18569 239 naaILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
478-659 |
6.01e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.89 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQpKVQVLQGltfTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQclVQYDHHYLHTQV 557
Cdd:PRK13409 340 LVEYPDLTKKLGDF-SLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--ISYKPQYIKPDY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 AAVGQEpLL------FGRSF-RENIAYGLNrtptMEEItavavesgahdfisgfpqgYDTEVGEtgnqLSGGQRQAVALA 630
Cdd:PRK13409 414 DGTVED-LLrsitddLGSSYyKSEIIKPLQ----LERL-------------------LDKNVKD----LSGGELQRVAIA 465
|
170 180
....*....|....*....|....*....
gi 239835765 631 RALIRKPLLLILDDATSALDAGNQLRVQR 659
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVEQRLAVAK 494
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
491-680 |
8.41e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 8.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 491 QPKVQVLQGLTFTLHPGTVTALVGPNGSGKST-VAALLQNLYQ---PTGGQLLLDGQCLVQYDHHY-----------LHT 555
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvynaetdVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGqEPLLFGRSFR--ENIAYGLNRTPTMEEITAVAVEsgahdfISGFPQGYDTEVG-ETGNQLSGGQRQAVALARA 632
Cdd:TIGR00956 151 PHLTVG-ETLDFAARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEA 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 239835765 633 LIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLS 680
Cdd:TIGR00956 224 SLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCS 271
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
479-712 |
9.44e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.24 E-value: 9.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAY-PNQP-KVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQ---LLLDGQCLVQYDHHY- 552
Cdd:PRK13651 3 IKVKNIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 553 --------------------LHTQVAAVGQ--EPLLFGRSFRENIAYGlnrtPTMEEITAVAVESGAHDFIS--GFPQGY 608
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 609 dteVGETGNQLSGGQRQAVALARALIRKPLLLILDDATSALD-AGNQ--LRVQRLLYESPKrasrTVLLITQQL-SLAEQ 684
Cdd:PRK13651 159 ---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKeiLEIFDNLNKQGK----TIILVTHDLdNVLEW 231
|
250 260
....*....|....*....|....*...
gi 239835765 685 AHHILFLREGsvgeqgthlQLMKRGGCY 712
Cdd:PRK13651 232 TKRTIFFKDG---------KIIKDGDTY 250
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
181-448 |
1.33e-06 |
|
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: 50.69 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 181 PFFTGRITD--WILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPAG 258
Cdd:cd18560 16 PLFLGRAVNalTLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 259 SITSRVTEDTanvcESISGTLSLLLWYLGRAL-----CLLVFMFWGSPYLTLVTLINLPllfllpkklgkVHQSLAVKVQ 333
Cdd:cd18560 96 EVVRIMDRGT----ESANTLLSYLVFYLVPTLlelivVSVVFAFHFGAWLALIVFLSVL-----------LYGVFTIKVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 334 ESLAK-----------STQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGI 402
Cdd:cd18560 161 EWRTKfrraankkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 239835765 403 LYLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAV 448
Cdd:cd18560 241 LLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
493-724 |
1.84e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.50 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 493 KVQVLQGLTFTLHPGTVTALVGPNGSGKSTvAALLQNLYQPTGGQ--LLLDGQCLvqyDHHYLHTQVAAvgQEPLLFGR- 569
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRrpWRF*TWCA---NRRALRRTIG*--HRPVR*GRr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 570 ---SFRENIaYGLNRTPTMEEITAVAvesGAHDFISGFpqGYDTEVGETGNQLSGGQRQAVALARALIRKPLLLILDDAT 646
Cdd:NF000106 99 esfSGRENL-YMIGR*LDLSRKDARA---RADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 647 SALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVGEQGTHLQL-MKRGGCYRAMVEALAAPAD 724
Cdd:NF000106 173 TGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELkTKVGGRTLQIRPAHAAELD 251
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
509-650 |
1.92e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.64 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 509 VTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVqyDHH---YLHTQVAAVG---QEPLLFGR-SFRENIAYGLNR 581
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEkgiCLPPEKRRIGyvfQDARLFPHyKVRGNLRYGMAK 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 239835765 582 T--PTMEEITAVAvesGAHDFISGFPQGydtevgetgnqLSGGQRQAVALARALIRKPLLLILDDATSALD 650
Cdd:PRK11144 104 SmvAQFDKIVALL---GIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
503-694 |
2.34e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.12 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 503 TLHPGTVTALVGPNGSGKSTvaallqnlyqptggqlLLDGQCLVqydhhylhtqvaavgqeplLFGRSFRENIAYGLNRT 582
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKST----------------ILDAIGLA-------------------LGGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 583 ptmEEITAVAVEsgahdFISGFPQgydtevgetgnqLSGGQRQAVALA-----RALIRKPlLLILDDATSALDAGNQLRV 657
Cdd:cd03227 62 ---CIVAAVSAE-----LIFTRLQ------------LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQAL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 239835765 658 QRLLYESPKRASrTVLLIT---QQLSLAEQAHHILFLREG 694
Cdd:cd03227 121 AEAILEHLVKGA-QVIVIThlpELAELADKLIHIKKVITG 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
501-666 |
2.73e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 501 TFTLHPGTVTALVGPNGSGKSTvaaLLQNLYQ------PTGGQLL-----LDG------QCLVQYD---------HHYLH 554
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTT---FLRYMAMhaidgiPKNCQILhveqeVVGddttalQCVLNTDiertqlleeEAQLV 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 TQVAAVgQEPLLFGRSFRENIAyGLNRTPT----------MEEITAVAVESGAHDFISGFPQGYDTEVGETgNQLSGGQR 624
Cdd:PLN03073 274 AQQREL-EFETETGKGKGANKD-GVDKDAVsqrleeiykrLELIDAYTAEARAASILAGLSFTPEMQVKAT-KTFSGGWR 350
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 239835765 625 QAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPK 666
Cdd:PLN03073 351 MRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK 392
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
497-679 |
3.45e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.11 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLhtqVAAVGQE-------PLL--- 566
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLved 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 567 ---FGRSFReniaYGLNRTPTMEE---ITAVAVESGAHDFisgfpqgYDTEVGEtgnqLSGGQRQAVALARALIRKPLLL 640
Cdd:PRK15056 100 vvmMGRYGH----MGWLRRAKKRDrqiVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVI 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 239835765 641 ILDDATSALDAGNQLRVQRLLYESpKRASRTVLLITQQL 679
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNL 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
478-661 |
5.00e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQpKVQVLQGltfTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQllLDGQCLVQYDHHYLHTQV 557
Cdd:COG1245 341 LVEYPDLTKSYGGF-SLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYKPQYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 ---------AAVGQEpllFGRS-FRENIAYGLNrtptMEEItavavesgahdfisgfpqgYDTEVGEtgnqLSGGQRQAV 627
Cdd:COG1245 415 dgtveeflrSANTDD---FGSSyYKTEIIKPLG----LEKL-------------------LDKNVKD----LSGGELQRV 464
|
170 180 190
....*....|....*....|....*....|....
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLL 661
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 498
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
179-454 |
5.55e-06 |
|
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: 48.66 E-value: 5.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASdGIYNITMG-HMHGRVHREVFRAVLRQETGFFLKNPA 257
Cdd:cd18555 20 LIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLR-GYIIIKLQtKLDKSLMSDFFEHLLKLPYSFFENRSS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 258 GSITSRvtedtAN----VCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTL-INLPLLFLLPKKLGKVHQslavKV 332
Cdd:cd18555 99 GDLLFR-----ANsnvyIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLlLGLLIVLLLLLTRKKIKK----LN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 333 QESLAKSTQVA---LEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKealayvAEVWTTSVSGM------LLKVGIL 403
Cdd:cd18555 170 QEEIVAQTKVQsylTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKK------KERLSNILNSIsssiqfIAPLLIL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 239835765 404 YLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18555 244 WIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
496-650 |
5.97e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 5.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 496 VLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGqclvqydhhylHTQVAAVGQE-PLLF------- 567
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQEtPALPqpaleyv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 568 ---GRSFRE-----NIAYGLNRTPT-------MEEITAVAVESGAHDFIS--GFPQgydTEVGETGNQLSGGQRQAVALA 630
Cdd:PRK10636 85 idgDREYRQleaqlHDANERNDGHAiatihgkLDAIDAWTIRSRAASLLHglGFSN---EQLERPVSDFSGGWRMRLNLA 161
|
170 180
....*....|....*....|
gi 239835765 631 RALIRKPLLLILDDATSALD 650
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
478-661 |
6.32e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLqnlyqpTGGqllldgqclvqydhhylHTQv 557
Cdd:PRK10938 260 RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGD-----------------HPQ- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 558 aAVGQEPLLFGR---------SFRENIAYgLNRTPTMEEITAVAVE----SGAHDFISGFPQ----------------GY 608
Cdd:PRK10938 313 -GYSNDLTLFGRrrgsgetiwDIKKHIGY-VSSSLHLDYRVSTSVRnvilSGFFDSIGIYQAvsdrqqklaqqwldilGI 390
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 239835765 609 DTEVGETGNQ-LSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLL 661
Cdd:PRK10938 391 DKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
495-549 |
6.82e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 6.82e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 495 QVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQN--LYQPTGGQLLLDGQCLVQYD 549
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE 77
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
179-454 |
9.60e-06 |
|
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: 47.96 E-value: 9.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTGRITDWILQDKTVPSFTRNIWLMSILTIASTALEFASDGIYNITMGHMHGRVHREVFRAVLRQETGFFLKNPAG 258
Cdd:cd18566 20 ATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 259 SITSRVtEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLAVKVQESLAK 338
Cdd:cd18566 100 AHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADER 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 339 STQVALEALSAMPTVRSFANEEGEAQKFRQKLEemKTLNKKEALAYVAEVW--TTSVSGMLLKVGILYLGGQLVIRGAVS 416
Cdd:cd18566 179 RQNFLIETLTGIHTIKAMAMEPQMLRRYERLQA--NAAYAGFKVAKINAVAqtLGQLFSQVSMVAVVAFGALLVINGDLT 256
|
250 260 270
....*....|....*....|....*....|....*...
gi 239835765 417 SGNLVSFVLYQLQFTQAVQVLLSLYPSMQKAVGSSEKI 454
Cdd:cd18566 257 VGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
497-679 |
1.55e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 497 LQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHHYLHTQVAAVgqepllfgrsfrENIA 576
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI------------ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 577 Y-----GLNRtptmEEITAVAVEsgahdfISGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKPLLLILDDats 647
Cdd:PRK13546 108 FkmlcmGFKR----KEIKAMTPK------IIEF-----SELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDE--- 169
|
170 180 190
....*....|....*....|....*....|....*
gi 239835765 648 ALDAGNQLRVQRLL---YESpKRASRTVLLITQQL 679
Cdd:PRK13546 170 ALSVGDQTFAQKCLdkiYEF-KEQNKTIFFVSHNL 203
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
484-684 |
1.63e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 484 VSFAYPNQPkVQVLQGLTFTLHPGTVTALVGPNGSGKSTVA----ALLQNLYQPTGGQLLLDGQCLVQYD----HHYLHT 555
Cdd:PRK15093 11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLLRLSprerRKLVGH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 556 QVAAVGQEPL-------LFGRSFRENIA-----------YGLNRTPTMEEITAVAVESgAHDFISGFPQgydtevgetgn 617
Cdd:PRK15093 90 NVSMIFQEPQscldpseRVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD-HKDAMRSFPY----------- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 239835765 618 QLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQ 684
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQ 224
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
179-421 |
1.69e-05 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 47.21 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 179 AIPFFTgritdwiLQ--DKTVPSftRNIWLMSILTIASTAL---EFASDGIYNITMGHMHGR----VHREVFRAVLRqet 249
Cdd:cd18586 20 APPIFM-------LQvyDRVLPS--GSLSTLLGLTLGMVVLlafDGLLRQVRSRILQRVGLRldveLGRRVFRAVLE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 250 GFFLKNPAGSITSRVtEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLINLPLLFLLPKKLGKVHQSLA 329
Cdd:cd18586 88 LPLESRPSGYWQQLL-RDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 330 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKTLNKKEALAYVAEVWTTSVSGMLLKVGILYLGGQL 409
Cdd:cd18586 167 GEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYL 246
|
250
....*....|..
gi 239835765 410 VIRGAVSSGNLV 421
Cdd:cd18586 247 VIDGELTIGALI 258
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
472-661 |
7.39e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 472 PSNMKGLVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDHh 551
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEP---VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 552 ylHTQVAAVGQEPLLFGR-SFRENIAY--GLN-RTPTMEEITAVAvesgahdfISGFPQGYDTEVgetgNQLSGGQRQAV 627
Cdd:PRK13543 81 --SRFMAYLGHLPGLKADlSTLENLHFlcGLHgRRAKQMPGSALA--------IVGLAGYEDTLV----RQLSAGQKKRL 146
|
170 180 190
....*....|....*....|....*....|....
gi 239835765 628 ALARALIRKPLLLILDDATSALDAGNQLRVQRLL 661
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
235-371 |
1.85e-04 |
|
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: 44.06 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 235 RVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLInlplL 314
Cdd:cd18605 76 RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLP----L 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 239835765 315 FLLPKKLGKV--HQSLAVKVQESLAKS---TQVAlEALSAMPTVRSFANEEGEAQKFRQKLE 371
Cdd:cd18605 152 AFIYYRIQRYyrATSRELKRLNSVNLSplyTHFS-ETLKGLVTIRAFRKQERFLKEYLEKLE 212
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
289-453 |
2.86e-04 |
|
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: 43.29 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 289 ALCLLVFMFwgSPYLTLVTLINLPLLFLLpkklGKVHQSLAVKVQESLAKS----TQVALEALSAMPTVRSFANEEGEAQ 364
Cdd:cd18583 127 AIVYLYYLF--DPYMGLIVAVVMVLYVWS----TIKLTSWRTKLRRDMIDAdreeRSILTESLLNWETVKYFNREPYEKE 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 365 KFRQKLEEMktlNKKEALAYVAEVWTTSVSGMLLKVGIL---YLGGQLVIRGAVSSGNLVSFVLYQLQFTQAVQVLLSLY 441
Cdd:cd18583 201 RYREAVKNY---QKAERKYLFSLNLLNAVQSLILTLGLLagcFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLY 277
|
170
....*....|..
gi 239835765 442 PSMQKAVGSSEK 453
Cdd:cd18583 278 RSIQSDLIDAER 289
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
235-457 |
3.05e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 43.23 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 235 RVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYLGRALCLLVFMFWGSPYLTLVTLInlplL 314
Cdd:cd18606 69 RLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPP----L 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 315 FLLPKKLGKVHQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFaneeGEAQKFRQKLEE-MKTLNKKEALAYVAEVW 389
Cdd:cd18606 145 LVLYYFIANYYRASSreLKRLESILRSFVYANfsESLSGLSTIRAY----GAQDRFIKKNEKlIDNMNRAYFLTIANQRW 220
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 239835765 390 ----TTSVSGML-LKVGILYLGGQLVIrGAVSSGNLVSFVlyqLQFTQAVQVLLSLYPSMQKAVGSSEKIFEY 457
Cdd:cd18606 221 lairLDLLGSLLvLIVALLCVTRRFSI-SPSSTGLVLSYV---LQITQVLSWLVRQFAEVENNMNSVERLLHY 289
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
478-696 |
3.09e-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: 44.05 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPKVQVLQGLTFTLHPGTVTALVGPNGSGKS-TVAALLQNLYQPTGGQLLLDGQ------------- 543
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKpvdirnpaqaira 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 544 --CLVQYDH--HYLHTQVAaVGQE---PLLFGRSFRENIAYGLNRTPTMEEITAVAVESgAHDFIsgfPQGydtevgetg 616
Cdd:TIGR02633 337 giAMVPEDRkrHGIVPILG-VGKNitlSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKT-ASPFL---PIG--------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 617 nQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYEspkRASRTVLLITQQLSLAEQ---AHHILFLRE 693
Cdd:TIGR02633 403 -RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQ---LAQEGVAIIVVSSELAEVlglSDRVLVIGE 478
|
...
gi 239835765 694 GSV 696
Cdd:TIGR02633 479 GKL 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
500-697 |
4.00e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 43.50 E-value: 4.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 500 LTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGGQLLLDGQCLVQYDhhylhtqVAAVGQEPLLFGRSFREniAYGL 579
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS-------TAQRLARGLVYLPEDRQ--SSGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 580 NrtptMEEITAVAVESGAHDFISGFPQ-GYDTEVGET-----------GNQ----LSGGQRQAVALARALIRKPLLLILD 643
Cdd:PRK15439 353 Y----LDAPLAWNVCALTHNRRGFWIKpARENAVLERyrralnikfnhAEQaartLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 644 DATSALDAGNQLRVQRLLyESPKRASRTVLLITQQLSLAEQ-AHHILFLREGSVG 697
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEIS 482
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
209-458 |
4.26e-04 |
|
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: 42.84 E-value: 4.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 209 ILTIASTALEFASDGIYniTMGHMHG--RVHREVFRAVLRQETGFFLKNPAGSITSRVTEDTANVCESISGTLSLLLWYL 286
Cdd:cd18604 51 LISLLSVLLGTLRYLLF--FFGSLRAsrKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLEST 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 287 GRALCLLVFMFWGSPYLTLVTLInlplLFLLPKKLGKV--HQSLAVKVQESLAKS---TQVAlEALSAMPTVRSFANEEg 361
Cdd:cd18604 129 LSLLVILIAIVVVSPAFLLPAVV----LAALYVYIGRLylRASRELKRLESVARSpilSHFG-ETLAGLVTIRAFGAEE- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 362 eaqKFRQKLeeMKTLNKKEALAY---VAEVW----TTSVSGML-LKVGILylggqLVIRGAVSSGnLVSFVL-YQLQFTQ 432
Cdd:cd18604 203 ---RFIEEM--LRRIDRYSRAFRylwNLNRWlsvrIDLLGALFsFATAAL-----LVYGPGIDAG-LAGFSLsFALGFSS 271
|
250 260
....*....|....*....|....*.
gi 239835765 433 AVQVLLSLYPSMQKAVGSSEKIFEYL 458
Cdd:cd18604 272 AILWLVRSYNELELDMNSVERIQEYL 297
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
478-650 |
4.41e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 478 LVEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLqnlyqpTGGQLLLDGQCLVQYD-------- 549
Cdd:PRK11147 3 LISIHGAWLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGRIIYEQDlivarlqq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 550 ----------------------------HHYLHTqvaaVGQEPllfgrsfRENIaygLNRTPTMEEITAVA----VESGA 597
Cdd:PRK11147 74 dpprnvegtvydfvaegieeqaeylkryHDISHL----VETDP-------SEKN---LNELAKLQEQLDHHnlwqLENRI 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 239835765 598 HDFISGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRKPLLLILDDATSALD 650
Cdd:PRK11147 140 NEVLAQLGLDPDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
498-527 |
1.57e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.19 E-value: 1.57e-03
10 20 30
....*....|....*....|....*....|....
gi 239835765 498 QGLTFTLHPGTVTALVGPNGSGKST----VAALL 527
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
490-704 |
1.94e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 490 NQPKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVaaLLQNLYqpTGGQLLLDGQcLVQYDHHylhtqvaavgqePLLFGR 569
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLISF-LPKFSRN------------KLIFID 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 570 SFRENIAYGLnrtptmeeitavavesgahdfisgfpqGYDTeVGETGNQLSGGQRQAVALARALIR--KPLLLILDDATS 647
Cdd:cd03238 67 QLQFLIDVGL---------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPST 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 648 ALDagnQLRVQRLLyESPKR---ASRTVLLITQQLSLAEQAHHILFLREGSvGEQGTHLQ 704
Cdd:cd03238 119 GLH---QQDINQLL-EVIKGlidLGNTVILIEHNLDVLSSADWIIDFGPGS-GKSGGKVV 173
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
607-696 |
2.70e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 607 GYDTEVGetgnQLSGGQRQAVALARALIRKPLLLILDDATSALDAGNQLRVQRLLYESPKRASRTVLLITQQLSLAEQAH 686
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITD 459
|
90
....*....|
gi 239835765 687 HILFLREGSV 696
Cdd:PRK10982 460 RILVMSNGLV 469
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
479-536 |
3.06e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 3.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 239835765 479 VEFQDVSFAYPNQPkvqVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLQNLYQPTGG 536
Cdd:PRK15064 320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
487-522 |
3.30e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 39.75 E-value: 3.30e-03
10 20 30
....*....|....*....|....*....|....*..
gi 239835765 487 AYP-NQPKVQVLQGLTFtlHPGtVTALVGPNGSGKST 522
Cdd:COG3910 19 AYPfNLPAVRNLEGLEF--HPP-VTFFVGENGSGKST 52
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
618-652 |
3.99e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 40.30 E-value: 3.99e-03
10 20 30
....*....|....*....|....*....|....*
gi 239835765 618 QLSGGQRQAVALARALIRKPLLLILDDATSALDAG 652
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
597-705 |
5.05e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 5.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 597 AHDFISGFPQ-------------GYdTEVGETGNQLSGGQRQAVALARALIRK---PLLLILDDATSAL--DAGNQLR-- 656
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfDDIKKLLev 874
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 239835765 657 VQRLlyespKRASRTVLLITQQLSLAEQAHHILFL------REGSVGEQGTHLQL 705
Cdd:TIGR00630 875 LQRL-----VDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
479-711 |
5.17e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.11 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 479 VEFQDVSFAYPnqpKVQVLQGLTFTLHPGTVTALVGPNGSGKSTVAALLqnlyqpTGGQLLLDGQCLV----QYDHHYLh 554
Cdd:NF033858 2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AGARKIQQGRVEVlggdMADARHR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 555 tqvAAVGQE----PLLFGR------SFRENIA-----YGLNRTPTMEEITAVAVESGAHDFISGfPQGydtevgetgnQL 619
Cdd:NF033858 72 ---RAVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAAERRRRIDELLRATGLAPFADR-PAG----------KL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 239835765 620 SGGQRQAVALARALIRKPLLLILDDATSALD--AGNQ---LrVQRLlyespkRASR---TVLLITQQLSLAEQAHHILFL 691
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRRQfweL-IDRI------RAERpgmSVLVATAYMEEAERFDWLVAM 210
|
250 260
....*....|....*....|
gi 239835765 692 REGSVGEQGTHLQLMKRGGC 711
Cdd:NF033858 211 DAGRVLATGTPAELLARTGA 230
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
501-521 |
8.38e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.53 E-value: 8.38e-03
|
| AAA_23 |
pfam13476 |
AAA domain; |
497-531 |
8.85e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 8.85e-03
10 20 30
....*....|....*....|....*....|....*.
gi 239835765 497 LQGLTFTLHPGtVTALVGPNGSGKST-VAALLQNLY 531
Cdd:pfam13476 9 FRDQTIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
|
|
| |
