|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
146-723 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 571.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 146 RLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGdSSVTHIMGIPsgtfyIGLLGLFFLGSACNFGRIIT 225
Cdd:COG1132 11 RLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG-GDLSALLLLL-----LLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 226 LRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLT 305
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 306 GYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFAS 385
Cdd:COG1132 165 LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 386 GIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKI 465
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 466 APTVGiPVPVTVGKAILSFRNVGFAYPtrPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG 545
Cdd:COG1132 325 PDPPG-AVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 546 VDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCS-FVLSFPEKWSTQVGTRGLQLSGGQ 624
Cdd:COG1132 402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHeFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFE 704
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*....
gi 19112543 705 RLSRPGTNFYKLMRWQLGK 723
Cdd:COG1132 560 ELLARGGLYARLYRLQFGE 578
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
139-716 |
8.31e-169 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 501.94 E-value: 8.31e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 139 NKKVNVFRLFTLARGQgWNFFIAG-SLLLVSSGVTMSIPYIVGKILDAgSSGDSsvthimGIPSGTFYIGLLGLFFLGSA 217
Cdd:TIGR00958 144 ETADLLFRLLGLSGRD-WPWLISAfVFLTLSSLGEMFIPFYTGRVIDT-LGGDK------GPPALASAIFFMCLLSIASS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 218 CNFG-RIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGM 296
Cdd:TIGR00958 216 VSAGlRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 297 MLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFV 376
Cdd:TIGR00958 296 MLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQ 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 377 LAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLF 456
Cdd:TIGR00958 376 LNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVF 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 457 ELLDAKPKIAPTVGIPVPVTVGKaiLSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAP 536
Cdd:TIGR00958 456 EYLDRKPNIPLTGTLAPLNLEGL--IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 537 SSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGT 615
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAhDFIMEFPNGYDTEVGE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 616 RGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEvmvdKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDG 695
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVERADQILVLKKG 689
|
570 580
....*....|....*....|.
gi 19112543 696 KVLEQGSFERLSRPGTNFYKL 716
Cdd:TIGR00958 690 SVVEMGTHKQLMEDQGCYKHL 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
156-721 |
1.79e-154 |
|
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: 460.32 E-value: 1.79e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 156 WNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSS--VTHIMgipsgTFYIGLLGLFFLGSACNFGRIITLrllSERI 233
Cdd:TIGR02204 18 GRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSglLNRYF-----AFLLVVALVLALGTAARFYLVTWL---GERV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 234 VSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDS----SIVGKSLSMylsdGLRSSVSAIAGIGMMLYVSMRLTGYMS 309
Cdd:TIGR02204 90 VADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTtllqSVIGSSLSM----ALRNALMCIGGLIMMFITSPKLTSLVL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 310 LIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFF 389
Cdd:TIGR02204 166 LAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 390 GSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAP-- 467
Cdd:TIGR02204 246 AIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKApa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 468 -TVGIPVPVTvgkAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGV 546
Cdd:TIGR02204 326 hPKTLPVPLR---GEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 547 DISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCS-FVLSFPEKWSTQVGTRGLQLSGGQK 625
Cdd:TIGR02204 403 DLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHeFISALPEGYDTYLGERGVTLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 626 QRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFER 705
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGR--TTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAE 560
|
570
....*....|....*.
gi 19112543 706 LSRPGTNFYKLMRWQL 721
Cdd:TIGR02204 561 LIAKGGLYARLARLQF 576
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
161-455 |
1.69e-146 |
|
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: 429.24 E-value: 1.69e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 161 AGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSvTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRAR 240
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGD-IEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 241 LFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAF 320
Cdd:cd18573 80 LFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 321 FYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATV 400
Cdd:cd18573 160 FYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 401 IAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18573 240 LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
136-721 |
9.93e-135 |
|
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: 413.85 E-value: 9.93e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 136 QTPNKKVNVFRLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIpsgtfyIGLLGLFFLG 215
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLA------IGLLLALLFE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 216 SACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTtDSSIVGKSLSMYLSDGLRSSVSAIAGIG 295
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLI 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 296 MMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLF 375
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 376 VLAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:COG2274 369 NARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERL 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 456 FELLDAKPKIAPTVGIPVPVTVGKAIlSFRNVGFAYPTRpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYA 535
Cdd:COG2274 449 DDILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 536 PSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVG 614
Cdd:COG2274 527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLhDFIEALPMGYDTVVG 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 615 TRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGD 694
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDK 684
|
570 580
....*....|....*....|....*..
gi 19112543 695 GKVLEQGSFERLSRPGTNFYKLMRWQL 721
Cdd:COG2274 685 GRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
145-706 |
7.71e-125 |
|
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: 383.68 E-value: 7.71e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 145 FRLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSG-DSSVthIMGIPsgtfyIGLLGLFFLGSACNFGRI 223
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGrDRSV--LWWVP-----LVVIGLAVLRGICSFVST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 224 ITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMR 303
Cdd:TIGR02203 76 YLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 304 LTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAF 383
Cdd:TIGR02203 156 LTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 384 ASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKP 463
Cdd:TIGR02203 236 AGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 464 KiAPTVGIPVPVTVGKaiLSFRNVGFAYPTRpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILA 543
Cdd:TIGR02203 316 E-KDTGTRAIERARGD--VEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 544 DGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGK-SNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLS 621
Cdd:TIGR02203 392 DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAqDFVDKLPLGLDTPIGENGVLLS 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 622 GGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQG 701
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
....*
gi 19112543 702 SFERL 706
Cdd:TIGR02203 550 THNEL 554
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
484-720 |
1.22e-117 |
|
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: 353.00 E-value: 1.22e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLV 563
Cdd:cd03249 3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 564 GQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIhDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 643 LDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRWQ 720
Cdd:cd03249 163 LDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
348-706 |
4.64e-102 |
|
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: 325.62 E-value: 4.64e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 348 LANVRTTQAFLGERQEVNRYNDYIRNlFVLAKREAFASgIFFGSTG--FLGNATVIAILALGGRMVAAGDITVGQL---S 422
Cdd:COG5265 225 LLNYETVKYFGNEAREARRYDEALAR-YERAAVKSQTS-LALLNFGqaLIIALGLTAMMLMAAQGVVAGTMTVGDFvlvN 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 423 SFL--LY-------TVYAggsivglsgcftDIMKGLGAASRLFELLDAKPKIAPTVGiPVPVTVGKAILSFRNVGFAY-P 492
Cdd:COG5265 303 AYLiqLYiplnflgFVYR------------EIRQALADMERMFDLLDQPPEVADAPD-APPLVVGGGEVRFENVSFGYdP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 493 TRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSG 572
Cdd:COG5265 370 ERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFND 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIAYGKSNASQEEIEDAAKRANCS-FVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALD 651
Cdd:COG5265 447 TIAYNIAYGRPDASEEEVEAAARAAQIHdFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 652 GEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERL 706
Cdd:COG5265 527 SRTERAIQAALREVARGR--TTLVIAHRLSTIVDADEILVLEAGRIVERGTHAEL 579
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
146-710 |
7.56e-100 |
|
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: 318.24 E-value: 7.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 146 RLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGipsgtFYIGLLGLFFLGSACNFGRIIT 225
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLP-----LLGLLLAVLLLRALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 226 LRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTdssivG-KSLSMYLSDGL-RSSVSAIAGIGMMLYVSM- 302
Cdd:COG4988 82 AFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTE-----GvEALDGYFARYLpQLFLAALVPLLILVAVFPl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 303 -RLTGYMSLI-VPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYN----DY-IRNLF 375
Cdd:COG4988 157 dWLSGLILLVtAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAeaseDFrKRTMK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 376 VLakREAFASGI---FFGSTGflgnatvIAILA--LGGRMVAaGDITVGQLSSFLLYT--VYAggSIVGLSGCFTDIMKG 448
Cdd:COG4988 237 VL--RVAFLSSAvleFFASLS-------IALVAvyIGFRLLG-GSLTLFAALFVLLLApeFFL--PLRDLGSFYHARANG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 449 LGAASRLFELLDAKPKIAPTVGIPVPVTVGKAIlSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQ 528
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSI-ELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 529 LLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPE 607
Cdd:COG4988 382 LLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLdEFVAALPD 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 608 KWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRAD 687
Cdd:COG4988 462 GLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQAD 539
|
570 580
....*....|....*....|...
gi 19112543 688 QIIVVGDGKVLEQGSFERLSRPG 710
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
482-716 |
1.27e-96 |
|
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: 298.38 E-value: 1.27e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAsIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG 561
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAF 640
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAhEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 641 LILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKL 716
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
227-718 |
3.68e-96 |
|
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: 309.00 E-value: 3.68e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 227 RLLSE----RIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTD----------------SSIVGkSLSMYLSDGLRS 286
Cdd:COG4987 76 RLVSHdatlRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADvdaldnlylrvllpllVALLV-ILAAVAFLAFFS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 287 SVSAIAGIGMMLyvsmrLTGymsLIVPPIALGAffygeyVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNR 366
Cdd:COG4987 155 PALALVLALGLL-----LAG---LLLPLLAARL------GRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALAR 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 367 YNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIM 446
Cdd:COG4987 221 LDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 447 KGLGAASRLFELLDAKPKIA-PTVGIPVPvtvGKAILSFRNVGFAYPTRPSAsIFDNLSFDIHPGTNVAIVAPSGGGKST 525
Cdd:COG4987 301 RVRAAARRLNELLDAPPAVTePAEPAPAP---GGPSLELEDVSFRYPGAGRP-VLDGLSLTLPPGERVAIVGPSGSGKST 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 526 ISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRAN-CSFVLS 604
Cdd:COG4987 377 LLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGlGDWLAA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 605 FPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIR 684
Cdd:COG4987 457 LPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLE 534
|
490 500 510
....*....|....*....|....*....|....
gi 19112543 685 RADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMR 718
Cdd:COG4987 535 RMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
482-720 |
1.69e-94 |
|
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: 292.98 E-value: 1.69e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAY-PTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:cd03253 1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPA 639
Cdd:cd03253 78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIhDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 640 FLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLmrW 719
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM--W 233
|
.
gi 19112543 720 Q 720
Cdd:cd03253 234 K 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
146-723 |
8.57e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 300.40 E-value: 8.57e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 146 RLFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAG-SSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRII 224
Cdd:PRK11176 15 RLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGfGKADRSVLKWMPL-------VVIGLMILRGITSFISSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 225 TLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRL 304
Cdd:PRK11176 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 305 TGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFA 384
Cdd:PRK11176 168 SLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 385 SGIFFGSTGFLGNATVIAILALGG-----RMVAAGDITVGQLSSFLLYTvyaggSIVGLSGCFTDIMKGLGAASRLFELL 459
Cdd:PRK11176 248 SSISDPIIQLIASLALAFVLYAASfpsvmDTLTAGTITVVFSSMIALMR-----PLKSLTNVNAQFQRGMAACQTLFAIL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 460 DAKPKiaPTVGIPVpVTVGKAILSFRNVGFAYPTRPSASIfDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSG 539
Cdd:PRK11176 323 DLEQE--KDEGKRV-IERAKGDIEFRNVTFTYPGKEVPAL-RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 540 KILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNA-SQEEIEDAAKRANCS-FVLSFPEKWSTQVGTRG 617
Cdd:PRK11176 399 EILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMdFINKMDNGLDTVIGENG 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 618 LQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKV 697
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEILVVEDGEI 556
|
570 580
....*....|....*....|....*.
gi 19112543 698 LEQGSFERLSRPGTNFYKLMRWQLGK 723
Cdd:PRK11176 557 VERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
285-720 |
9.51e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 287.24 E-value: 9.51e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 285 RSSVSAIAGIGMMLYVSMRLTGYMSLIVppIALGAFFY--GEYVRKLSRTTQDAL----GDL-TRVSEeKLANVRTTQAF 357
Cdd:PRK13657 135 REHLATLVALVVLLPLALFMNWRLSLVL--VVLGIVYTliTTLVMRKTKDGQAAVeehyHDLfAHVSD-AIGNVSVVQSY 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 358 LGERQEVNRYNDYIRNLF-----VLAkREAFASGIFFGSTGFlgnaTVIAILALGGRMVAAGDITVGQLSSFLLYTVYAG 432
Cdd:PRK13657 212 NRIEAETQALRDIADNLLaaqmpVLS-WWALASVLNRAASTI----TMLAILVLGAALVQKGQLRVGEVVAFVGFATLLI 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 433 GSIVGLSGCFTDIMKglgAASRL---FELLDAKPKIAPTVGIPVPVTVGKAIlSFRNVGFAYPTRPSAsiFDNLSFDIHP 509
Cdd:PRK13657 287 GRLDQVVAFINQVFM---AAPKLeefFEVEDAVPDVRDPPGAIDLGRVKGAV-EFDDVSFSYDNSRQG--VEDVSFEAKP 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 510 GTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEE 589
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 590 IEDAAKRANCS-FVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHN 668
Cdd:PRK13657 441 MRAAAERAQAHdFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKG 520
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 669 RsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRWQ 720
Cdd:PRK13657 521 R--TTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
484-706 |
1.02e-85 |
|
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: 269.87 E-value: 1.02e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAY-PTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGL 562
Cdd:cd03254 5 FENVNFSYdEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 563 VGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFL 641
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAhDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 642 ILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERL 706
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
164-455 |
2.48e-82 |
|
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: 263.27 E-value: 2.48e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 164 LLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHimgipSGTFYIgLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFA 243
Cdd:cd18557 4 FLLISSAAQLLLPYLIGRLIDTIIKGGDLDVL-----NELALI-LLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 244 KCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYG 323
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 324 EYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAI 403
Cdd:cd18557 158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 404 LALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18557 238 LWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
165-454 |
4.91e-80 |
|
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: 257.18 E-value: 4.91e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 165 LLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAK 244
Cdd:cd18780 5 LLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 245 CMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGE 324
Cdd:cd18780 85 IIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 325 YVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAIL 404
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 19112543 405 ALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASR 454
Cdd:cd18780 245 WYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVR 294
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
229-722 |
1.96e-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: 268.15 E-value: 1.96e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 229 LSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRL----TTDSSIVGKSLSMYLsDGLRSSVSaiagIGMMLYVSMRL 304
Cdd:TIGR01846 206 LTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVreleQIRNFLTGSALTVVL-DLLFVVVF----LAVMFFYSPTL 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 305 TGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYND----YIRNLFVLAKR 380
Cdd:TIGR01846 281 TGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRqlaaYVAASFRVTNL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 381 EAFASGIFfgstGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLD 460
Cdd:TIGR01846 361 GNIAGQAI----ELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 461 AKPKIAPTVGIPVPVTVGKaiLSFRNVGFAYptRP-SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSG 539
Cdd:TIGR01846 437 SPTEPRSAGLAALPELRGA--ITFENIRFRY--APdSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 540 KILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGL 618
Cdd:TIGR01846 513 QVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAhDFISELPQGYNTEVGEKGA 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEvmvdKTIQSLMHN--RSMTTITIAHKLATIRRADQIIVVGDGK 696
Cdd:TIGR01846 593 NLSGGQRQRIAIARALVGNPRILIFDEATSALDYESE----ALIMRNMREicRGRTVIIIAHRLSTVRACDRIIVLEKGQ 668
|
490 500
....*....|....*....|....*.
gi 19112543 697 VLEQGSFERLSRPGTNFYKLMRWQLG 722
Cdd:TIGR01846 669 IAESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
479-697 |
1.58e-77 |
|
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: 248.15 E-value: 1.58e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRS 558
Cdd:cd03248 9 KGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRN 637
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAhSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKV 697
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
482-696 |
3.66e-77 |
|
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: 244.99 E-value: 3.66e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAsIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG 561
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSGTIGENIaygksnasqeeiedaakrancsfvlsfpekwstqvgtrglqLSGGQKQRIAIARALLRNPAFL 641
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 642 ILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGK 696
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
161-455 |
8.38e-74 |
|
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: 240.85 E-value: 8.38e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 161 AGSLLLVSSGVTMSIPYIVGKILDAG-SSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSRLRA 239
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAAlGGGDTASLNQIAL-------LLLGLFLLQAVFSFFRIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 240 RLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGA 319
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 320 FFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNAT 399
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 400 VIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
164-720 |
1.24e-71 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 243.85 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 164 LLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIPSGTFYIGLL--GLFFLGSACNFGRiitlrllSERIVSRLRARL 241
Cdd:PRK10789 3 LLIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIAVVvyLLRYVWRVLLFGA-------SYQLAVELREDF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 242 FAKCMSLDGAFFDFHKHGDLISRLTTDSSIV----GKSLsMYLSDGLrssVSAIAGIGMM-LYVSMRLTGYMSLIVPPIA 316
Cdd:PRK10789 76 YRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaaGEGV-LTLVDSL---VMGCAVLIVMsTQISWQLTLLALLPMPVMA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYI-----RNLFVlAKREA-FASGIFFG 390
Cdd:PRK10789 152 IMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAedtgkKNMRV-ARIDArFDPTIYIA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 391 stgfLGNATVIAIlALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPTVg 470
Cdd:PRK10789 231 ----IGMANLLAI-GGGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGS- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 471 IPVPVTVGKAILSFRNvgFAYPTRpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIST 550
Cdd:PRK10789 305 EPVPEGRGELDVNIRQ--FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 551 YNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIA 629
Cdd:PRK10789 382 LQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVhDDILRLPQGYDTEVGERGVMLSGGQKQRIS 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEvmvdktiQSLMHN-----RSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFE 704
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTE-------HQILHNlrqwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD 534
|
570
....*....|....*...
gi 19112543 705 RLS-RPGtnFYKLM-RWQ 720
Cdd:PRK10789 535 QLAqQSG--WYRDMyRYQ 550
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
482-720 |
1.36e-70 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 230.45 E-value: 1.36e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYptRP-SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:cd03252 1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPA 639
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAhDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 640 FLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRW 719
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 19112543 720 Q 720
Cdd:cd03252 237 Q 237
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
138-721 |
1.54e-68 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 238.32 E-value: 1.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 138 PNKKVNVFRLFTLA-RGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILD-AGSSGDSSvtHIMGIpsgtfYIGLLGLFFLG 215
Cdd:TIGR03797 117 PDKALGLRDLLRFAlRGARRDLLAILAMGLLGTLLGMLVPIATGILIGtAIPDADRS--LLVQI-----ALALLAAAVGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 216 SACNFGR-IITLRLLSeRIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIvGKSLSMYLSDGLRSSVSAIAGI 294
Cdd:TIGR03797 190 AAFQLAQsLAVLRLET-RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQI-RRILSGSTLTTLLSGIFALLNL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 295 GMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANV---RTTQAflgerqEVnryndyi 371
Cdd:TIGR03797 268 GLMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGIsklRVAGA------EN------- 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 372 RNLFVLAKREAFASGIFFgSTGFLGNA-----------TVIAILALGGRMVAAGDITVGqlsSFLLYTVYAG---GSIVG 437
Cdd:TIGR03797 335 RAFARWAKLFSRQRKLEL-SAQRIENLltvfnavlpvlTSAALFAAAISLLGGAGLSLG---SFLAFNTAFGsfsGAVTQ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 438 LSGCFTDIMKGLGAASRLFELLDAKPKIAPTVGIPVPVTVGKAIlsfRNVGFAYptRPSAS-IFDNLSFDIHPGTNVAIV 516
Cdd:TIGR03797 411 LSNTLISILAVIPLWERAKPILEALPEVDEAKTDPGKLSGAIEV---DRVTFRY--RPDGPlILDDVSLQIEPGEFVAIV 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 517 APSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAyGKSNASQEEIEDAAKR 596
Cdd:TIGR03797 486 GPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWEAARM 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 597 ANCSF-VLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmhnrSMTTIT 675
Cdd:TIGR03797 565 AGLAEdIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIV 640
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 19112543 676 IAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRWQL 721
Cdd:TIGR03797 641 IAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQL 686
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
161-454 |
6.18e-68 |
|
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: 225.12 E-value: 6.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 161 AGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIpsgtfyIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRAR 240
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAV------LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 241 LFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAF 320
Cdd:cd18572 75 LFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 321 FYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATV 400
Cdd:cd18572 155 VYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQ 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19112543 401 IAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASR 454
Cdd:cd18572 235 VLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEK 288
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
482-702 |
1.25e-65 |
|
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: 216.59 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYptRP-SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:cd03244 3 IEFKNVSLRY--RPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSGTIGENIA-YGKsnASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNP 638
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLkEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 639 AFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
203-692 |
4.15e-65 |
|
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: 224.86 E-value: 4.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 203 TFYIGLLGLFFLGSAC-NFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSLSMYLS 281
Cdd:TIGR02857 44 LPALGALALVLLLRALlGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVE----ALDGYFA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 282 DGLRSSVSAIAGIGMMLYV----SMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAF 357
Cdd:TIGR02857 120 RYLPQLVLAVIVPLAILAAvfpqDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 358 LGERQEVNRYNDYIRNL-----FVLakREAFASGI---FFGSTGflgnatvIAILA--LGGRMVAaGDITV--GQLSSFL 425
Cdd:TIGR02857 200 GRAKAQAAAIRRSSEEYrertmRVL--RIAFLSSAvleLFATLS-------VALVAvyIGFRLLA-GDLDLatGLFVLLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 426 LYTVYAggSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPtVGIPVPVTVGKAIlSFRNVGFAYPTRPSAsiFDNLSF 505
Cdd:TIGR02857 270 APEFYL--PLRQLGAQYHARADGVAAAEALFAVLDAAPRPLA-GKAPVTAAPASSL-EFSGVSVAYPGRRPA--LRPVSF 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 506 DIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNA 585
Cdd:TIGR02857 344 TVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDA 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 586 SQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQS 664
Cdd:TIGR02857 424 SDAEIREALERAGLdEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRA 503
|
490 500
....*....|....*....|....*...
gi 19112543 665 LMHNRsmTTITIAHKLATIRRADQIIVV 692
Cdd:TIGR02857 504 LAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
161-455 |
7.91e-65 |
|
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: 216.97 E-value: 7.91e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 161 AGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVThimgipSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRAR 240
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTAL------LNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 241 LFAKCMSLDGAFFDFHKHGDLISRLTTDS----SIVGKSLSMylsdGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIA 316
Cdd:cd18575 75 VFAHLLRLSPSFFETTRTGEVLSRLTTDTtliqTVVGSSLSI----ALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLG 396
Cdd:cd18575 151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 397 NATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18575 231 FGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
484-701 |
3.24e-63 |
|
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: 210.14 E-value: 3.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAYPTRPSASIfDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLV 563
Cdd:cd03245 5 FRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 564 GQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCS-FVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:cd03245 84 PQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTdFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 643 LDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQG 701
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
327-712 |
5.80e-63 |
|
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: 220.00 E-value: 5.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 327 RKLSRTTQDALGDLTRVSEEKLANVRTTQAfLGERQEVNR-----YNDYIRNLFVLAKReafaSGIFFGSTGFLGNATVI 401
Cdd:COG4618 180 RKPLKEANEAAIRANAFAEAALRNAEVIEA-MGMLPALRRrwqraNARALALQARASDR----AGGFSALSKFLRLLLQS 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 402 AILALGGRMVAAGDITVGQL--SSFLLYTVYAggSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPTVGIPVPvtvgK 479
Cdd:COG4618 255 AVLGLGAYLVIQGEITPGAMiaASILMGRALA--PIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPLPRP----K 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPSAsIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSH 559
Cdd:COG4618 329 GRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 560 FGLVGQEPVLFSGTIGENIA-YGKSNAsqEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRN 637
Cdd:COG4618 408 IGYLPQDVELFDGTIAENIArFGDADP--EKVVAAAKLAGVhEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGD 485
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS----FERLSRPGTN 712
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPrdevLARLARPAAA 563
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-694 |
1.28e-56 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 209.89 E-value: 1.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 119 KDEQAQDISKINTNGTLQTP-------NKKvNVFRLFTLARGQGWNFFIA--------GSLLLVS------SGVTMsiPY 177
Cdd:PTZ00265 2 KKDQRQKKDNNSGGGNLSIKdevekelNKK-GTFELYKKIKTQKIPFFLPfkclpashRKLLGVSfvcatiSGGTL--PF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 178 IV---GKILDAGSSGDSsVTHIMgipsgtFYIGLLGLF-----FLGSACnfgriitLRLLSERIVSRLRARLFAKCMSLD 249
Cdd:PTZ00265 79 FVsvfGVIMKNMNLGEN-VNDII------FSLVLIGIFqfilsFISSFC-------MDVVTTKILKTLKLEFLKSVFYQD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 250 GAFFDFHKHGDLISRL-----TTDSSIVGKSLSMYlsdglrSSVSAIAGIGMM-LYVSMRLTGYMSLIVPPIALGAFFYG 323
Cdd:PTZ00265 145 GQFHDNNPGSKLTSDLdfyleQVNAGIGTKFITIF------TYASAFLGLYIWsLFKNARLTLCITCVFPLIYICGVICN 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 324 EYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYN-------DYI-RNLFVLAKREAFASGIFFGSTGF- 394
Cdd:PTZ00265 219 KKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNlseklysKYIlKANFMESLHIGMINGFILASYAFg 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 395 --LGNATVIAILA--------LGGRMVAagdITVGQLSSFLLYTVYAGGsivglsgcFTDIMKGLGAASRLFELLDAKPK 464
Cdd:PTZ00265 299 fwYGTRIIISDLSnqqpnndfHGGSVIS---ILLGVLISMFMLTIILPN--------ITEYMKSLEATNSLYEIINRKPL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 465 IAPTVGIPVPVTVGKaiLSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILA- 543
Cdd:PTZ00265 368 VENNDDGKKLKDIKK--IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIn 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 544 DGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYG----------------KSNASQEEIEDA-AKRANCS------ 600
Cdd:PTZ00265 446 DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQENKNKRnSCRAKCAgdlndm 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 601 -----------------------------------FVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDE 645
Cdd:PTZ00265 526 snttdsneliemrknyqtikdsevvdvskkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDE 605
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 19112543 646 ATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGD 694
Cdd:PTZ00265 606 ATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
501-718 |
1.40e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 200.07 E-value: 1.40e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFyAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAY 580
Cdd:PRK11174 367 GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 581 GKSNASQEEIEDAAKRANCS-FVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVD 659
Cdd:PRK11174 446 GNPDASDEQLQQALENAWVSeFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 660 KTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMR 718
Cdd:PRK11174 526 QALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
158-455 |
1.79e-55 |
|
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: 191.49 E-value: 1.79e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHImgipsgtfyIGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLL---------ALLVALFLLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIAL 317
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 318 GAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGN 397
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 398 ATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18551 232 LALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
227-680 |
3.70e-55 |
|
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: 197.97 E-value: 3.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 227 RLLSE----RIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSV---SAIAGI----- 294
Cdd:TIGR02868 74 RLVGHdaalRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVvgaAAVAAIavlsv 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 295 --GMMLYVSMRLTGymsLIVPPIALGAffygeyVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIR 372
Cdd:TIGR02868 154 paALILAAGLLLAG---FVAPLVSLRA------ARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADR 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 373 NLFVLAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAA 452
Cdd:TIGR02868 225 ELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 453 SRLFELLDAKPKIA-PTVGIPVPVTVGKAILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLL 531
Cdd:TIGR02868 305 ERIVEVLDAAGPVAeGSAPAAGAVGLGKPTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLA 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 532 RFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWS 610
Cdd:TIGR02868 383 GLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLaDWLRALPDGLD 462
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 611 TQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKL 680
Cdd:TIGR02868 463 TVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
158-455 |
5.48e-55 |
|
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: 190.45 E-value: 5.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILD-AGSSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSR 236
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDdVIPAGDLSLLLWIAL-------LLLLLALLRALLSYLRRYLAARLGQRVVFD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIA 316
Cdd:cd07346 74 LRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLG 396
Cdd:cd07346 154 LILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 397 NATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd07346 234 ALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
229-715 |
5.94e-55 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 204.88 E-value: 5.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 229 LSERIVSRLRARLFAKCMSLDGAFFDFHKH--GDLISRLTTDSSIvgkslsmyLSDGLRSSVSAIAGIGMMLYVSMRLTG 306
Cdd:PTZ00265 893 IGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHL--------LKTGLVNNIVIFTHFIVLFLVSMVMSF 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 307 YMSLIVPPIALGAFFYGEYVRKLsRTTQDALGDLtrvsEEKLANVRTTQAFLGERQEVNR----------YN-------- 368
Cdd:PTZ00265 965 YFCPIVAAVLTGTYFIFMRVFAI-RARLTANKDV----EKKEINQPGTVFAYNSDDEIFKdpsfliqeafYNmntviiyg 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 369 --DYIRNLFVLA--------KREAFASGIFFG---STGFLGNATViaiLALGGRMVAAGDITVG----QLSSFLLYTVYA 431
Cdd:PTZ00265 1040 leDYFCNLIEKAidysnkgqKRKTLVNSMLWGfsqSAQLFINSFA---YWFGSFLIRRGTILVDdfmkSLFTFLFTGSYA 1116
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 432 GgSIVGLSGcftDIMKGLGAASRLFELLDAKPKI--APTVGIPVPVT-VGKAILSFRNVGFAYPTRPSASIFDNLSFDIH 508
Cdd:PTZ00265 1117 G-KLMSLKG---DSENAKLSFEKYYPLIIRKSNIdvRDNGGIRIKNKnDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCD 1192
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 509 PGTNVAIVAPSGGGKSTISQLLLRFYA----------------------------------------------------- 535
Cdd:PTZ00265 1193 SKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstv 1272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 536 -PSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQV 613
Cdd:PTZ00265 1273 fKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIdEFIESLPNKYDTNV 1352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 614 GTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVG 693
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
570 580
....*....|....*....|....*..
gi 19112543 694 DGK-----VLEQGSFERLSRPGTNFYK 715
Cdd:PTZ00265 1433 NPDrtgsfVQAHGTHEELLSVQDGVYK 1459
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
482-697 |
1.19e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 183.86 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG 561
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSGTIGENIA----YGKSNASQEEIEDAAKRancsfvLSFPE---KWSTQvgtrglQLSGGQKQRIAIARAL 634
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPfpfqLRERKFDRERALELLER------LGLPPdilDKPVE------RLSGGERQRLALIRAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 635 LRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:COG4619 146 LLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
327-701 |
1.94e-53 |
|
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: 193.33 E-value: 1.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 327 RKLSRTTQdALGDLTRVSEEKLANVRTTQAfLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGS-TGFLGNATVIAILA 405
Cdd:TIGR01842 167 KPLKEATE-ASIRANNLADSALRNAEVIEA-MGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNlSKYFRIVLQSLVLG 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 406 LGGRMVAAGDITVGQL--SSFLLYTvyAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPTVGIPVPvtvgKAILS 483
Cdd:TIGR01842 245 LGAYLAIDGEITPGMMiaGSILVGR--ALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPEP----EGHLS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAyPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLV 563
Cdd:TIGR01842 319 VENVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 564 GQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:TIGR01842 398 PQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVhELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVV 477
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 643 LDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQG 701
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
158-455 |
7.81e-53 |
|
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: 184.55 E-value: 7.81e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVThIMGIPsgtfyIGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEA-LLLVP-----LAIIGLFLLRGLASYLQTYLMAYVGQRVVRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIAL 317
Cdd:cd18552 75 RNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 318 GAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGN 397
Cdd:cd18552 155 PIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 398 ATVIAILALGGRMVAAGDITVGQLSSFL--LYTVYAggSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18552 235 IAIALVLWYGGYQVISGELTPGEFISFItaLLLLYQ--PIKRLSNVNANLQRGLAAAERI 292
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
190-716 |
1.43e-52 |
|
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: 194.19 E-value: 1.43e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 190 DSSVTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDS 269
Cdd:TIGR01193 184 DTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDAS 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 270 SIVGKSLSMYLSDGLRSSVSAIAGIgMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLA 349
Cdd:TIGR01193 264 SIIDALASTILSLFLDMWILVIVGL-FLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLN 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 350 NVRTTQAFLGERQEVN----RYNDYIRNLFVLAKREAFASGIFFGSTGFLgnatVIAILALGGRMVAAGDITVGQLSSFL 425
Cdd:TIGR01193 343 GIETIKSLTSEAERYSkidsEFGDYLNKSFKYQKADQGQQAIKAVTKLIL----NVVILWTGAYLVMRGKLTLGQLITFN 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 426 LYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKIAPTVGIPVPVTVGKAIlSFRNVGFAYPTrpSASIFDNLSF 505
Cdd:TIGR01193 419 ALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDI-VINDVSYSYGY--GSNILSDISL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 506 DIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYG-KSN 584
Cdd:TIGR01193 496 TIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKEN 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 585 ASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEvmvDKTIQ 663
Cdd:TIGR01193 576 VSQDEIWAACEIAEIkDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVN 652
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 664 SLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKL 716
Cdd:TIGR01193 653 NLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
382-718 |
1.52e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 188.50 E-value: 1.52e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 382 AFASGIFFGSTGFlgnaTVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDA 461
Cdd:PRK11160 245 GLSQALMILANGL----TVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEALMPVAGAFQHLGQVIASARRINEITEQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 462 KPKIA-PTVGIPVPvtvGKAILSFRNVGFAYPTRPSaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGK 540
Cdd:PRK11160 321 KPEVTfPTTSTAAA---DQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 541 ILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCSFVLSFPEKWSTQVGTRGLQL 620
Cdd:PRK11160 397 ILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQL 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 621 SGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQ 700
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQFDRICVMDNGQIIEQ 554
|
330
....*....|....*...
gi 19112543 701 GSFERLSRPGTNFYKLMR 718
Cdd:PRK11160 555 GTHQELLAQQGRYYQLKQ 572
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
482-697 |
5.54e-51 |
|
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: 175.10 E-value: 5.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG 561
Cdd:cd03246 1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSGTIGENIaygksnasqeeiedaakrancsfvlsfpekwstqvgtrglqLSGGQKQRIAIARALLRNPAFL 641
Cdd:cd03246 80 YLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 642 ILDEATSALDGEAEVMVDKTIQSlMHNRSMTTITIAHKLATIRRADQIIVVGDGKV 697
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
175-454 |
3.96e-50 |
|
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: 177.35 E-value: 3.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 175 IPYIVGKILDagssgdsSVTHIMGIPSGTFY-------IGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMS 247
Cdd:cd18574 15 IPLLLGDLVN-------VISRSLKETNGDFIedlkkpaLKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 248 LDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVR 327
Cdd:cd18574 88 QDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 328 KLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILALG 407
Cdd:cd18574 168 KLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 19112543 408 GRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASR 454
Cdd:cd18574 248 GSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGAR 294
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
482-702 |
1.84e-49 |
|
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: 173.29 E-value: 1.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG 561
Cdd:COG1122 1 IELENLSFSYPGGTPA--LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPV--LFSGTIGENIAYGKSNA--SQEEIEDAAKRAncsfvLSfpekwstQVGTRGL------QLSGGQKQRIAIA 631
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENLglPREEIRERVEEA-----LE-------LVGLEHLadrpphELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 632 RALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDprGRRELL--ELLKRL-NKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
158-430 |
3.82e-48 |
|
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: 170.90 E-value: 3.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIpsgtFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNV----YSLALLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIAL 317
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 318 GAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGN 397
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|...
gi 19112543 398 ATVIAILALGGRMVAAGDITVGQLSSFLLYTVY 430
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDLVAFLSLFAQ 269
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
457-702 |
1.94e-47 |
|
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: 175.86 E-value: 1.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 457 ELLDAKPKIAPTVGIPVPVTV-GKAILSFRNVGFAYPTRPSASIF--DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRF 533
Cdd:COG1123 235 QALAAVPRLGAARGRAAPAAAaAEPLLEVRNLSKRYPVRGKGGVRavDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 534 YAPSSGKILADGVDISTYN---VHQWRSHFGLVGQEPV--LFSG-TIGENIAYGKSN---ASQEEIEDAAKRAncsfvLS 604
Cdd:COG1123 315 LRPTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYssLNPRmTVGDIIAEPLRLhglLSRAERRERVAEL-----LE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 605 fpekwstQVG-TRGL------QLSGGQKQRIAIARALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTIT 675
Cdd:COG1123 390 -------RVGlPPDLadryphELSGGQRQRVAIARALALEPKLLILDEPTSALDvsVQAQIL--NLLRDLQRELGLTYLF 460
|
250 260
....*....|....*....|....*...
gi 19112543 676 IAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:COG1123 461 ISHDLAVVRYiADRVAVMYDGRIVEDGP 488
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
483-696 |
2.76e-47 |
|
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: 166.49 E-value: 2.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 483 SFRNVGFAYPTRPSAsIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGL 562
Cdd:cd03225 1 ELKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 563 VGQEP--VLFSGTIGENIAYGKSNA--SQEEIEDAAKRANCSFVLSFPEKWSTQvgtrglQLSGGQKQRIAIARALLRNP 638
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLglPEEEIEERVEEALELVGLEGLRDRSPF------TLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 639 AFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
206-725 |
1.43e-46 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 174.91 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 206 IGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLR 285
Cdd:PRK10790 69 AAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 286 SsvsaIAGIGMMLYVSMRLTGYMSL----IVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAF---- 357
Cdd:PRK10790 149 S----AALIGAMLVAMFSLDWRMALvaimIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFrqqa 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 358 -LGERQEVNRYNDYirnlfvLAKREAFA-SGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSI 435
Cdd:PRK10790 225 rFGERMGEASRSHY------MARMQTLRlDGFLLRPLLSLFSALILCGLLMLFGFSASGTIEVGVLYAFISYLGRLNEPL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 436 VGLSGCFTDIMKGLGAASRLFELLDAkPKiaPTVGIPV-PVTVGKaiLSFRNVGFAYptRPSASIFDNLSFDIHPGTNVA 514
Cdd:PRK10790 299 IELTTQQSMLQQAVVAGERVFELMDG-PR--QQYGNDDrPLQSGR--IDIDNVSFAY--RDDNLVLQNINLSVPSRGFVA 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 515 IVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAYGKsNASQEEIEDAA 594
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQAL 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 595 KRAN-CSFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmhnRSMTT 673
Cdd:PRK10790 451 ETVQlAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV---REHTT 527
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 674 -ITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLMRWQLGKVE 725
Cdd:PRK10790 528 lVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
158-428 |
3.30e-46 |
|
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: 166.07 E-value: 3.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAG-SSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSR 236
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSViGGGLRELLWLLAL-------LILGVALLRGVFRYLQGYLAEKASQKVAYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIA 316
Cdd:cd18542 74 LRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLG 396
Cdd:cd18542 154 LFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLS 233
|
250 260 270
....*....|....*....|....*....|..
gi 19112543 397 NATVIAILALGGRMVAAGDITVGQLSSFLLYT 428
Cdd:cd18542 234 GLQIVLVLWVGGYLVINGEITLGELVAFISYL 265
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
481-701 |
9.96e-45 |
|
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: 159.98 E-value: 9.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAS-IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQ---W 556
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RSHFGLVGQE------PVLfsgTIGENIAYG----KSNASQEEIEDAAKRANCSFVLsfPEKWSTQvgtRGLQLSGGQKQ 626
Cdd:cd03257 81 RKEIQMVFQDpmsslnPRM---TIGEQIAEPlrihGKLSKKEARKEAVLLLLVGVGL--PEEVLNR---YPHELSGGQRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 627 RIAIARALLRNPAFLILDEATSALDgeaeVMVDKTIQSLMHN----RSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALD----VSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
498-702 |
7.77e-44 |
|
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: 156.80 E-value: 7.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 498 SIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGEN 577
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 I-AYGKSnaSQEEIEDAAKrancsfvlsfpekwstqVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEV 656
Cdd:cd03369 102 LdPFDEY--SDEEIYGALR-----------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19112543 657 MVDKTIQSLMHNrsMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:cd03369 163 LIQKTIREEFTN--STILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
482-702 |
2.87e-43 |
|
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: 157.21 E-value: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYP--TRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIST-YNVHQWRS 558
Cdd:TIGR04520 1 IEVENVSFSYPesEKP---ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEP--VLFSGTIGENIAYGKSNA--SQEEIEDAAKRAncsfvlsfpekwSTQVGTRGL------QLSGGQKQRI 628
Cdd:TIGR04520 78 KVGMVFQNPdnQFVGATVEDDVAFGLENLgvPREEMRKRVDEA------------LKLVGMEDFrdrephLLSGGQKQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 629 AIARALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDpkGRKEVL--ETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
158-427 |
3.67e-43 |
|
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: 157.96 E-value: 3.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMgipsgTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLL-----RYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLS---MYLSDGLrssVSAIAGIGMMLYVSMRLTGYMSLIVPP 314
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGpgiLYLVDAL---FLGVLVLVMMFTISPKLTLIALLPLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 315 IALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGF 394
Cdd:cd18541 153 LALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGL 232
|
250 260 270
....*....|....*....|....*....|...
gi 19112543 395 LGNATVIAILALGGRMVAAGDITVGQLSSFLLY 427
Cdd:cd18541 233 LIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
482-701 |
4.29e-43 |
|
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: 153.62 E-value: 4.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNvHQWRSHFG 561
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSGTIGENIaygksnasqeeiedaakrancsfvlsfpekwstqvgtrGLQLSGGQKQRIAIARALLRNPAFL 641
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 642 ILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQG 701
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
478-706 |
7.12e-43 |
|
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: 155.14 E-value: 7.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 478 GKAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW- 556
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELy 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 --RSHFGLVGQEPVLFSG-TIGENIAYG---KSNASQEEIEDAAKrancsFVLSfpekwstQVGTRGL------QLSGGQ 624
Cdd:COG1127 79 elRRRIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVL-----EKLE-------LVGLPGAadkmpsELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSF 703
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226
|
...
gi 19112543 704 ERL 706
Cdd:COG1127 227 EEL 229
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
158-454 |
9.54e-43 |
|
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: 156.79 E-value: 9.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIPSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIAL 317
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 318 GAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGN 397
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 398 ATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASR 454
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
159-455 |
2.11e-42 |
|
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: 155.71 E-value: 2.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 159 FIAGSLLLVSSGVTMSIPYIV-GKILDA---GSSGDSSVTHIMGIpSGTFYIGLLGLFFLGSACNFGRIITLRLLSERIV 234
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVfGDLFDAftdFGSGESSPDEFLDD-VNKYALYFVYLGIGSFVLSYIQTACWTITGERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 235 SRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPP 314
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 315 IALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGF 394
Cdd:cd18577 160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFF 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 395 LGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18577 240 IIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
165-455 |
5.37e-42 |
|
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: 154.39 E-value: 5.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 165 LLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMGIpsgtFYIGLLGlfFLGSACNFGRIITLRLLSERIVSRLRARLFAK 244
Cdd:cd18784 5 LLAAAVGEIFIPYYTGQVIDGIVIEKSQDKFSRAI----IIMGLLA--IASSVAAGIRGGLFTLAMARLNIRIRNLLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 245 CMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGE 324
Cdd:cd18784 79 IVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 325 YVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAIL 404
Cdd:cd18784 159 YYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 19112543 405 ALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18784 239 YYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
482-706 |
3.71e-41 |
|
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: 150.34 E-value: 3.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW---RS 558
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSG-TIGENIAYG---KSNASQEEIEDAAKrancsFVLSFpekwstqVGTRGL------QLSGGQKQRI 628
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVL-----EKLEA-------VGLRGAedlypaELSGGMKKRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 629 AIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:cd03261 146 ALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
500-648 |
6.84e-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: 146.64 E-value: 6.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 500 FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSG-TIGENI 578
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 579 AYG------KSNASQEEIEDAAKRancsfvLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATS 648
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEK------LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
479-702 |
1.26e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 150.14 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRS 558
Cdd:PRK13632 5 SVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEP-VLFSG-TIGENIAYGKSNAS------QEEIEDAAKRANCSFVLSF-PEKwstqvgtrglqLSGGQKQRIA 629
Cdd:PRK13632 84 KIGIIFQNPdNQFIGaTVEDDIAFGLENKKvppkkmKDIIDDLAKKVGMEDYLDKePQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
479-706 |
1.39e-40 |
|
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: 156.22 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPSASIfDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPS---SGKILADGVDISTYNVHQ 555
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQEP--VLFSGTIGENIAYGKSN--ASQEEIEDAAKRAncsfvlsfpekwSTQVGTRGL------QLSGGQK 625
Cdd:COG1123 81 RGRRIGMVFQDPmtQLNPVTVGDQIAEALENlgLSRAEARARVLEL------------LEAVGLERRldryphQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 626 QRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATI-RRADQIIVVGDGKVLEQGSFE 704
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPE 228
|
..
gi 19112543 705 RL 706
Cdd:COG1123 229 EI 230
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
482-706 |
3.88e-40 |
|
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: 147.33 E-value: 3.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFY-----APSSGKILADGVDIST--YNVH 554
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDldVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 555 QWRSHFGLVGQEPVLFSGTIGENIAYG------KSNASQEEI-EDAAKRAncsfvlsfpEKWsTQVGTR--GLQLSGGQK 625
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKA---------ALW-DEVKDRlhALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 626 QRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmhNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFE 704
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTE 225
|
..
gi 19112543 705 RL 706
Cdd:cd03260 226 QI 227
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
481-702 |
1.25e-38 |
|
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: 143.65 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVL-FSGTIGENIAYGK-------SNASQEEiEDAAKRAncsfvLSfpekwstQVGTRGL------QLSGGQKQ 626
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRyphlglfGRPSAED-REAVEEA-----LE-------RTGLEHLadrpvdELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 627 RIAIARALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAH--KLAtIRRADQIIVVGDGKVLEQGS 702
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLARERGRTVVMVLHdlNLA-ARYADRLVLLKDGRIVAQGP 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
251-718 |
1.69e-38 |
|
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: 154.33 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 251 AFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGigmmLYVSMRLTGYMSLIVPPIALGAF----FYGEYV 326
Cdd:TIGR00957 1054 SFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGA----LIVILLATPIAAVIIPPLGLLYFfvqrFYVASS 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 327 RKLSRTTQDALGDLTRVSEEKLANVRTTQAFlgERQEvnRYnDYIRNLFVLAKREAFASGIFFG-----STGFLGNATVI 401
Cdd:TIGR00957 1130 RQLKRLESVSRSPVYSHFNETLLGVSVIRAF--EEQE--RF-IHQSDLKVDENQKAYYPSIVANrwlavRLECVGNCIVL 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 402 --AILALGGR-MVAAGdiTVGQLSSFLLYTVYAGGSIVGLSgcfTDIMKGLGAASRLFELLDAKPK-------IAPTVGI 471
Cdd:TIGR00957 1205 faALFAVISRhSLSAG--LVGLSVSYSLQVTFYLNWLVRMS---SEMETNIVAVERLKEYSETEKEapwqiqeTAPPSGW 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 472 PvpvTVGKaiLSFRNVGFAYptRPSAS-IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIST 550
Cdd:TIGR00957 1280 P---PRGR--VEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK 1352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 551 YNVHQWRSHFGLVGQEPVLFSGTIGENIAyGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIA 629
Cdd:TIGR00957 1353 IGLHDLRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLkTFVSALPDKLDHECAEGGENLSVGQRQLVC 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNrsMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRP 709
Cdd:TIGR00957 1432 LARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
....*....
gi 19112543 710 GTNFYKLMR 718
Cdd:TIGR00957 1510 RGIFYSMAK 1518
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
479-700 |
5.49e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.95 E-value: 5.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPSA-SIFDNLSFDIHPGTNVAIVAPSGGGKST----ISqLLLRfyaPSSGKILADGVDISTYNV 553
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllniLG-GLDR---PTSGEVLIDGQDISSLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 HQW----RSHFGLVGQEPVLFSG-TIGENIAY-----GKSNAsqeeieDAAKRAncsfvlsfpEKWSTQVGTRGL----- 618
Cdd:COG1136 78 RELarlrRRHIGFVFQFFNLLPElTALENVALplllaGVSRK------ERRERA---------RELLERVGLGDRldhrp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 -QLSGGQKQRIAIARALLRNPAFLILDEATSALDGE--AEVMvdKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDG 695
Cdd:COG1136 143 sQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKtgEEVL--ELLRELNRELGTTIVMVTHDPELAARADRVIRLRDG 220
|
....*
gi 19112543 696 KVLEQ 700
Cdd:COG1136 221 RIVSD 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
479-711 |
6.54e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.46 E-value: 6.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYP--TRPSasiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW 556
Cdd:PRK13635 3 EEIIRVEHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RSHFGLVGQEP-VLFSG-TIGENIAYGKSNAS------QEEIEDAAKRANC-SFVLSFPEKwstqvgtrglqLSGGQKQR 627
Cdd:PRK13635 80 RRQVGMVFQNPdNQFVGaTVQDDVAFGLENIGvpreemVERVDQALRQVGMeDFLNREPHR-----------LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 628 IAIARALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFER 705
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDprGRREVL--ETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
....*.
gi 19112543 706 LSRPGT 711
Cdd:PRK13635 227 IFKSGH 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
483-696 |
6.83e-38 |
|
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: 138.53 E-value: 6.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 483 SFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGL 562
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 563 VgqepvlfsgtigeniaygksnasqeeiedaakrancsfvlsfpekwstqvgtrgLQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:cd00267 78 V------------------------------------------------------PQLSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 643 LDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRRA-DQIIVVGDGK 696
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
158-428 |
1.49e-37 |
|
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: 142.14 E-value: 1.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILD---AGSSGDSSVTHIMGIpsgtFYIGLLglfFLGSACNFGRIITLRLLSERIV 234
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyiVPGQGDLQGLLLLAL----LYLGLL---LLSFLLQYLQTYLLQKLGQRII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 235 SRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSLSMYLSDGLRSSVSA---IAGI-GMMLYVSMRLTGYMSL 310
Cdd:cd18544 74 YDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE----ALNELFTSGLVTLIGDlllLIGIlIAMFLLNWRLALISLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 311 IVPPIALGAFFYGEYVRKLSRTTQDALGDL-TRVSEEkLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFF 389
Cdd:cd18544 150 VLPLLLLATYLFRKKSRKAYREVREKLSRLnAFLQES-ISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFR 228
|
250 260 270
....*....|....*....|....*....|....*....
gi 19112543 390 GSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYT 428
Cdd:cd18544 229 PLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYI 267
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
482-701 |
3.72e-37 |
|
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: 138.42 E-value: 3.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPtrpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHqwRSHFG 561
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENIAYG--KSNASQEEIEDAAKRANCSFVLSFPEKwstqvgTRGLQLSGGQKQRIAIARALLRNP 638
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLN------RYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 639 AFLILDEATSALDGE-AEVMVDKtIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQG 701
Cdd:cd03259 150 SLLLLDEPLSALDAKlREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
450-709 |
5.12e-37 |
|
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: 145.98 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 450 GAASRLFE---------LLDAKPKIAPtvgIPVPVTvGKAILSFRNVGFAYPTRpsASIF----------DNLSFDIHPG 510
Cdd:COG4172 239 GPTAELFAapqhpytrkLLAAEPRGDP---RPVPPD-APPLLEARDLKVWFPIK--RGLFrrtvghvkavDGVSLTLRRG 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 511 TNVAIVAPSGGGKSTISQLLLRFyAPSSGKILADGVDISTYNVHQ---WRSHFGLVGQEPvlFSG-----TIGENIAYG- 581
Cdd:COG4172 313 ETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDP--FGSlsprmTVGQIIAEGl 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 582 ---KSNASQEEIEDAAKRAncsfvLsfpekwsTQVGtrgL----------QLSGGQKQRIAIARALLRNPAFLILDEATS 648
Cdd:COG4172 390 rvhGPGLSAAERRARVAEA-----L-------EEVG---LdpaarhryphEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 649 ALDgeaeVMVDKTI----QSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFER-LSRP 709
Cdd:COG4172 455 ALD----VSVQAQIldllRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQvFDAP 517
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
164-427 |
6.02e-37 |
|
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: 140.32 E-value: 6.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 164 LLLVSSGVTMSIPYIVGKILDAG-SSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLF 242
Cdd:cd18546 7 LVVVDTAASLAGPLLVRYGIDSGvRAGDLGVLLLAAA-------AYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 243 AKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSLSMYLSDGLRSSVSAI---AGI-GMMLYVSMRLTGYMSLIVPPIALG 318
Cdd:cd18546 80 AHLQRLSLDFHERETSGRIMTRMTSDID----ALSELLQTGLVQLVVSLltlVGIaVVLLVLDPRLALVALAALPPLALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 319 AFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNA 398
Cdd:cd18546 156 TRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNL 235
|
250 260
....*....|....*....|....*....
gi 19112543 399 TVIAILALGGRMVAAGDITVGQLSSFLLY 427
Cdd:cd18546 236 ATAAVLLVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
482-714 |
7.28e-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: 138.78 E-value: 7.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAS-IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPvlFS-----GTIGENIA-----YGKSNAsQEEIEDAAKRAN--CSFVLSFPEkwstqvgtrglQLSGGQKQRI 628
Cdd:COG1124 82 QMVFQDP--YAslhprHTVDRILAeplriHGLPDR-EERIAELLEQVGlpPSFLDRYPH-----------QLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 629 AIARALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFER 705
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDvsVQAEIL--NLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
....*....
gi 19112543 706 LSRPGTNFY 714
Cdd:COG1124 226 LLAGPKHPY 234
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
156-465 |
1.70e-36 |
|
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: 139.51 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 156 WNFFIAGSLLLVSSGVTMSI-PYIVGKILDA-GSSGDSSVTHimgipSGTFYIGL-LGLFFLGSACNFGRIITLRLLSER 232
Cdd:cd18578 8 WPLLLLGLIGAIIAGAVFPVfAILFSKLISVfSLPDDDELRS-----EANFWALMfLVLAIVAGIAYFLQGYLFGIAGER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 233 IVSRLRARLFAKCMSLDGAFFDFHKH--GDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSL 310
Cdd:cd18578 83 LTRRLRKLAFRAILRQDIAWFDDPENstGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 311 IVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFG 390
Cdd:cd18578 163 TVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFG 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 391 STGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRLFELLDAKPKI 465
Cdd:cd18578 243 LSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
485-701 |
1.08e-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: 132.94 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 485 RNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVG 564
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 565 QepVLfsgtigeniaygksnaSQEEIEDAAKRancsfvlSFPEkwstqvgtrglqLSGGQKQRIAIARALLRNPAFLILD 644
Cdd:cd03214 80 Q--AL----------------ELLGLAHLADR-------PFNE------------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 645 EATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQG 701
Cdd:cd03214 123 EPTSHLDiaHQIELL--ELLRRLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
158-427 |
1.39e-35 |
|
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: 136.51 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHImgipsGTFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLL-----LGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSLSMYLSDGLRSSVSA---IAGIG-MMLYVSMRLTGYMSLIVP 313
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVA----NVERLIADGIPQGITNvltLVGVAiILFSINPKLALLTLIPIP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 314 PIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTG 393
Cdd:cd18778 152 FLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLME 231
|
250 260 270
....*....|....*....|....*....|....
gi 19112543 394 FLGNATVIAILALGGRMVAAGDITVGQLSSFLLY 427
Cdd:cd18778 232 FLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
499-696 |
1.52e-35 |
|
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: 132.31 E-value: 1.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN--VHQWRSHFGLVGQEPVLFSG-TIG 575
Cdd:cd03229 15 VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 576 ENIAYGksnasqeeiedaakrancsfvlsfpekwstqvgtrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAE 655
Cdd:cd03229 95 ENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19112543 656 VMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:cd03229 137 REVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
481-710 |
2.01e-35 |
|
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: 133.86 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSASI-FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN---VHQW 556
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTaLKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RSHFGLVGQEPVLFSG-TIGENIAY-----GKSNASQEE----------IEDAAKrancsfvlSFPEkwstqvgtrglQL 620
Cdd:cd03258 81 RRRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIEErvlellelvgLEDKAD--------AYPA-----------QL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 621 SGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLE 699
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221
|
250
....*....|..
gi 19112543 700 QGS-FERLSRPG 710
Cdd:cd03258 222 EGTvEEVFANPQ 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
482-706 |
2.53e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 133.73 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasifdnLSFD--IHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRSh 559
Cdd:COG3840 2 LRLDDLTYRYGDFP-------LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 560 FGLVGQEPVLFSG-TIGENIAYG-----KSNASQ-EEIEDAAKRancsfvlsfpekwstqVGTRGL------QLSGGQKQ 626
Cdd:COG3840 73 VSMLFQENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALER----------------VGLAGLldrlpgQLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 627 RIAIARALLRNPAFLILDEATSALD----GEaevMVDkTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDpalrQE---MLD-LVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212
|
....*
gi 19112543 702 SFERL 706
Cdd:COG3840 213 PTAAL 217
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
158-427 |
2.89e-35 |
|
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: 135.29 E-value: 2.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAG-SSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSR 236
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYiPNGDLSGLLIIAL-------LFLALNLVNWVASRLRIYLMAKVGQRILYD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSLSMYLSDGLRSSVS---AIAGI-GMMLYVSMRLTGYMSLIV 312
Cdd:cd18545 75 LRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVN----SLSDLLSNGLINLIPdllTLVGIvIIMFSLNVRLALVTLAVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 313 PPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFlgERQEVN-----RYNDYIRNLFVLAkreAFASGI 387
Cdd:cd18545 151 PLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSF--AREDENeeifdELNRENRKANMRA---VRLNAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 19112543 388 FFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLY 427
Cdd:cd18545 226 FWPLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGY 265
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
482-696 |
5.71e-35 |
|
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: 131.82 E-value: 5.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAS--IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKIladgvdistynvhQWRSH 559
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 560 FGLVGQEPVLFSGTIGENIAYGKSnASQEEIEDAAKraNCSFVL---SFPEKWSTQVGTRGLQLSGGQKQRIAIARALLR 636
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-FDEERYEKVIK--ACALEPdleILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 637 NPAFLILDEATSALDGE-AEVMVDKTIQS-LMHNRsmTTITIAHKLATIRRADQIIVVGDGK 696
Cdd:cd03250 145 DADIYLLDDPLSAVDAHvGRHIFENCILGlLLNNK--TRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
158-455 |
7.26e-35 |
|
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: 134.15 E-value: 7.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILD-AGSSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSR 236
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDgPIAHGDRSALWPLVL-------LLLALGVAEAVLSFLRRYLAGRLSLGVEHD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSdGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIA 316
Cdd:cd18543 74 LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLG 396
Cdd:cd18543 153 LVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALP 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 397 NATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18543 233 ELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
482-711 |
7.90e-35 |
|
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: 131.83 E-value: 7.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSA-SIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStynvhQWRSHF 560
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFS-GTIGENIAYG------KSNASQEEIEDAAKRANCS-FVLSFPEkwstqvgtrglQLSGGQKQRIAIAR 632
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlelqgvPKAEARERAEELLELVGLSgFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 633 ALLRNPAFLILDEATSALD-GEAEVMVDkTIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGdgkvleqgsferlSRPG 710
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDaLTREQLQE-ELLDIWRETGKTVLLVTHDIDeAVFLADRVVVLS-------------ARPG 210
|
.
gi 19112543 711 T 711
Cdd:cd03293 211 R 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
481-702 |
1.05e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 133.39 E-value: 1.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAsIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAP---SSGKILADGVDISTYNVHQWR 557
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQEP-VLFSG-TIGENIAYGKSN--ASQEEIEDAAKRancsfVLSfpekwstQVGTRGLQ------LSGGQKQR 627
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGaTVGDDVAFGLENraVPRPEMIKIVRD-----VLA-------DVGMLDYIdsepanLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 628 IAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
501-708 |
1.48e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 131.72 E-value: 1.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHFGLVGQEPVLFSG-TIGENI- 578
Cdd:COG1131 17 DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTVRENLr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 579 ----AYGKSNASQEE-IEDAAKRancsfvLSFPEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:COG1131 96 ffarLYGLPRKEARErIDELLEL------FGLTDAADRKVGT----LSGGMKQRLGLALALLHDPELLILDEPTSGLDPE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 654 AEVMVDKTIQSLmhNRSMTTITIA-HKLATIRR-ADQIIVVGDGKVLEQGSFERLSR 708
Cdd:COG1131 166 ARRELWELLREL--AAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
482-697 |
1.64e-34 |
|
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: 131.07 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAS-IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW---- 556
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RSHFGLVGQEPVLFSG-TIGENIAYGKSnASQEEIEDAAKRAncsfvlsfpEKWSTQVGTRGL------QLSGGQKQRIA 629
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELPLL-LAGVPKKERRERA---------EELLERVGLGDRlnhypsELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKV 697
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
481-709 |
4.57e-34 |
|
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: 132.87 E-value: 4.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRP-SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAP---SSGKILADGVDISTYNVHQW 556
Cdd:COG0444 1 LLEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RS----HFGLVGQE------PVLfsgTIGENIA--------YGKSNASQEEIE--------DAAKRANcsfvlSFPEkws 610
Cdd:COG0444 81 RKirgrEIQMIFQDpmtslnPVM---TVGDQIAeplrihggLSKAEARERAIEllervglpDPERRLD-----RYPH--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 611 tqvgtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALDG--EAEVMvdKTIQSLMHNRSMTTITIAHKLATIRR-AD 687
Cdd:COG0444 150 --------ELSGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAQIL--NLLKDLQRELGLAILFITHDLGVVAEiAD 219
|
250 260
....*....|....*....|...
gi 19112543 688 QIIVVGDGKVLEQGSFERL-SRP 709
Cdd:COG0444 220 RVAVMYAGRIVEEGPVEELfENP 242
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
158-428 |
1.10e-33 |
|
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: 131.09 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDagssgDSSVTHIMGIPSGTFYI---GLLGLFFLGSACNFGRIITLRLLSERIV 234
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILID-----DVLIQLGPGGNTSLLLLlvlGLAGAYVLSALLGILRGRLLARLGERIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 235 SRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSLSMYLSDGL----RSSVSAIAGIGMMLYVSMRLTGYMSL 310
Cdd:cd18563 76 ADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTD----RLQDFLSDGLpdflTNILMIIGIGVVLFSLNWKLALLVLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 311 IVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFG 390
Cdd:cd18563 152 PVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFP 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 19112543 391 STGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYT 428
Cdd:cd18563 232 LLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYL 269
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
173-454 |
1.13e-33 |
|
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: 130.92 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 173 MSIPYIVGKILDAGSSGDSsvthimgiPSGTFY-IGLLGLFFLGSACNFGRIITLRLLS-ERIVSRLRARLFAKCMSLDG 250
Cdd:cd18590 13 TFIPYYTGRVIDILGGEYQ--------HNAFTSaIGLMCLFSLGSSLSAGLRGGLFMCTlSRLNLRLRHQLFSSLVQQDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 251 AFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLS 330
Cdd:cd18590 85 GFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 331 RTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILALGGRM 410
Cdd:cd18590 165 QAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19112543 411 VAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASR 454
Cdd:cd18590 245 IQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAK 288
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
481-699 |
1.76e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.25 E-value: 1.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN---VHQWR 557
Cdd:COG2884 1 MIRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQE-PVLFSGTIGENIAY-----GKSNAS-QEEIEDA------AKRANCsfvlsFPEkwstqvgtrglQLSGGQ 624
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEiRRRVREVldlvglSDKAKA-----LPH-----------ELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLILDEATSALDgeaevmvDKTIQSLMH-----NRSMTTITIA-HKLATIRRADQ-IIVVGDGKV 697
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLD-------PETSWEIMElleeiNRRGTTVLIAtHDLELVDRMPKrVLELEDGRL 215
|
..
gi 19112543 698 LE 699
Cdd:COG2884 216 VR 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
486-702 |
2.21e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.78 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 486 NVGFAY-PTRPSASI-FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVH--QWRSHFG 561
Cdd:PRK13637 7 NLTHIYmEGTPFEKKaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEP--VLFSGTIGENIAYGKSN--ASQEEIEDAAKRANCSFVLSFpEKWSTQvgtRGLQLSGGQKQRIAIARALLRN 637
Cdd:PRK13637 87 LVFQYPeyQLFEETIEKDIAFGPINlgLSEEEIENRVKRAMNIVGLDY-EDYKDK---SPFELSGGQKRRVAIAGVVAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:PRK13637 163 PKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
482-718 |
2.50e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 138.33 E-value: 2.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYptRPS-ASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:PLN03130 1238 IKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSGTIGENI-AYGKSNASqeEIEDAAKRANCSFVLSF-PEKWSTQVGTRGLQLSGGQKQRIAIARALLRNP 638
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLdPFNEHNDA--DLWESLERAHLKDVIRRnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 639 AFLILDEATSALDGEAEVMVDKTIQSLMhnRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERL-SRPGTNFYKLM 717
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEF--KSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMV 1471
|
.
gi 19112543 718 R 718
Cdd:PLN03130 1472 Q 1472
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
481-702 |
4.59e-33 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 127.42 E-value: 4.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLR----FYAPSSGKILADGVDI--STYNVH 554
Cdd:COG1126 1 MIEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKST----LLRcinlLEEPDSGTITVDGEDLtdSKKDIN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 555 QWRSHFGLVGQEPVLFSG-TIGENIAYG----KsNASQEEIEDAAK----------RANcsfvlSFPEkwstqvgtrglQ 619
Cdd:COG1126 74 KLRRKVGMVFQQFNLFPHlTVLENVTLApikvK-KMSKAEAEERAMellervgladKAD-----AYPA-----------Q 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 LSGGQKQRIAIARALLRNPAFLILDEATSALDGE--AEVMvdKTIQSLMHnRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:COG1126 137 LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPElvGEVL--DVMRDLAK-EGMTMVVVTHEMGFAREvADRVVFMDGGR 213
|
....*.
gi 19112543 697 VLEQGS 702
Cdd:COG1126 214 IVEEGP 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
479-713 |
5.02e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 130.60 E-value: 5.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLR----FYAPSSGKILADGVDISTYNVH 554
Cdd:COG3842 3 MPALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTT----LLRmiagFETPDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 555 QwRsHFGLVGQEPVLFSG-TIGENIAYG--KSNASQEEIEDAAKRAncsfvLSfpekwstQVGTRGL------QLSGGQK 625
Cdd:COG3842 76 K-R-NVGMVFQDYALFPHlTVAENVAFGlrMRGVPKAEIRARVAEL-----LE-------LVGLEGLadryphQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 626 QRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLA---TIrrADQIIVVGDGKVLEQGS 702
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
250
....*....|..
gi 19112543 703 FERL-SRPGTNF 713
Cdd:COG3842 220 PEEIyERPATRF 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
476-651 |
8.06e-33 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 127.51 E-value: 8.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 476 TVGKAILSFRNVGFAYPTRPSA-SIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLR----FYAPSSGKILADGVDist 550
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKST----LLRliagLEKPTSGEVLVDGKP--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 551 ynVHQWRSHFGLVGQEPVLFs-gTIGENIAYG--KSNASQEEIEDAAKRAncsfvLSfpekwstQVGTRGL------QLS 621
Cdd:COG1116 75 --VTGPGPDRGVVFQEPALLpwlTVLDNVALGleLRGVPKAERRERAREL-----LE-------LVGLAGFedayphQLS 140
|
170 180 190
....*....|....*....|....*....|
gi 19112543 622 GGQKQRIAIARALLRNPAFLILDEATSALD 651
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
204-718 |
9.28e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 136.26 E-value: 9.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 204 FYIGLLGLFFLGS-ACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTD----SSIVGKSLSM 278
Cdd:PLN03232 951 FYIVVYALLGFGQvAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDigdiDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 279 YLSDgLRSSVSAIAGIGMMLYVSmrLTGYMSLIVppialgaFFYGEY---------VRKLSRTTQDALGDLTRVSEEKLA 349
Cdd:PLN03232 1031 FMNQ-LWQLLSTFALIGTVSTIS--LWAIMPLLI-------LFYAAYlyyqstsreVRRLDSVTRSPIYAQFGEALNGLS 1100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 350 NVRTTQAFLGERQEVNRYNDY-IRnlFVLAKreafasgifFGSTGFLgnatVIAILALGGRMV-AAGDITVGQLSSFLLY 427
Cdd:PLN03232 1101 SIRAYKAYDRMAKINGKSMDNnIR--FTLAN---------TSSNRWL----TIRLETLGGVMIwLTATFAVLRNGNAENQ 1165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 428 TVYAggSIVGL----SGCFTDIMKG-LGAASRLFELLDAKPKIAPTVGIPVPVTV------------GKAILSFRNVGFA 490
Cdd:PLN03232 1166 AGFA--STMGLllsyTLNITTLLSGvLRQASKAENSLNSVERVGNYIDLPSEATAiiennrpvsgwpSRGSIKFEDVHLR 1243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 491 YptRPS-ASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVL 569
Cdd:PLN03232 1244 Y--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 570 FSGTIGENI-AYGKSNASqeEIEDAAKRANCSFVLS-FPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEAT 647
Cdd:PLN03232 1322 FSGTVRFNIdPFSEHNDA--DLWEALERAHIKDVIDrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 648 SALDGEAEVMVDKTIQSLMhnRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS-FERLSRPGTNFYKLMR 718
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIREEF--KSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSpQELLSRDTSAFFRMVH 1469
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
480-708 |
1.45e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 126.32 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN---VHQW 556
Cdd:COG3638 1 PMLELRNLSKRYPGGTPA--LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RS-------HFGLVGQEPVLfsgtigENIAYGK-----------SNASQEEIEDAAKrancsfVLSfpekwstQVG---- 614
Cdd:COG3638 79 RRrigmifqQFNLVPRLSVL------TNVLAGRlgrtstwrsllGLFPPEDRERALE------ALE-------RVGladk 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 615 --TRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEA--EVMvdKTIQSLMHNRSMTTITIAHKLATIRR-ADQI 689
Cdd:COG3638 140 ayQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTarQVM--DLLRRIAREDGITVVVNLHQVDLARRyADRI 217
|
250
....*....|....*....
gi 19112543 690 IVVGDGKVLEQGSFERLSR 708
Cdd:COG3638 218 IGLRDGRVVFDGPPAELTD 236
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
501-709 |
3.80e-32 |
|
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: 124.76 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHqwRSHFGLVGQEPVLFSG-TIGENIA 579
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPHmTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 580 YGKSNASQEEIEDAAKRANCSFVLSFPEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVD 659
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 660 KTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFER-LSRP 709
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEvFKKP 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
481-701 |
6.03e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 125.25 E-value: 6.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTrPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:PRK13648 7 IIVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPV-LFSGTIGE-NIAYGKSNAS------QEEIEDAAKRANCSfvlsfpekwsTQVGTRGLQLSGGQKQRIAIAR 632
Cdd:PRK13648 86 GIVFQNPDnQFVGSIVKyDVAFGLENHAvpydemHRRVSEALKQVDML----------ERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 633 ALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQG 701
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
166-428 |
1.02e-31 |
|
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: 125.25 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 166 LVSSGVTMSIPYIVGKILDAGssgdssvthimgIPSGTFY------IGLLGLFFLGSACNFGRIITLRLLSERIVSRLRA 239
Cdd:cd18549 12 VLIAALDLVFPLIVRYIIDDL------------LPSKNLRliliigAILLALYILRTLLNYFVTYWGHVMGARIETDMRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 240 RLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGA 319
Cdd:cd18549 80 DLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 320 FFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYnDYIRNLFVLAKREAF-ASGIFFGSTGFLGNA 398
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKF-DEGNDRFLESKKKAYkAMAYFFSGMNFFTNL 238
|
250 260 270
....*....|....*....|....*....|
gi 19112543 399 TVIAILALGGRMVAAGDITVGQLSSFLLYT 428
Cdd:cd18549 239 LNLVVLVAGGYFIIKGEITLGDLVAFLLYV 268
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
158-454 |
1.76e-31 |
|
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: 124.43 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAG-SSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSR 236
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGiANGDLSYILRTGL-------LMLLLALLGLIAGILAGYFAAKASQGFGRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIA 316
Cdd:cd18548 74 LRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLG 396
Cdd:cd18548 154 LVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIM 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 397 NATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASR 454
Cdd:cd18548 234 NLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKR 291
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
479-697 |
4.32e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.92 E-value: 4.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRS 558
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEP-VLFSG-TIGENIAYGKSNASQEeIEDAAKRANCSFVLSFPEKWSTQVGTRglqLSGGQKQRIAIARALLR 636
Cdd:PRK13650 82 KIGMVFQNPdNQFVGaTVEDDVAFGLENKGIP-HEEMKERVNEALELVGMQDFKEREPAR---LSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 637 NPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKV 697
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
481-711 |
4.56e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.42 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSA-SIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA----PSSGKILADGVDISTYNVHQ 555
Cdd:COG1135 1 MIELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKST----LIRCINllerPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRS----------HFGLvgqepvLFSGTIGENIAY-----GKSNASQEE----------IEDaakRANcsfvlSFPEkws 610
Cdd:COG1135 77 LRAarrkigmifqHFNL------LSSRTVAENVALpleiaGVPKAEIRKrvaellelvgLSD---KAD-----AYPS--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 611 tqvgtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEaevmvdkTIQSLMH-----NRSM--TTITIAHKLATI 683
Cdd:COG1135 140 --------QLSGGQKQRVGIARALANNPKVLLCDEATSALDPE-------TTRSILDllkdiNRELglTIVLITHEMDVV 204
|
250 260 270
....*....|....*....|....*....|
gi 19112543 684 RR-ADQIIVVGDGKVLEQGS-FERLSRPGT 711
Cdd:COG1135 205 RRiCDRVAVLENGRIVEQGPvLDVFANPQS 234
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
480-697 |
5.03e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.73 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDistynVHQWRSH 559
Cdd:COG1121 5 PAIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 560 FGLVGQEP------------VLFSGTIGENIAYGKSNASQ-EEIEDAAKRANCSfvlsfpEKWSTQVGtrglQLSGGQKQ 626
Cdd:COG1121 77 IGYVPQRAevdwdfpitvrdVVLMGRYGRRGLFRRPSRADrEAVDEALERVGLE------DLADRPIG----ELSGGQQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 627 RIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
499-697 |
2.14e-30 |
|
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: 119.17 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDI--STYNVHQWRSHFGLVGQEPVLFSG-TIG 575
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 576 ENIAYGKSNASQEEIEDAAKRAncsfvlsfpEKWSTQVG------TRGLQLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:cd03262 95 ENITLAPIKVKGMSKAEAEERA---------LELLEKVGladkadAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 19112543 650 LDGE--AEVMvdKTIQSLMHNrSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:cd03262 166 LDPElvGEVL--DVMKDLAEE-GMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
501-709 |
3.21e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 121.76 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW---RSHFGLVGQEPvlFSG----- 572
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDP--YASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIAYGKSN---ASQEEIEDAAKRA------NCSFVLSFPEkwstqvgtrglQLSGGQKQRIAIARALLRNPAFLIL 643
Cdd:COG4608 113 TVGDIIAEPLRIhglASKAERRERVAELlelvglRPEHADRYPH-----------EFSGGQRQRIGIARALALNPKLIVC 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 644 DEATSALdgeaevmvDKTIQS--------LMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL-SRP 709
Cdd:COG4608 182 DEPVSAL--------DVSIQAqvlnlledLQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELyARP 249
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
482-697 |
3.56e-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: 117.11 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHFG 561
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENiaygksnasqeeiedaakrancsfvlsfpekwstqvgtrgLQLSGGQKQRIAIARALLRNPAF 640
Cdd:cd03230 77 YLPEEPSLYENlTVREN----------------------------------------LKLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 641 LILDEATSALDGEAEVMVDKTIQSLmhNRSMTTITIA-HKLATI-RRADQIIVVGDGKV 697
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLREL--KKEGKTILLSsHILEEAeRLCDRVAILNNGRI 173
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
482-713 |
1.05e-29 |
|
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: 117.79 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG 561
Cdd:cd03295 1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENIAYGKS--NASQEEIEDAAKRA-------NCSFVLSFPEkwstqvgtrglQLSGGQKQRIAIA 631
Cdd:cd03295 79 YVIQQIGLFPHmTVEENIALVPKllKWPKEKIRERADELlalvgldPAEFADRYPH-----------ELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 632 RALLRNPAFLILDEATSALDG------EAEVmvdKTIQSLMHNrsmTTITIAHKL-ATIRRADQIIVVGDGKVLEQGS-F 703
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPitrdqlQEEF---KRLQQELGK---TIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTpD 221
|
250
....*....|
gi 19112543 704 ERLSRPGTNF 713
Cdd:cd03295 222 EILRSPANDF 231
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
163-455 |
1.17e-29 |
|
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: 119.11 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 163 SLLLVSSGVTMSIPYIVGKILDAGSSGDSsvthimgiPSG-TFYIGLLGLFFLGSA-----CNFGRIITLrllsERIVSR 236
Cdd:cd18589 3 GLVVLSSLGEMAIPYYTGRMTDWIMNKDA--------PEAfTAAITVMSLLTIASAvsefvCDLIYNITM----SRIHSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIA 316
Cdd:cd18589 71 LQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLG 396
Cdd:cd18589 151 LVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 397 NATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18589 231 LALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
474-706 |
1.55e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 117.83 E-value: 1.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 474 PVTVGKAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLR-------FYaPS---SGKILA 543
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKST----LLRclnrmndLI-PGarvEGEILL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 544 DGVDI--STYNVHQWRSHFGLVGQEPVLFSGTIGENIAYG------KSNASQEEI-EDAAKRANcsfvLsfpekWStQVG 614
Cdd:COG1117 76 DGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAA----L-----WD-EVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 615 TR----GLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmtTITIA-HKLATIRR-ADQ 688
Cdd:COG1117 146 DRlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY---TIVIVtHNMQQAARvSDY 222
|
250
....*....|....*...
gi 19112543 689 IIVVGDGKVLEQGSFERL 706
Cdd:COG1117 223 TAFFYLGELVEFGPTEQI 240
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
482-707 |
5.45e-29 |
|
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: 115.73 E-value: 5.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVhQWRSHFG 561
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENIAY------GKSNASQEEIEDAAKRANCSFVLSfpEKWSTqvgtrglqLSGGQKQRIAIARAL 634
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfaelygLFDEELKKRIEELIELLGLEEFLD--RRVGE--------LSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 635 LRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITiAHKLATIRR-ADQIIVVGDGKVLEQGSFERLS 707
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFS-SHIMQEVEAlCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
507-706 |
6.56e-29 |
|
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: 116.16 E-value: 6.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 507 IHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAyGKSNAS 586
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECKCT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 587 QEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSL 665
Cdd:cd03288 123 DDRLWEALEIAQLkNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19112543 666 MHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERL 706
Cdd:cd03288 203 FADR--TVVTIAHRVSTILDADLVLVLSRGILVECDTPENL 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
176-725 |
1.47e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 123.16 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 176 PYIVGKILDAGSSGDssvthimgiPSGTFYIGLLGLFF---LGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAF 252
Cdd:PLN03232 321 PVILSHLLQSMQEGD---------PAWVGYVYAFLIFFgvtFGVLCESQYFQNVGRVGFRLRSTLVAAIFHKSLRLTHEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 253 FDFHKHGDLISRLTTDSSIVgKSLSMYLSdGLRSSVSAIAGIGMMLYVSMRLTGY-----MSLIVPPIALgaffygeYVR 327
Cdd:PLN03232 392 RKNFASGKVTNMITTDANAL-QQIAEQLH-GLWSAPFRIIVSMVLLYQQLGVASLfgsliLFLLIPLQTL-------IVR 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 328 KLSRTTQDALGDLTR---VSEEKLANVRTTQAFLGERQEVNRYNDyIRNLFVLAKREAfasGIFFGSTGFLGNAT--VIA 402
Cdd:PLN03232 463 KMRKLTKEGLQWTDKrvgIINEILASMDTVKCYAWEKSFESRIQG-IRNEELSWFRKA---QLLSAFNSFILNSIpvVVT 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 403 ILALGGRMVAAGDITVGQ-LSSFLLYTVYAGgSIVGLSGCFTDIMKGLGAASRLFELLDAKPKI-APTvgiPvPVTVGKA 480
Cdd:PLN03232 539 LVSFGVFVLLGGDLTPARaFTSLSLFAVLRS-PLNMLPNLLSQVVNANVSLQRIEELLLSEERIlAQN---P-PLQPGAP 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSgkilADGVDIstynvhqwRSHF 560
Cdd:PLN03232 614 AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----TSSVVI--------RGSV 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSGTIGENIAYGKSNASQ---EEIEDAAKRANCSFvlsFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRN 637
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFGSDFESErywRAIDVTALQHDLDL---LPGRDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 638 PAFLILDEATSALDGE-AEVMVDKTIQSLMhnRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKL 716
Cdd:PLN03232 759 SDIYIFDDPLSALDAHvAHQVFDSCMKDEL--KGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
....*....
gi 19112543 717 MRwQLGKVE 725
Cdd:PLN03232 837 ME-NAGKMD 844
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
485-702 |
2.36e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.18 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 485 RNVGFAY-----PTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIS-TYNVHQWRS 558
Cdd:PRK13633 8 KNVSYKYesneeSTEKLA--LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEP--VLFSGTIGENIAYGKSN--ASQEEI----EDAAKRANCSFVLSFPEKWstqvgtrglqLSGGQKQRIAI 630
Cdd:PRK13633 86 KAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIrervDESLKKVGMYEYRRHAPHL----------LSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 631 ARALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDpsGRREVV--NTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
481-709 |
2.84e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.83 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTisqLLLRF---YAPSSGKILADGVDISTYNVHQWR 557
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKST---LLLHLngiYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQEP--VLFSGTIGENIAYGKSNA--SQEEIEdaaKRANCSFVLsfpekwstqVGTRGLQ------LSGGQKQR 627
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGPVNMglDKDEVE---RRVEEALKA---------VRMWDFRdkppyhLSYGQKKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 628 IAIARALLRNPAFLILDEATSALD--GEAEVMvdkTIQSLMHNRSMTTITIAHKL-ATIRRADQIIVVGDGKVLEQGSFE 704
Cdd:PRK13647 147 VAIAGVLAMDPDVIVLDEPMAYLDprGQETLM---EILDRLHNQGKTVIVATHDVdLAAEWADQVIVLKEGRVLAEGDKS 223
|
....*
gi 19112543 705 RLSRP 709
Cdd:PRK13647 224 LLTDE 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
482-713 |
4.08e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.01 E-value: 4.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA----PSSGKILADGVDISTyNVHQWR 557
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTT----LLRIIAgletPDSGRIVLNGRDLFT-NLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQEPVLFSG-TIGENIAYG--KSNASQEEIedaAKRAncsfvlsfpEKWSTQVGTRGL------QLSGGQKQRI 628
Cdd:COG1118 75 RRVGFVFQHYALFPHmTVAENIAFGlrVRPPSKAEI---RARV---------EELLELVQLEGLadrypsQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 629 AIARALLRNPAFLILDEATSALDgeaeVMVDKTIQSL---MHNRS-MTTITIAHKL--AtIRRADQIIVVGDGKVLEQGS 702
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALD----AKVRKELRRWlrrLHDELgGTTVFVTHDQeeA-LELADRVVVMNQGRIEQVGT 217
|
250
....*....|..
gi 19112543 703 FERL-SRPGTNF 713
Cdd:COG1118 218 PDEVyDRPATPF 229
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
480-654 |
4.45e-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: 112.19 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLR----FYAPSSGKILADGVDISTyNVHQ 555
Cdd:COG4133 1 MMLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT----LLRilagLLPPSAGEVLWNGEPIRD-ARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQEPVLFSG-TIGENIAY----GKSNASQEEIEDAAKRancsfvlsfpekwstqVGTRGL------QLSGGQ 624
Cdd:COG4133 73 YRRRLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEA----------------VGLAGLadlpvrQLSAGQ 136
|
170 180 190
....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLILDEATSALDGEA 654
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAG 166
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
482-697 |
5.76e-28 |
|
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: 113.05 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTY---NVHQWRS 558
Cdd:cd03256 1 IEVENLSKTYPNGKKA--LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSG-TIGENIAYGKSNA-----------SQEEIEDAAKrancsfVLsfpekwsTQVG------TRGLQL 620
Cdd:cd03256 79 QIGMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALA------AL-------ERVGlldkayQRADQL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 621 SGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
482-713 |
9.34e-28 |
|
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: 111.95 E-value: 9.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStyNVHQWRSHFG 561
Cdd:cd03300 1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT--NLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENIAYG--KSNASQEEIEDAAKRAncsfvLSfpekwstQVGTRGL------QLSGGQKQRIAIAR 632
Cdd:cd03300 76 TVFQNYALFPHlTVFENIAFGlrLKKLPKAEIKERVAEA-----LD-------LVQLEGYanrkpsQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 633 ALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQGSFERL-SRPG 710
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIyEEPA 223
|
...
gi 19112543 711 TNF 713
Cdd:cd03300 224 NRF 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
479-690 |
1.46e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 111.34 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRS 558
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANCSFVLsfPEKWSTQvgtRGLQLSGGQKQRIAIARALLRNP 638
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFAL--PDTILTK---NIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 639 AFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQII 690
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
206-427 |
1.54e-27 |
|
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: 113.38 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 206 IGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLR 285
Cdd:cd18564 58 AALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 286 SSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVN 365
Cdd:cd18564 138 NLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEER 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 366 RyndyirnlFVLAKREAFASGI--------FFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLY 427
Cdd:cd18564 218 R--------FARENRKSLRAGLraarlqalLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
484-702 |
1.85e-27 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.13 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAYPTrPSASI--FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRS--- 558
Cdd:PRK11153 4 LKNISKVFPQ-GGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 -------HFGLvgqepvLFSGTIGENIAYG--KSNASQEEIED-----------AAKRancsfvLSFPEkwstqvgtrgl 618
Cdd:PRK11153 83 qigmifqHFNL------LSSRTVFDNVALPleLAGTPKAEIKArvtellelvglSDKA------DRYPA----------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEaevmvdkTIQSLMH-----NR--SMTTITIAHKLATIRR-ADQII 690
Cdd:PRK11153 140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPA-------TTRSILEllkdiNRelGLTIVLITHEMDVVKRiCDRVA 212
|
250
....*....|..
gi 19112543 691 VVGDGKVLEQGS 702
Cdd:PRK11153 213 VIDAGRLVEQGT 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
147-645 |
1.96e-27 |
|
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: 117.21 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 147 LFTLARGQGWNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSVthimgipsGTFYIGLLGLFFLGSACNFGRIITL 226
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALINQALNATGAALARL--------LLLFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 227 rllSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMyLSDGLRSSVSAIAGIGMMLYVSMRLTG 306
Cdd:COG4615 76 ---GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 307 yMSLIVppIALGAFFYGEYVRKL------SRTTQDAL----GDLTR-VSEEKLaNVRTTQAFLGE--RQEVNRYNDYIR- 372
Cdd:COG4615 152 -LTLVL--LGLGVAGYRLLVRRArrhlrrAREAEDRLfkhfRALLEgFKELKL-NRRRRRAFFDEdlQPTAERYRDLRIr 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 373 --NLFVLAkrEAFASGIFFGstgFLGnatviAILALggrMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLG 450
Cdd:COG4615 228 adTIFALA--NNWGNLLFFA---LIG-----LILFL---LPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 451 AASRLFELLDAKPKIAPTVGIPVPVTVGKAI--LSFRNVGFAYPTRPSASIFD--NLSFDIHPGTNVAIVAPSGGGKSTI 526
Cdd:COG4615 295 ALRKIEELELALAAAEPAAADAAAPPAPADFqtLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 527 SQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGeniayGKSNASQEEIEDAAKRANCSFVLSFP 606
Cdd:COG4615 375 AKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRLLG-----LDGEADPARARELLERLELDHKVSVE 449
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 19112543 607 E-KWSTqvgtrgLQLSGGQKQRIAIARALLRNPAFLILDE 645
Cdd:COG4615 450 DgRFST------TDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
457-706 |
2.44e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.73 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 457 ELLDAKPKiaptvGIPVPVTVGKA-ILSFRNVGFAYPTRPS--------ASIFDNLSFDIHPGTNVAIVAPSGGGKSTIS 527
Cdd:PRK15134 255 KLLNSEPS-----GDPVPLPEPASpLLDVEQLQVAFPIRKGilkrtvdhNVVVKNISFTLRPGETLGLVGESGSGKSTTG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 528 QLLLRFYApSSGKILADGVDISTYNVHQ---WRSHFGLVGQEP---------VLfsGTIGENIAYGKSNASQEEIEDAAK 595
Cdd:PRK15134 330 LALLRLIN-SQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 596 RAncsfvlsfpekwSTQVG----TRG---LQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHN 668
Cdd:PRK15134 407 AV------------MEEVGldpeTRHrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
250 260 270
....*....|....*....|....*....|....*....
gi 19112543 669 RSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK15134 475 HQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
501-704 |
2.78e-27 |
|
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: 110.60 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRSHFGLVG--QEPVLFSG-TIGEN 577
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHE-IARLGIGRtfQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 IAYG---------KSNASQEEIEDAAKRANcsFVLSF---PEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDE 645
Cdd:cd03219 96 VMVAaqartgsglLLARARREEREARERAE--ELLERvglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 646 ATSAL-DGEAEVMVDkTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFE 704
Cdd:cd03219 170 PAAGLnPEETEELAE-LIREL-RERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPD 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
479-709 |
5.54e-27 |
|
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: 115.94 E-value: 5.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRN--VGFAYPTRPSAsIFDNLSFDIHPGTNVAIVAPSGGGKS----TISQLLLRFYAPSSGKILADGVDISTYN 552
Cdd:COG4172 4 MPLLSVEDlsVAFGQGGGTVE-AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 VHQWR----SHFGLVGQEPV-----LFsgTIGENIA--------YGKSNASQEEIE--------DAAKRANcsfvlSFPE 607
Cdd:COG4172 83 ERELRrirgNRIAMIFQEPMtslnpLH--TIGKQIAevlrlhrgLSGAAARARALEllervgipDPERRLD-----AYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 608 kwstqvgtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALDgeaeVmvdkTIQ--------SLMHNRSMTTITIAHK 679
Cdd:COG4172 156 -----------QLSGGQRQRVMIAMALANEPDLLIADEPTTALD----V----TVQaqildllkDLQRELGMALLLITHD 216
|
250 260 270
....*....|....*....|....*....|..
gi 19112543 680 LATIRR-ADQIIVVGDGKVLEQGSFERL-SRP 709
Cdd:COG4172 217 LGVVRRfADRVAVMRQGEIVEQGPTAELfAAP 248
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
466-702 |
1.12e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.19 E-value: 1.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 466 APTVGIPVPVTVGKaiLSFRNVGFAY----PTrpsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI 541
Cdd:PTZ00243 1295 SPTSAAPHPVQAGS--LVFEGVQMRYreglPL-----VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEI 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 542 LADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGENIAyGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQL 620
Cdd:PTZ00243 1368 RVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLrERVASESEGIDSRVLEGGSNY 1446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 621 SGGQKQRIAIARALL-RNPAFLILDEATSALDGEAEVMVDKTIQSLMHNrsMTTITIAHKLATIRRADQIIVVGDGKVLE 699
Cdd:PTZ00243 1447 SVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSA--YTVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
|
...
gi 19112543 700 QGS 702
Cdd:PTZ00243 1525 MGS 1527
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
480-702 |
1.44e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.70 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLR----FYAPSSGKILADGVDIStyNVHQ 555
Cdd:COG3839 2 ASLELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKST----LLRmiagLEDPTSGEILIGGRDVT--DLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQEPVLF-SGTIGENIAYGKSNA--SQEEIEDAAKRAncsfvlsfpekwSTQVGTRGL------QLSGGQKQ 626
Cdd:COG3839 73 KDRNIAMVFQSYALYpHMTVYENIAFPLKLRkvPKAEIDRRVREA------------AELLGLEDLldrkpkQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 627 RIAIARALLRNPAFLILDEATSALDgeAEVMVD--KTIQSLMHNRSMTTITIAHKLA---TIrrADQIIVVGDGKVLEQG 701
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLD--AKLRVEmrAEIKRLHRRLGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVG 216
|
.
gi 19112543 702 S 702
Cdd:COG3839 217 T 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
502-701 |
1.60e-26 |
|
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: 107.77 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFDIhPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGV--DISTYNVH---QWRsHFGLVGQEPVLFSG-TIG 575
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINlppQQR-KIGLVFQQYALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 576 ENIAYGKSNASQEEIEDAAKRANCSFVLsfpekwsTQVGTRG-LQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEA 654
Cdd:cd03297 94 ENLAFGLKRKRNREDRISVDELLDLLGL-------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19112543 655 EVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
502-713 |
1.91e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 109.27 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRS-----------HFGLVGQEPVLf 570
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALLPHRTVL- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 571 sgtigENIAYG---KSNASQEEIEDAAKrancsfVLSfpekwstQVGTRGL------QLSGGQKQRIAIARALLRNPAFL 641
Cdd:cd03294 121 -----ENVAFGlevQGVPRAEREERAAE------ALE-------LVGLEGWehkypdELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 642 ILDEATSALD----GEaevMVDKTIQsLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQGSFER-LSRPGTNF 713
Cdd:cd03294 183 LMDEAFSALDplirRE---MQDELLR-LQAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEiLTNPANDY 256
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
481-706 |
3.48e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.87 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDI--STYNVHQWRS 558
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSG-TIGENIAYGK---SNASQEEIEDAAK----------RANcsfvlSFPEkwstqvgtrglQLSGGQ 624
Cdd:PRK09493 78 EAGMVFQQFYLFPHlTALENVMFGPlrvRGASKEEAEKQARellakvglaeRAH-----HYPS-----------ELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSF 703
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLA-EEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDP 220
|
...
gi 19112543 704 ERL 706
Cdd:PRK09493 221 QVL 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
502-701 |
3.61e-26 |
|
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: 106.81 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFD--IHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHqwRSHFGLVGQEPVLFSG-TIGENI 578
Cdd:cd03298 14 PMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 579 AYGKS-----NASQEEIEDAAKRancsfvlsfpekwstQVGTRGL------QLSGGQKQRIAIARALLRNPAFLILDEAT 647
Cdd:cd03298 92 GLGLSpglklTAEDRQAIEVALA---------------RVGLAGLekrlpgELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 648 SALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
504-706 |
4.35e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 107.36 E-value: 4.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 504 SFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDiSTYNVHQWRShFGLVGQEPVLFSG-TIGENIAYG- 581
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRP-VSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 582 ----KSNASQ-EEIEDAAKRANCSFVLS-FPEkwstqvgtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALD---- 651
Cdd:PRK10771 97 npglKLNAAQrEKLHAIARQMGIEDLLArLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 652 GEAEVMVDktiqSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK10771 166 QEMLTLVS----QVCQERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
356-709 |
5.51e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 112.98 E-value: 5.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 356 AFL-GERQEVN----RYNDYIRNLFVLAKREAfasGIFFGSTGFLGNATVIAILALGGRmVAAGDITVGQLSSfllyTVY 430
Cdd:COG4178 235 ALYrGEAAERRrlrrRFDAVIANWRRLIRRQR---NLTFFTTGYGQLAVIFPILVAAPR-YFAGEITLGGLMQ----AAS 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 431 AGGSIVG-LSgCFTDIMKGLGA----ASRLFELLDA-KPKIAPTVGIPVPVTVGKAILSFRNVGFAYPT-RPsasIFDNL 503
Cdd:COG4178 307 AFGQVQGaLS-WFVDNYQSLAEwratVDRLAGFEEAlEAADALPEAASRIETSEDGALALEDLTLRTPDgRP---LLEDL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 504 SFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA---PS-SGKI-LADGVDIStynvhqwrshfgLVGQEPVLFSGTIGENI 578
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKST----LLRAIAglwPYgSGRIaRPAGARVL------------FLPQRPYLPLGTLREAL 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 579 AY--GKSNASQEEIEDAAKRANcsfvLsfpEKWSTQVGTR---GLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:COG4178 447 LYpaTAEAFSDAELREALEAVG----L---GHLAERLDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 654 AEVMVDKTIQSLMHNrsMTTITIAHKLATIRRADQIIV-VGDGkvleQGSFERLSRP 709
Cdd:COG4178 520 NEAALYQLLREELPG--TTVISVGHRSTLAAFHDRVLElTGDG----SWQLLPAEAP 570
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
480-701 |
8.21e-26 |
|
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: 107.09 E-value: 8.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSG---KILadGVDISTYNVHQW 556
Cdd:COG1119 2 PLLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RSHFGLV---------GQEPVL------FSGTIGeniAYGKSNASQEEiedaakRAncsfvlsfpEKWSTQVGTRGL--- 618
Cdd:COG1119 77 RKRIGLVspalqlrfpRDETVLdvvlsgFFDSIG---LYREPTDEQRE------RA---------RELLELLGLAHLadr 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 ---QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRA-DQIIVVGD 694
Cdd:COG1119 139 pfgTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLLKD 218
|
....*..
gi 19112543 695 GKVLEQG 701
Cdd:COG1119 219 GRVVAAG 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
499-706 |
1.50e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 105.21 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLR----FYAPSSGKILADGVDISTYNVHQwRSHFGL--VGQEPVLFSG 572
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTT----LLKtimgLLPPRSGSIRFDGRDITGLPPHE-RARAGIgyVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 -TIGENIAYGKSNASQEEIEDAAKRAncsFVLsFP---EKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATS 648
Cdd:cd03224 90 lTVEENLLLGAYARRRAKRKARLERV---YEL-FPrlkERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 649 ALdgeAEVMVDKTIQSL--MHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:cd03224 162 GL---APKIVEEIFEAIreLRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
484-697 |
1.59e-25 |
|
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: 105.18 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAYPtrPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN---VHQWRSHF 560
Cdd:cd03292 3 FINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSG-TIGENIAYGKSnASQEEIEDAAKRAncSFVLSfpekwstQVGTRG------LQLSGGQKQRIAIARA 633
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAFALE-VTGVPPREIRKRV--PAALE-------LVGLSHkhralpAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 634 LLRNPAFLILDEATSALDGEAEVMVDKTIQSLmhNRSMTTITIAHKLATI--RRADQIIVVGDGKV 697
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKI--NKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
501-713 |
3.67e-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: 104.73 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStyNVHQWRSHFGLVGQEPVLFSG-TIGENIA 579
Cdd:cd03296 19 DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGFVFQHYALFRHmTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 580 YG-KSNASQEEIEDAAKRANCSFVLSFpekwstqVGTRGL------QLSGGQKQRIAIARALLRNPAFLILDEATSALDG 652
Cdd:cd03296 97 FGlRVKPRSERPPEAEIRAKVHELLKL-------VQLDWLadrypaQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 653 EAEVMVDKTIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQGSFERLSR-PGTNF 713
Cdd:cd03296 170 KVRKELRRWLRRLHDELHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDhPASPF 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
486-697 |
3.90e-25 |
|
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: 103.49 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 486 NVGFAYptRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTynvHQWRSHFGLVGQ 565
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 566 EP--VLFSGTIGENIAYGKSNAS--QEEIEDAAKRANcsfvLSFPEKWSTQvgtrglQLSGGQKQRIAIARALLRNPAFL 641
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDagNEQAETVLKDLD----LYALKERHPL------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 642 ILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
482-651 |
7.08e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 102.95 E-value: 7.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAP---SSGKILADGVDISTYNVHQwRs 558
Cdd:COG4136 2 LSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ-R- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSG-TIGENIAYG-----KSNASQEEIEDAAKRANCS-FVLSFPEkwstqvgtrglQLSGGQKQRIAIA 631
Cdd:COG4136 77 RIGILFQDDLLFPHlSVGENLAFAlpptiGRAQRRARVEQALEEAGLAgFADRDPA-----------TLSGGQRARVALL 145
|
170 180
....*....|....*....|
gi 19112543 632 RALLRNPAFLILDEATSALD 651
Cdd:COG4136 146 RALLAEPRALLLDEPFSKLD 165
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
503-701 |
8.23e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.06 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 503 LSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN--------VHQWRSHFGLVGQEPVLFSG-T 573
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglIRQLRQHVGFVFQNFNLFPHrT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 IGENIAYGKSNASQEEIEDAAKRAncsfvlsfpEKWSTQVGTRGLQ------LSGGQKQRIAIARALLRNPAFLILDEAT 647
Cdd:PRK11264 102 VLENIIEGPVIVKGEPKEEATARA---------RELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEVILFDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 648 SALDGEAEVMVDKTIQSLMH-NRSMTTITiaHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQeKRTMVIVT--HEMSFARDvADRAIFMDQGRIVEQG 226
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
481-702 |
1.21e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTisqLLLRF---YAPSSGKILADGVDIStYN---VH 554
Cdd:PRK13639 1 ILETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKST---LFLHFngiLKPTSGEVLIKGEPIK-YDkksLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 555 QWRSHFGLVGQEP--VLFSGTIGENIAYGKSNA--SQEEIEDAAKRAncsfvlsfpekwSTQVGTRGLQ------LSGGQ 624
Cdd:PRK13639 75 EVRKTVGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEA------------LKAVGMEGFEnkpphhLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLILDEATSALD--GEAEVMvdktiqSLMHN---RSMTTITIAHK--LATIrRADQIIVVGDGKV 697
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDpmGASQIM------KLLYDlnkEGITIIISTHDvdLVPV-YADKVYVMSDGKI 215
|
....*
gi 19112543 698 LEQGS 702
Cdd:PRK13639 216 IKEGT 220
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
496-713 |
1.30e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 496 SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwrSHFGLVGQEPVLFSG-TI 574
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPHmSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GENIAYG--KSNASQEEIEDAAKRANCSFVLS-FPEKWSTQVgtrglqlSGGQKQRIAIARALLRNPAFLILDEATSALD 651
Cdd:PRK11432 96 GENVGYGlkMLGVPKEERKQRVKEALELVDLAgFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 652 GEAEVMVDKTIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQGSFERLSR-PGTNF 713
Cdd:PRK11432 169 ANLRRSMREKIRELQQQFNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRqPASRF 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
483-701 |
1.46e-24 |
|
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: 102.23 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 483 SFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGvdistYNVHQWRSHFGL 562
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 563 VGQ------------EPVLFSGTIGENIAYGKSNASQ-EEIEDAAKRANCSfvlsfpEKWSTQVGtrglQLSGGQKQRIA 629
Cdd:cd03235 73 VPQrrsidrdfpisvRDVVLMGLYGHKGLFRRLSKADkAKVDEALERVGLS------ELADRQIG----ELSGGQQQRVL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVgDGKVLEQG 701
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
476-702 |
1.65e-24 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.18 E-value: 1.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 476 TVGKAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStyNVHQ 555
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQEPVLFSG-TIGENIAYG--KSNASQEEIE----DAAKRANCSfvlSFPEKwstqvgtRGLQLSGGQKQRI 628
Cdd:PRK09452 84 ENRHVNTVFQSYALFPHmTVFENVAFGlrMQKTPAAEITprvmEALRMVQLE---EFAQR-------KPHQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 629 AIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAH-KLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK09452 154 AIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
482-702 |
1.72e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.20 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSASIfDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHFG 561
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENIAY-----GKSNASQEEIEDAAKRancsfVLSFPEKWSTQVGTrglqLSGGQKQRIAIARALL 635
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR-----VLGLTDKANKRART----LSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 636 RNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSM--TTitiaHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIilTT----HSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
481-702 |
2.42e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.77 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG--VDISTYNVHQWRS 558
Cdd:PRK13636 5 ILKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEP--VLFSGTIGENIAYGKSNAS------QEEIEDAAKRANCSFVLSFPEKWstqvgtrglqLSGGQKQRIAI 630
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAVNLKlpedevRKRVDNALKRTGIEHLKDKPTHC----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 631 ARALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIR-RADQIIVVGDGKVLEQGS 702
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmGVSEIM--KLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
454-725 |
3.34e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.06 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 454 RLFELLDAKPKI-APTVgipvPVTVGKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGK-STISQLLL 531
Cdd:PLN03130 590 RLEELLLAEERVlLPNP----PLEPGLPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLG 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 532 RFYAPSSGKILAdgvdistynvhqwRSHFGLVGQEPVLFSGTIGENIAYGkSNASQEEIEDAAKRANCSFVLS-FPEKWS 610
Cdd:PLN03130 666 ELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDlLPGGDL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 611 TQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGE-AEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQI 689
Cdd:PLN03130 732 TEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGK--TRVLVTNQLHFLSQVDRI 809
|
250 260 270
....*....|....*....|....*....|....*.
gi 19112543 690 IVVGDGKVLEQGSFERLSRPGTNFYKLMRwQLGKVE 725
Cdd:PLN03130 810 ILVHEGMIKEEGTYEELSNNGPLFQKLME-NAGKME 844
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
481-702 |
3.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.86 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEP--VLFSGTIGENIAYGKSNASQEEiEDAAKRANCSFVLSFPEKWSTQVGTRglqLSGGQKQRIAIARALLRNP 638
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPR-EEMIKRVDEALLAVNMLDFKTREPAR---LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 639 AFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK13642 160 EIIILDESTSMLDptGRQEIM--RVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAA 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
480-699 |
4.27e-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: 101.36 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPSA-SIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA----PSSGKILADGVDISTYN-- 552
Cdd:COG4181 7 PIIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKST----LLGLLAgldrPTSGTVRLAGQDLFALDed 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 -VHQWRS-HFGLVGQ-EPVLFSGTIGENIAY-----GKSnasqeeieDAAKRAncsfvlsfpEKWSTQVGTRGL------ 618
Cdd:COG4181 83 aRARLRArHVGFVFQsFQLLPTLTALENVMLplelaGRR--------DARARA---------RALLERVGLGHRldhypa 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 QLSGGQKQRIAIARALLRNPAFLILDEATSALDGE-AEVMVDkTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKV 697
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAAtGEQIID-LLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
..
gi 19112543 698 LE 699
Cdd:COG4181 225 VE 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
498-706 |
5.39e-24 |
|
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: 102.24 E-value: 5.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 498 SIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYApSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSGTIGEN 577
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 I-AYGKSnaSQEEIEDAAKRANCSFVL-SFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAE 655
Cdd:cd03289 97 LdPYGKW--SDEEIWKVAEEVGLKSVIeQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 656 VMVDKTiqsLMHNRSMTTITIA-HKLATIRRADQIIVVGDGKVLEQGSFERL 706
Cdd:cd03289 175 QVIRKT---LKQAFADCTVILSeHRIEAMLECQRFLVIEENKVRQYDSIQKL 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
501-701 |
7.78e-24 |
|
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: 100.02 E-value: 7.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStyNVHQWRSHFGLVGQEPVLFSG-TIGENIA 579
Cdd:cd03301 17 DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYPHmTVYDNIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 580 YG-KSN-ASQEEIE----DAAKRANCSFVLSFPEKwstqvgtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:cd03301 95 FGlKLRkVPKDEIDervrEVAELLQIEHLLDRKPK----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19112543 654 AEVMVDKTIQSLMHNRSMTTITIAH-KLATIRRADQIIVVGDGKVLEQG 701
Cdd:cd03301 165 LRVQMRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
501-697 |
8.39e-24 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 98.27 E-value: 8.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGvdistynvhqwrshfglvgqEPVLFSGTIgeniay 580
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFASPR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 581 gksnasqeeiedAAKRANCSFVLsfpekwstqvgtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDK 660
Cdd:cd03216 71 ------------DARRAGIAMVY---------------QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190
....*....|....*....|....*....|....*...
gi 19112543 661 TIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:cd03216 124 VIRRL-RAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
482-702 |
1.49e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.36 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPT-RP--SASIFDnLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTY----NVH 554
Cdd:PRK13649 3 INLQNVSYTYQAgTPfeGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 555 QWRSHFGLVGQ--EPVLFSGTIGENIAYGKSN--ASQEEIEDAA--KRANCSFVLSFPEKwstqvgtRGLQLSGGQKQRI 628
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAreKLALVGISESLFEK-------NPFELSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 629 AIARALLRNPAFLILDEATSALD--GEAEVMvdkTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDpkGRKELM---TLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
481-706 |
2.19e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 100.65 E-value: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYptRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEP--VLFSGTIGENIAYGKSNASQEEiEDAAKRANCSFVLSFPEKWSTQVGTrglQLSGGQKQRIAIARALLRNP 638
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDE-ETVAHRVSSALHMLGLEELRDRVPH---HLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 639 AFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATI-RRADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
481-706 |
2.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.45 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN-VHQWRSH 559
Cdd:PRK13644 1 MIRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 560 FGLVGQEP-VLFSG-TIGENIAYGKSNASQEEIEdAAKRANCSFVLSFPEKWSTQVGTrglQLSGGQKQRIAIARALLRN 637
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLAFGPENLCLPPIE-IRKRVDRALAEIGLEKYRHRSPK---TLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
501-701 |
2.35e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 98.44 E-value: 2.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStyNVHQWRSHFGLVGQEPVLFSGTIG-ENI- 578
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPNLTArENLr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 579 ----AYGKSNASQEEIEDaakrancsfVLSFPEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGEA 654
Cdd:cd03268 95 llarLLGIRKKRIDEVLD---------VVGLKDSAKKKVKG----FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19112543 655 EVMVDKTIQSLmhNRSMTTITIA-HKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03268 162 IKELRELILSL--RDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
501-704 |
2.55e-23 |
|
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: 99.73 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRSHFGLV--GQEPVLFSG-TIGEN 577
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR-IARLGIArtFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 IA-----------------YGKSNASQEEIEDAAKRAnCSFV-LSfpEKWSTQVGTrglqLSGGQKQRIAIARALLRNPA 639
Cdd:COG0411 100 VLvaaharlgrgllaallrLPRARREEREARERAEEL-LERVgLA--DRADEPAGN----LSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 640 FLILDEATSAL-DGEAEVMVDkTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFE 704
Cdd:COG0411 173 LLLLDEPAAGLnPEETEELAE-LIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
501-709 |
5.72e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 100.42 E-value: 5.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN---VHQWRSHFGLVGQEPvlfsgtigen 577
Cdd:PRK11308 32 DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 iaYGKSNASQ------EE---IE---DAAKRAncSFVLSFPEKwstqVGTRGLQ-------LSGGQKQRIAIARALLRNP 638
Cdd:PRK11308 102 --YGSLNPRKkvgqilEEpllINtslSAAERR--EKALAMMAK----VGLRPEHydryphmFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 639 AFLILDEATSALDgeaeVMVDKTIQSLMHN--RSMTT--ITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL-SRP 709
Cdd:PRK11308 174 DVVVADEPVSALD----VSVQAQVLNLMMDlqQELGLsyVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIfNNP 246
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
164-457 |
6.43e-23 |
|
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: 99.48 E-value: 6.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 164 LLLVSSGVTMSIPYIVGKILDAGssgdssvthimgIPSGTFY------IGLLGLFFLGSACNFG-RIITLRLlSERIVSR 236
Cdd:cd18550 7 LILLSALLGLLPPLLLREIIDDA------------LPQGDLGllvllaLGMVAVAVASALLGVVqTYLSARI-GQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIA 316
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 317 LGAFFYGEYVRKLSRTTQDALGDLTRVSEEKL--ANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGF 394
Cdd:cd18550 154 LPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 395 LGNATVIAILALGGRMVAAGDITVGQLSSF--LLYTVYagGSIVGLSGCFTDIMKGLGaasrLFE 457
Cdd:cd18550 234 FTAIGPALVYWVGGLLVIGGGLTIGTLVAFtaLLGRLY--GPLTQLLNIQVDLMTSLA----LFE 292
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
498-702 |
7.99e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.55 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 498 SIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSG-TIGE 576
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 577 NIAYGKS-------NASQEEIEDAAKRANCSFVLSFPEKWSTQvgtrglqLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:PRK11231 96 LVAYGRSpwlslwgRLSAEDNARVNQAMEQTRINHLADRRLTD-------LSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 650 LD--GEAEVMvdKTIQSlMHNRSMTTITIAHKL-ATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK11231 169 LDinHQVELM--RLMRE-LNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
484-722 |
1.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.94 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAY-PTRPSA--SIFD-NLSFDihPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDISTYNVHQW-- 556
Cdd:PRK13634 5 FQKVEHRYqYKTPFErrALYDvNVSIP--SGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtIGERVITAGKKNKKLkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 -RSHFGLVGQ--EPVLFSGTIGENIAYGKSNASQEEiEDAAKRANCSFVL-SFPEKWSTQvgtRGLQLSGGQKQRIAIAR 632
Cdd:PRK13634 83 lRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELvGLPEELLAR---SPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 633 ALLRNPAFLILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERLSRP 709
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDpkGRKEMM--EMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFAD 236
|
250
....*....|...
gi 19112543 710 GTnfyKLMRWQLG 722
Cdd:PRK13634 237 PD---ELEAIGLD 246
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
482-702 |
1.13e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.75 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAY-PTRPSASI-FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDI----STYNVHQ 555
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKKgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQ--EPVLFSGTIGENIAYGKSN--ASQEEIEDAAKrancsfvlsfpeKWSTQVGTRG-------LQLSGGQ 624
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL------------KWLKKVGLSEdliskspFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLILDEATSALD--GEAEVM-VDKTIQSLMHnrsmTTITIAHKLATIRR-ADQIIVVGDGKVLEQ 700
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDpeGRKEMMqLFKDYQKAGH----TVILVTHNMDDVAEyADDVLVLEHGKLIKH 226
|
..
gi 19112543 701 GS 702
Cdd:PRK13641 227 AS 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
482-706 |
3.30e-22 |
|
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: 96.07 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRSHFG 561
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 L--VGQEPVLFSG-TIGENIA-----YGKSNASQEEIEDA-------AKRANcsfvlsfpekwstqvgTRGLQLSGGQKQ 626
Cdd:cd03218 77 IgyLPQEASIFRKlTVEENILavleiRGLSKKEREEKLEElleefhiTHLRK----------------SKASSLSGGERR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 627 RIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERL 706
Cdd:cd03218 141 RVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
460-704 |
3.88e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 3.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 460 DAKPKIAptvgIPVPVTVGKAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSG 539
Cdd:COG0488 298 DKTVEIR----FPPPERLGKKVLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 540 KI-LADGVDISTYNVHqwrsHFGLVGQEPVLfsgtigENIAYGKSNASQEEIEDAAKRancsFVLSfPEKWSTQVGTrgl 618
Cdd:COG0488 371 TVkLGETVKIGYFDQH----QEELDPDKTVL------DELRDGAPGGTEQEVRGYLGR----FLFS-GDDAFKPVGV--- 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 qLSGGQKQRIAIARALLRNPAFLILDEATSALDGEaevmvdkTIQSLmhNRSM-----TTITIAHKLATIRR-ADQIIVV 692
Cdd:COG0488 433 -LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE-------TLEAL--EEALddfpgTVLLVSHDRYFLDRvATRILEF 502
|
250
....*....|...
gi 19112543 693 GDGKVLE-QGSFE 704
Cdd:COG0488 503 EDGGVREyPGGYD 515
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
482-678 |
5.21e-22 |
|
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: 93.37 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTrpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA---PS-SGKIladgvdistynVHQWR 557
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSS----LFRALAglwPWgSGRI-----------GMPEG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQEPVLFSGTIGENIAYgksnasqeeiedaakrancsfvlsfPekWSTQvgtrglqLSGGQKQRIAIARALLRN 637
Cdd:cd03223 64 EDLLFLPQRPYLPLGTLREQLIY-------------------------P--WDDV-------LSGGEQQRLAFARLLLHK 109
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19112543 638 PAFLILDEATSALDGEAEvmvdKTIQSLMHNRSMTTITIAH 678
Cdd:cd03223 110 PKFVFLDEATSALDEESE----DRLYQLLKELGITVISVGH 146
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
493-717 |
5.23e-22 |
|
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: 101.91 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 493 TRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFyAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSG 572
Cdd:TIGR01271 1228 TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIAyGKSNASQEEIEDAAKRANC-SFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALD 651
Cdd:TIGR01271 1307 TFRKNLD-PYEQWSDEEIWKVAEEVGLkSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 652 GEAEVMVDKTIQSLMHNrsMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLM 717
Cdd:TIGR01271 1386 PVTLQIIRKTLKQSFSN--CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
481-699 |
9.49e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.52 E-value: 9.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPT------RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVH 554
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 555 QWRSHFG---LVGQEP---VLFSGTIGENIAygksnasqE------EIEDAAKRANCSFVLSFPEKWSTQVGTRGLQLSG 622
Cdd:PRK10419 83 QRKAFRRdiqMVFQDSisaVNPRKTVREIIR--------EplrhllSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 623 GQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLE 699
Cdd:PRK10419 155 GQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-685 |
9.56e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 9.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 485 RNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSS-----GKILADGVDI--STYNVHQWR 557
Cdd:PRK14258 11 NNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQEPVLFSGTIGENIAYGKSNAS---QEEIEDAAKRAncsfvLSFPEKW---STQVGTRGLQLSGGQKQRIAIA 631
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpKLEIDDIVESA-----LKDADLWdeiKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19112543 632 RALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR 685
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
494-702 |
1.04e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.22 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 494 RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVL-FSG 572
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIAYGKSNASQEEIEDAAkrancsfvlsFPEKWSTQVGTRGL------QLSGGQKQRIAIARALLR------NPAF 640
Cdd:PRK13548 92 TVEEVVAMGRAPHGLSRAEDDA----------LVAAALAQVDLAHLagrdypQLSGGEQQRVQLARVLAQlwepdgPPRW 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 641 LILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK13548 162 LLLDEPTSALDlaHQHHVL--RLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
499-704 |
1.11e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRF--YAPSSGKILADGVDISTYNVHQwRSHFGL-VG-QEPVLFSG-T 573
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDE-RARAGIfLAfQYPVEIPGvS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 IGE--NIAYGKSNASQEEIEDAAKRANcsfvlsfpeKWSTQVG------TRGLQ--LSGGQKQRIAIARALLRNPAFLIL 643
Cdd:COG0396 94 VSNflRTALNARRGEELSAREFLKLLK---------EKMKELGldedflDRYVNegFSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 644 DEATSALDGEAEVMVDKTIQSlMHNRSMTTITIAH--KLATIRRADQIIVVGDGKVLEQGSFE 704
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNK-LRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
480-651 |
1.49e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 94.93 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYP-TRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwrs 558
Cdd:COG4525 2 SMLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 hfGLVGQEPVLFSG-TIGENIAYGKSNASQEEIEDAAkRAncsfvlsfpEKWSTQVGTRGL------QLSGGQKQRIAIA 631
Cdd:COG4525 79 --GVVFQKDALLPWlNVLDNVAFGLRLRGVPKAERRA-RA---------EELLALVGLADFarrriwQLSGGMRQRVGIA 146
|
170 180
....*....|....*....|
gi 19112543 632 RALLRNPAFLILDEATSALD 651
Cdd:COG4525 147 RALAADPRFLLMDEPFGALD 166
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
480-700 |
1.71e-21 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 94.87 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPT------RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNV 553
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 HQ---WRSHFGLVGQE-PVLFSG--TIGENIAYGKSNAsqEEIEDAAKRANCSFVLSFPEKWSTQVGTRGLQLSGGQKQR 627
Cdd:TIGR02769 81 KQrraFRRDVQLVFQDsPSAVNPrmTVRQIIGEPLRHL--TSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 628 IAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQ 700
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-428 |
3.99e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 94.94 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 176 PYIVGKILDAGSSGDSSVTHIMG---IPSGT-----FYIGLL-GLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCM 246
Cdd:cd18565 19 PLLIGVAIDAVFNGEASFLPLVPaslGPADPrgqlwLLGGLTvAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 247 SLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYV 326
Cdd:cd18565 99 RLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 327 RKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILAL 406
Cdd:cd18565 179 EPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVV 258
|
250 260
....*....|....*....|....*...
gi 19112543 407 GGRMVAAG------DITVGQLSSFLLYT 428
Cdd:cd18565 259 GGYWVLDGpplftgTLTVGTLVTFLFYT 286
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
482-701 |
5.20e-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: 91.87 E-value: 5.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRpsaSIFDNLSFDIHPGTnVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHFG 561
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENIAYgksNASQEEIEDAAKRANCSFVLS---FPEKWSTQVGtrglQLSGGQKQRIAIARALLRN 637
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDY---IAWLKGIPSKEVKARVDEVLElvnLGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLMHNRsmTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
499-713 |
6.56e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 6.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA----PSSGKILADGVDIStyNVHQWRSHFGLVGQEPVLFSG-T 573
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTT----LLRIIAglehQTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFRHmT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 IGENIAYGKSNASQEEIEDAAK-RANCSFVLS----------FPEkwstqvgtrglQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:PRK10851 91 VFDNIAFGLTVLPRRERPNAAAiKAKVTQLLEmvqlahladrYPA-----------QLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 643 LDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAH-KLATIRRADQIIVVGDGKVLEQGSFERLSR-PGTNF 713
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWRePATRF 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
471-713 |
9.83e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.90 E-value: 9.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 471 IPVP-VTVGKA---ILSFRNVGFAYPTRPSAsifDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGV 546
Cdd:PRK11607 5 IPRPqAKTRKAltpLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 547 DIStyNVHQWRSHFGLVGQEPVLFSG-TIGENIAYG--KSNASQEEIEDaakRANCSFVLSFPEKWSTQvgtRGLQLSGG 623
Cdd:PRK11607 82 DLS--HVPPYQRPINMMFQSYALFPHmTVEQNIAFGlkQDKLPKAEIAS---RVNEMLGLVHMQEFAKR---KPHQLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 624 QKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAH-KLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250
....*....|..
gi 19112543 703 FERL-SRPGTNF 713
Cdd:PRK11607 234 PEEIyEHPTTRY 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
482-715 |
1.11e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 92.00 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI--------LADGVDISTynV 553
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdFSQKPSEKA--I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 HQWRSHFGLVGQE----PVLfsgTIGENIAYGKSNASQEEIEDAAKRANcsFVLS------FPEKWStqvgtrgLQLSGG 623
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAM--KLLArlrltdKADRFP-------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 624 QKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNrSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
250
....*....|...
gi 19112543 703 FERLSRPGTNFYK 715
Cdd:COG4161 225 ASHFTQPQTEAFA 237
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
482-722 |
1.75e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 92.15 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAY----PTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIS--TYNVH- 554
Cdd:PRK13646 3 IRFDNVSYTYqkgtPYEHQA--IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThkTKDKYi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 555 -QWRSHFGLVGQ--EPVLFSGTIGENIAYGKSNASQ--EEIEDAAKRanCSFVLSFPEKWSTQvgtRGLQLSGGQKQRIA 629
Cdd:PRK13646 81 rPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMnlDEVKNYAHR--LLMDLGFSRDVMSQ---SPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERLSR 708
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
250
....*....|....
gi 19112543 709 PGTnfyKLMRWQLG 722
Cdd:PRK13646 236 DKK---KLADWHIG 246
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
482-715 |
2.14e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTrpSASIFDnLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGK--ILADGVDISTYN----VHQ 555
Cdd:PRK11124 3 IQLNGINCFYGA--HQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFSKTPsdkaIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQE----PVLfsgTIGENI--------AYGKSNASQEEIEDAAKRANCSFVLSFPekwstqvgtrgLQLSGG 623
Cdd:PRK11124 80 LRRNVGMVFQQynlwPHL---TVQQNLieapcrvlGLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 624 QKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmhnrSMTTIT---IAHKLATIRR-ADQIIVVGDGKVLE 699
Cdd:PRK11124 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL----AETGITqviVTHEVEVARKtASRVVYMENGHIVE 221
|
250
....*....|....*.
gi 19112543 700 QGSFERLSRPGTNFYK 715
Cdd:PRK11124 222 QGDASCFTQPQTEAFK 237
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
486-709 |
2.50e-20 |
|
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: 91.84 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 486 NVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGvDISTYNVHQWrshfglvgq 565
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RISFSSQFSW--------- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 566 epvLFSGTIGENIAYGKS----------NASQEEiEDAAKrancsfvlsFPEKWSTQVGTRGLQLSGGQKQRIAIARALL 635
Cdd:cd03291 109 ---IMPGTIKENIIFGVSydeyryksvvKACQLE-EDITK---------FPEKDNTVLGEGGITLSGGQRARISLARAVY 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 636 RNPAFLILDEATSALD--GEAEVMvDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLS--RP 709
Cdd:cd03291 176 KDADLYLLDSPFGYLDvfTEKEIF-ESCVCKLMANK--TRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQslRP 250
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
479-702 |
2.94e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.99 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPSasiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRF--YAPS---SGKILADGVDISTYNV 553
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 H--QWRSHFGLVGQEPVLFSGTIGENIAYG------KSNASQEE-IEDAAKRANCsfvlsfpekWStQVGTR----GLQL 620
Cdd:PRK14239 80 DtvDLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASI---------WD-EVKDRlhdsALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 621 SGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATiRRADQIIVVGDGKVLEQ 700
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAS-RISDRTGFFLDGDLIEY 228
|
..
gi 19112543 701 GS 702
Cdd:PRK14239 229 ND 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
482-697 |
3.97e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 90.51 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILAdgvdiSTYNVHQWRSHFG 561
Cdd:PRK11247 13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GTAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFS-GTIGENIAYGKSNASQEEIEDA------AKRANcsfvlsfpeKWSTQvgtrglqLSGGQKQRIAIARAL 634
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQAlaavglADRAN---------EWPAA-------LSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 635 LRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKV 697
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
456-701 |
4.26e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 4.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 456 FELLDAKPKIAPTVGIpvpvtvgkailSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYA 535
Cdd:PRK13536 27 SEAKASIPGSMSTVAI-----------DLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 536 PSSGKILADGVDISTyNVHQWRSHFGLVGQEPVL-FSGTIGEN-IAYGKS-NASQEEIEdaakrANCSFVLSFPeKWSTQ 612
Cdd:PRK13536 93 PDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVRENlLVFGRYfGMSTREIE-----AVIPSLLEFA-RLESK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 613 VGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRR-ADQIIV 691
Cdd:PRK13536 166 ADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCV 244
|
250
....*....|
gi 19112543 692 VGDGKVLEQG 701
Cdd:PRK13536 245 LEAGRKIAEG 254
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
500-695 |
4.53e-20 |
|
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: 89.80 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 500 FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILAD----GVDISTYNVHQW----RSHFGLVGQ------ 565
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREIlalrRRTIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 566 ---------EPVLFSGTigeniaygksnaSQEEIEDAAKRAncsfvLSF---PEK-WSTQVGTrglqLSGGQKQRIAIAR 632
Cdd:COG4778 107 rvsaldvvaEPLLERGV------------DREEARARAREL-----LARlnlPERlWDLPPAT----FSGGEQQRVNIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 633 ALLRNPAFLILDEATSALDGEA-EVMVDKtIQSLMHnRSMTTITIAHKLATIRR-ADQIIVVGDG 695
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAANrAVVVEL-IEEAKA-RGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
479-701 |
4.88e-20 |
|
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: 88.76 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPTRPSAS---IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLL--LRFYAPSSGKILADGVDISTynv 553
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 HQWRSHFGLVGQEPVLFSG-TIGENIAYgksnasqeeiedAAKrancsfvlsfpekwstqvgTRGLqlSGGQKQRIAIAR 632
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTlTVRETLMF------------AAK-------------------LRGL--SGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 633 ALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLAT--IRRADQIIVVGDGKVLEQG 701
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
481-714 |
5.07e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 94.54 E-value: 5.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAY-PTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG----------VDIS 549
Cdd:PRK10261 12 VLAVENLNIAFmQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 550 TYNVHQWRSHFG----LVGQEPV-----LFsgTIGENIAYG---KSNASQEEIEDAAKRAncSFVLSFPEKwSTQVGTRG 617
Cdd:PRK10261 92 EQSAAQMRHVRGadmaMIFQEPMtslnpVF--TVGEQIAESirlHQGASREEAMVEAKRM--LDQVRIPEA-QTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 618 LQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGE 246
|
250
....*....|....*...
gi 19112543 697 VLEQGSFERLSRPGTNFY 714
Cdd:PRK10261 247 AVETGSVEQIFHAPQHPY 264
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
480-698 |
6.92e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 6.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPT-RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW-- 556
Cdd:PRK10535 3 ALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 --RSHFGLVGQEPVLFSG-TIGENIAYGKSNASQEEIEDAAkRANCSFV-LSFPEKwstqVGTRGLQLSGGQKQRIAIAR 632
Cdd:PRK10535 83 lrREHFGFIFQRYHLLSHlTAAQNVEVPAVYAGLERKQRLL-RAQELLQrLGLEDR----VEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 633 ALLRNPAFLILDEATSALDGEA--EVMvdkTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVL 698
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSgeEVM---AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
495-695 |
7.48e-20 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 88.93 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 495 PSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSH----FGLVGQEPVLF 570
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 571 SGTIGENIAYGKSNASQ--EEIEDAakranCSF-----VLSFPEKwsTQVGTRGLQLSGGQKQRIAIARALLRNPAFLIL 643
Cdd:cd03290 92 NATVEENITFGSPFNKQryKAVTDA-----CSLqpdidLLPFGDQ--TEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 644 DEATSALDGE-AEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDG 695
Cdd:cd03290 165 DDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
501-701 |
8.49e-20 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 88.58 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHFGLV-GQEPVLFSGTIGENIA 579
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVsDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 580 Y-----G-KSNASQEEIEDAAKRancsfvLSFPEKWSTQVGtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALDge 653
Cdd:cd03266 101 YfaglyGlKGDELTARLEELADR------LGMEELLDRRVG----GFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD-- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 654 aeVMVDKTI-QSLMHNRSM--TTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03266 169 --VMATRALrEFIRQLRALgkCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
480-702 |
1.27e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 89.13 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRpsASIF--------DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTY 551
Cdd:COG4167 3 ALLEVRNLSKTFKYR--TGLFrrqqfeavKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 552 NvHQWRS-HFGLVGQEPvlfsgtigeNIAYgksNASQeeiedaakraNCSFVLSFPEKWST----------------QVG 614
Cdd:COG4167 81 D-YKYRCkHIRMIFQDP---------NTSL---NPRL----------NIGQILEEPLRLNTdltaeereerifatlrLVG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 615 TRGLQ-------LSGGQKQRIAIARALLRNPAFLILDEATSALDgeaeVMVDKTIQSLM----HNRSMTTITIAHKLATI 683
Cdd:COG4167 138 LLPEHanfyphmLSSGQKQRVALARALILQPKIIIADEALAALD----MSVRSQIINLMlelqEKLGISYIYVSQHLGIV 213
|
250 260
....*....|....*....|
gi 19112543 684 RR-ADQIIVVGDGKVLEQGS 702
Cdd:COG4167 214 KHiSDKVLVMHQGEVVEYGK 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
484-654 |
1.75e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.44 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 484 FRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDIstynvhqwrshfGL 562
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsIPKGLRI------------GY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 563 VGQEPVLFSG-TIGENI----------------AYGKSNASQEEIEDAAK-------------RANCSFVLS---FP-EK 608
Cdd:COG0488 66 LPQEPPLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAElqeefealggweaEARAEEILSglgFPeED 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19112543 609 WSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGEA 654
Cdd:COG0488 146 LDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
504-709 |
3.80e-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: 89.77 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 504 SFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA----PSSGKILADG---VDIST-YNVHQWRSHFGLVGQEPVLFSG-TI 574
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTT----LLRAIAglerPDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GENIAYGKSNASQEE-------------IEDAAKRancsfvlsFPEkwstqvgtrglQLSGGQKQRIAIARALLRNPAFL 641
Cdd:COG4148 95 RGNLLYGRKRAPRAErrisfdevvellgIGHLLDR--------RPA-----------TLSGGERQRVAIGRALLSSPRLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 642 ILDEATSALDGE--AEVMvdKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFER-LSRP 709
Cdd:COG4148 156 LMDEPLAALDLArkAEIL--PYLERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEvLSRP 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
501-708 |
4.09e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSH-FGLVGQEPVLFSG-TIGENI 578
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 579 AYGK---------SNASQEEIEDAAKRancsfvLSFPEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:COG1129 101 FLGReprrgglidWRAMRRRARELLAR------LGLDIDPDTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 650 LDG-EAEVMVDkTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERLSR 708
Cdd:COG1129 171 LTErEVERLFR-IIRRL-KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELTE 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
480-706 |
4.13e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 86.96 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKST----ISQLLlrfyAPSSGKILADGVDISTYNVHQ 555
Cdd:COG0410 2 PMLEVENLHAGYGGIH---VLHGVSLEVEEGEIVALLGRNGAGKTTllkaISGLL----PPRSGSIRFDGEDITGLPPHR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 -WRSHFGLVGQEPVLFSG-TIGENI---AYGKSNasqeeieDAAKRANCSFVLS-FP---EKWSTQVGTrglqLSGGQKQ 626
Cdd:COG0410 75 iARLGIGYVPEGRRIFPSlTVEENLllgAYARRD-------RAEVRADLERVYElFPrlkERRRQRAGT----LSGGEQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 627 RIAIARALLRNPAFLILDEATSALdgeAEVMVDK---TIQSLmhNRSMTTITIA-HKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIRRL--NREGVTILLVeQNARFALEiADRAYVLERGRIVLEG 218
|
....*
gi 19112543 702 SFERL 706
Cdd:COG0410 219 TAAEL 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
478-702 |
4.56e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.41 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 478 GKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYA------PSSGKILADGVDISTY 551
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 552 NVHQWRSHFGLVGQEPVLFSG-TIGENIAYG-KSNASQEEIEDAAKRANCSFVLSFPEKWSTQVGTRGLQLSGGQKQRIA 629
Cdd:PRK14246 84 DAIKLRKEVGMVFQQPNPFPHlSIYDNIAYPlKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLT 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmhNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
481-651 |
4.97e-19 |
|
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: 86.56 E-value: 4.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYP-TRPSASIFDNLSFDIHPGTNVAIVAPSGGGKST----ISQLLLRFYApSSGKILADGVDISTynvHQ 555
Cdd:cd03234 3 VLPWWDVGLKAKnWNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPRKP---DQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQEPVLFSG-TIGENIAYGKSNASQEEIEDAAKRANCSFVLSfPEKWSTQVGTRGLQ-LSGGQKQRIAIARA 633
Cdd:cd03234 79 FQKCVAYVRQDDILLPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLL-RDLALTRIGGNLVKgISGGERRRVSIAVQ 157
|
170
....*....|....*...
gi 19112543 634 LLRNPAFLILDEATSALD 651
Cdd:cd03234 158 LLWDPKVLILDEPTSGLD 175
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
499-717 |
5.09e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 92.28 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILadgvdistynvHQWRSHFGlvGQEPVLFSGTIGENI 578
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK-----------HSGRISFS--PQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 579 AYGKS----------NASQEEiEDAAKrancsfvlsFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATS 648
Cdd:TIGR01271 508 IFGLSydeyrytsviKACQLE-EDIAL---------FPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 649 ALD--GEAEVMvDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRPGTNFYKLM 717
Cdd:TIGR01271 578 HLDvvTEKEIF-ESCLCKLMSNK--TRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
481-702 |
5.92e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.87 E-value: 5.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAY-PTRPSAS--IFDnLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDISTYN---V 553
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPFASraLFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtVGDIVVSSTSKqkeI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 HQWRSHFGLVGQEP--VLFSGTIGENIAYGKSN--ASQEEIEDAAKRANCSFVLSfPEKWSTQvgtrGLQLSGGQKQRIA 629
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLA-DEFWEKS----PFELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
501-701 |
6.31e-19 |
|
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: 85.80 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG--VDISTYNvhqwrsHFGLVGQEPVLFSG-TIGEN 577
Cdd:cd03269 17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAARN------RIGYLPEERGLYPKmKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 IAY-------GKSNAsQEEIEDAAKRancsFVLSfpEKWSTQVGtrglQLSGGQKQRIAIARALLRNPAFLILDEATSAL 650
Cdd:cd03269 91 LVYlaqlkglKKEEA-RRRIDEWLER----LELS--EYANKRVE----ELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 651 DG-EAEVMVDKtIQSLMHNRSmTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03269 160 DPvNVELLKDV-IRELARAGK-TVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
501-697 |
6.46e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG--VDISTYN---------VHQwrsHFGLVgqePVL 569
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRdaialgigmVHQ---HFMLV---PNL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 570 fsgTIGENIAYGKSNASQ---------EEIEDAAKRancsfvLSFPEKWSTQVGtrglQLSGGQKQRIAIARALLRNPAF 640
Cdd:COG3845 96 ---TVAENIVLGLEPTKGgrldrkaarARIRELSER------YGLDVDPDAKVE----DLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 641 LILDEATSAL-DGEAE-------VMVD--KTIqslmhnrsmttITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:COG3845 163 LILDEPTAVLtPQEADelfeilrRLAAegKSI-----------IFITHKLREVMAiADRVTVLRRGKV 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-709 |
6.58e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.89 E-value: 6.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 496 SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFY-----APSSGKILADGVDISTYNVHQWRSHFGLVGQEP-VL 569
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 570 FSGTIGENIAYG-KSN---ASQEEIEDAAKRAncsfvLSFPEKWS---TQVGTRGLQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:PRK14247 95 PNLSIFENVALGlKLNrlvKSKKELQERVRWA-----LEKAQLWDevkDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 643 LDEATSALDGEAEVMVDKTIQSLmhNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSF-ERLSRP 709
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTrEVFTNP 236
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
486-707 |
6.69e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 486 NVGFAYPTRPSASI--FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIST-----YNVHQWRS 558
Cdd:PRK13645 11 NVSYTYAKKTPFEFkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEP--VLFSGTIGENIAYGKSNASQEEIEDAAKRANCSFVLSFPEKWSTQvgtRGLQLSGGQKQRIAIARALLR 636
Cdd:PRK13645 91 EIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKR---SPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 637 NPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS-FERLS 707
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSpFEIFS 240
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
503-708 |
9.28e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 88.63 E-value: 9.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 503 LSFDIhPGTNV-AIVAPSGGGKSTISQLLLRFYAPSSGKILADG---------VDISTynvHQWRshFGLVGQEPVLFSG 572
Cdd:TIGR02142 16 ADFTL-PGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgIFLPP---EKRR--IGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 -TIGENIAYG--KSNASQEEIEDAAKRAncsfVLSFpekwSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:TIGR02142 90 lSVRGNLRYGmkRARPSERRISFERVIE----LLGI----GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 650 LDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERLSR 708
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
481-701 |
1.38e-18 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 86.13 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSasiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKIL---ADGVDISTYNV---- 553
Cdd:PRK11701 6 LLSVRGLTKLYGPRKG---CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRDLYALseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 --HQWRSHFGLVGQEP-------VLFSGTIGENIA------YGK--SNASQ--EEIEDAAKRANcsfvlSFPEkwstqvg 614
Cdd:PRK11701 83 rrRLLRTEWGFVHQHPrdglrmqVSAGGNIGERLMavgarhYGDirATAGDwlERVEIDAARID-----DLPT------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 615 trglQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIR-RADQIIVVG 693
Cdd:PRK11701 151 ----TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVMK 226
|
....*...
gi 19112543 694 DGKVLEQG 701
Cdd:PRK11701 227 QGRVVESG 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
504-715 |
1.64e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 504 SFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWR-----------SHFGLVGQEPVLFSG 572
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIAYGKSNASQEEIEDAAKRANC-SFVLSFPEkwstqvgtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALD 651
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLeNYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 652 GEAEVMVDKTIQSLMHNRSMTTITIAHKL-ATIRRADQIIVVGDGKVLEQGS-FERLSRPGTNFYK 715
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTpDEILNNPANDYVR 262
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
490-706 |
1.64e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 87.45 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 490 AYPTRPSASI--FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW---RSHFGLVG 564
Cdd:PRK15079 25 QWFWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 565 QEPvLFS----GTIGENIA-----YgKSNASQEEIEDAAKrANCSFVLSFPEkwstQVGTRGLQLSGGQKQRIAIARALL 635
Cdd:PRK15079 105 QDP-LASlnprMTIGEIIAeplrtY-HPKLSRQEVKDRVK-AMMLKVGLLPN----LINRYPHEFSGGQCQRIGIARALI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 636 RNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK15079 178 LEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
502-702 |
2.27e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.60 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFDIHPGTNVAIVAPSGGGKSTIsqllLRFY---------APSSGKILADGVDISTYNVH--QWRSHFGLVGQEPVLF 570
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTI----LRCFnrlndlipgFRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 571 SGTIGENIAYG-KSNASQEEIEDAAKRANCSFVLsfpekWST---QVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEA 646
Cdd:PRK14243 104 PKSIYDNIAYGaRINGYKGDMDELVERSLRQAAL-----WDEvkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 647 TSALDGEAEVMVDKTIQSLmhNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK14243 179 CSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-697 |
2.32e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.52 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRSHF-GLVGQEPVL---FSGTI 574
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RAKYiGRVFQDPMMgtaPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GEN--IAY----------GKSNASQEEIEDAAKRANcsfvLSFPEKWSTQVGtrglQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:COG1101 100 EENlaLAYrrgkrrglrrGLTKKRRELFRELLATLG----LGLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 643 LDEATSALD-GEAEVMVDKTiQSLMHNRSMTTITIAHKL--AtIRRADQIIVVGDGKV 697
Cdd:COG1101 172 LDEHTAALDpKTAALVLELT-EKIVEENNLTTLMVTHNMeqA-LDYGNRLIMMHEGRI 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
482-718 |
2.44e-18 |
|
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: 90.39 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYpTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGvdistynvhqwrsHFG 561
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVA 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSGTIGENIAYGKS---NASQEEIEDAAKRANCSFVlsfPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNP 638
Cdd:TIGR00957 703 YVPQQAWIQNDSLRENILFGKAlneKYYQQVLEACALLPDLEIL---PSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 639 AFLILDEATSALDGE-AEVMVDKTI--QSLMHNRsmTTITIAHKLATIRRADQIIVVGDGKVLEQGSF-ERLSRPGTnFY 714
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNK--TRILVTHGISYLPQVDVIIVMSGGKISEMGSYqELLQRDGA-FA 856
|
....
gi 19112543 715 KLMR 718
Cdd:TIGR00957 857 EFLR 860
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
480-702 |
2.44e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSH 559
Cdd:PRK13537 6 APIDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 560 FGLVGQ----EPVLfsgTIGENI-AYGKSNAsqeeIEDAAKRANCSFVLSFP---EKWSTQVGtrglQLSGGQKQRIAIA 631
Cdd:PRK13537 82 VGVVPQfdnlDPDF---TVRENLlVFGRYFG----LSAAAARALVPPLLEFAkleNKADAKVG----ELSGGMKRRLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 632 RALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGA 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
480-711 |
2.84e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.22 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW-RS 558
Cdd:PRK10575 10 TTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFaRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSGTIGENIAYGK----------SNASQEEIEDAAkrancsfvlsfpekwsTQVGTRGL------QLSG 622
Cdd:PRK10575 87 VAYLPQQLPAAEGMTVRELVAIGRypwhgalgrfGAADREKVEEAI----------------SLVGLKPLahrlvdSLSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 623 GQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKL-ATIRRADQIIVVGDGKVLEQG 701
Cdd:PRK10575 151 GERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDInMAARYCDYLVALRGGEMIAQG 230
|
250
....*....|
gi 19112543 702 SFERLSRPGT 711
Cdd:PRK10575 231 TPAELMRGET 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
499-704 |
5.90e-18 |
|
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: 82.57 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRF--YAPSSGKILADGVDISTYNVHQwRSHFG--LVGQEPVLFSG-T 573
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGifLAFQYPPEIPGvK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 IGENIAYgksnasqeeiedaakrANCSFvlsfpekwstqvgtrglqlSGGQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:cd03217 94 NADFLRY----------------VNEGF-------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 654 AEVMVDKTIQSLmHNRSMTTITIAH--KLATIRRADQIIVVGDGKVLEQGSFE 704
Cdd:cd03217 139 ALRLVAEVINKL-REEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
475-708 |
9.89e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 9.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 475 VTVGKAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG---VDISTY 551
Cdd:PRK15439 5 DTTAPPLLCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 552 NVHQwrshFG--LVGQEPVLFSG-TIGENIAYG--KSNASQEEIEDAAKRANCSFVLSfpekwsTQVGTrglqLSGGQKQ 626
Cdd:PRK15439 82 KAHQ----LGiyLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQLDLD------SSAGS----LEVADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 627 RIAIARALLRNPAFLILDEATSALD-GEAEVMVDKtIQSLMhNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFE 704
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTpAETERLFSR-IRELL-AQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTA 225
|
....
gi 19112543 705 RLSR 708
Cdd:PRK15439 226 DLST 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
475-717 |
1.19e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 475 VTVGKAILSFRNVGFAYPTRpsASIF----------DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILAD 544
Cdd:PRK10261 307 VVDGEPILQVRNLVTRFPLR--SGLLnrvtrevhavEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFN 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 545 GVDIST---YNVHQWRSHFGLVGQEPVLF---SGTIGENIAYGKSNASQEEIEDAAKRAncSFVLSfpekwstQVGTRG- 617
Cdd:PRK10261 385 GQRIDTlspGKLQALRRDIQFIFQDPYASldpRQTVGDSIMEPLRVHGLLPGKAAAARV--AWLLE-------RVGLLPe 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 618 ------LQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQII 690
Cdd:PRK10261 456 hawrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVA 535
|
250 260 270
....*....|....*....|....*....|.
gi 19112543 691 VVGDGKVLEQGS----FERLSRPGTNfyKLM 717
Cdd:PRK10261 536 VMYLGQIVEIGPrravFENPQHPYTR--KLM 564
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
156-429 |
2.09e-17 |
|
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: 83.30 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 156 WNFFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSsvthIMGIPsgtFYIGLLGLFFLGSACNFGRIITLR-LLSERIV 234
Cdd:cd18540 2 KLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGT----LDGLT---GFILLYLGLILIQALSVFLFIRLAgKIEMGVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 235 SRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPP 314
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 315 IALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGF 394
Cdd:cd18540 155 LAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLF 234
|
250 260 270
....*....|....*....|....*....|....*
gi 19112543 395 LGNATVIAILALGGRMVAAGDITVGQLSSFLLYTV 429
Cdd:cd18540 235 LGSIATALVLWYGGILVLAGAITIGTLVAFISYAT 269
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
480-645 |
3.07e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTIsqlllrFY------APSSGKILADGVDISTYNV 553
Cdd:COG1137 2 MTLEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 HQwRSHFGLvG---QEPVLFSG-TIGENIA-----YGKSNASQEEIEDA-------AKRANcsfvlsfpekwstqvgTRG 617
Cdd:COG1137 73 HK-RARLGI-GylpQEASIFRKlTVEDNILavlelRKLSKKEREERLEElleefgiTHLRK----------------SKA 134
|
170 180
....*....|....*....|....*...
gi 19112543 618 LQLSGGQKQRIAIARALLRNPAFLILDE 645
Cdd:COG1137 135 YSLSGGERRRVEIARALATNPKFILLDE 162
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
501-702 |
4.65e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 82.46 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStynvHQWRSHFGLVGQEPVLFSG-TIGENIA 579
Cdd:COG4152 18 DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGYLPEERGLYPKmKVGEQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 580 Y-----GKS-NASQEEIEDAAKRancsfvLSFPEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:COG4152 94 YlarlkGLSkAEAKRRADEWLER------LGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 654 -AEVMVDkTIQSLmhNRSMTTItI--AHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:COG4152 164 nVELLKD-VIREL--AAKGTTV-IfsSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
502-721 |
7.03e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.60 E-value: 7.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADgvdistynvhqwRShFGLVGQEPVLFSGTIGENIAYg 581
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNILF- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 582 ksnASQEEIEDAAKRANCSF----VLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGE-AEV 656
Cdd:PTZ00243 744 ---FDEEDAARLADAVRVSQleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 657 MVDKTIqsLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFERLSRpgTNFYKLMRWQL 721
Cdd:PTZ00243 821 VVEECF--LGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR--TSLYATLAAEL 881
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
159-455 |
9.25e-17 |
|
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: 81.94 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 159 FIAGSLLLVSSGVTMSIPYIV-GKILDAGSSG--------DSSVTHIMGIP------SGTFYIGLLGLFFLGSACNFGRI 223
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIfGDMTDSFTNGgmtnitgnSSGLNSSAGPFekleeeMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 224 ITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMR 303
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 304 LTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAF 383
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 384 ASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
498-702 |
1.29e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 498 SIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVLFSG-TIGE 576
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 577 NIAYGKSNAS------QEEIEDAAKRANCSFVLSFPEKWSTQVgtrglqLSGGQKQRIAIARALLRNPAFLILDEATSAL 650
Cdd:PRK10253 101 LVARGRYPHQplftrwRKEDEEAVTKAMQATGITHLADQSVDT------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 651 DGEAEVMVDKTIQSLMHNRSMTTITIAHKL-ATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGA 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
501-696 |
1.83e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYaPS---SGKILADGVDISTYNVHQW-RSHFGLVGQEPVLFSG-TIG 575
Cdd:PRK13549 22 DNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 576 ENIAYGKSNASQEEIEDAAKRANCsfvlsfpEKWSTQVG------TRGLQLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:PRK13549 101 ENIFLGNEITPGGIMDYDAMYLRA-------QKLLAQLKldinpaTPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19112543 650 L-DGEAEVMVDkTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:PRK13549 174 LtESETAVLLD-IIRDL-KAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
487-706 |
3.70e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.37 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 487 VGFAYPTrpsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSG-----KILADGVDISTY-NVHQWRSHF 560
Cdd:PRK14271 29 LGFAGKT-----VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSGTIGENIAYGKSnaSQEEIEDAAKRANCSFVLSFPEKWST---QVGTRGLQLSGGQKQRIAIARALLRN 637
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVLAGVR--AHKLVPRKEFRGVAQARLTEVGLWDAvkdRLSDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLMHNrsMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
480-702 |
4.49e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVH-QWRS 558
Cdd:PRK10895 2 ATLTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEPVLFSG-TIGENIAYG---KSNASQEEIEDAAKRANCSFVLSFPEKwstqvgTRGLQLSGGQKQRIAIARAL 634
Cdd:PRK10895 79 GIGYLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRD------SMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 635 LRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
501-706 |
6.68e-16 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 77.41 E-value: 6.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIS--TYNVhqwRSHFGLVGQEPVLFSGTIG-EN 577
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVrePREV---RRRIGIVFQDLSVDDELTGwEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 IA-----YGKSNAS-QEEIEDaakrancsfVLSFPEKWST---QVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATS 648
Cdd:cd03265 94 LYiharlYGVPGAErRERIDE---------LLDFVGLLEAadrLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 649 ALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
501-707 |
1.01e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.59 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-------------------LADGVDISTY-----NVHQW 556
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekvLEKLVIQKTRfkkikKIKEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RSHFGLVGQ--EPVLFSGTIGENIAYGKSNASQEEiEDAAKRAncsfvlsfpEKWSTQVG--TRGLQ-----LSGGQKQR 627
Cdd:PRK13651 104 RRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRA---------AKYIELVGldESYLQrspfeLSGGQKRR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 628 IAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATI-RRADQIIVVGDGKVLEQG-SFER 705
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGdTYDI 252
|
..
gi 19112543 706 LS 707
Cdd:PRK13651 253 LS 254
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
481-651 |
1.03e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwrshf 560
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQ-EPVLFSGTIGENIAYGKSNA--SQEEIEDAAKRANCSFVLSFPEK---WstqvgtrglQLSGGQKQRIAIARAL 634
Cdd:PRK11248 73 GVVFQnEGLLPWRNVQDNVAFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKryiW---------QLSGGQRQRVGIARAL 143
|
170
....*....|....*..
gi 19112543 635 LRNPAFLILDEATSALD 651
Cdd:PRK11248 144 AANPQLLLLDEPFGALD 160
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
485-706 |
1.48e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.50 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 485 RNVGFaypTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDI---STYNVHQWRSHFG 561
Cdd:PRK11831 11 RGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSG-TIGENIAYGKSNASQeeIEDAAKRANCSFVLSfpekwstQVGTRGL------QLSGGQKQRIAIARAL 634
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLREHTQ--LPAPLLHSTVMMKLE-------AVGLRGAaklmpsELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 635 LRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
501-701 |
1.83e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHfGLVG--QEPVLF-SGTIGEN 577
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM-GVVRtfQHVRLFrEMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 I--------------------AYGKsnASQEEIEDAAkrancsfvlsfpeKWSTQVGTRGL------QLSGGQKQRIAIA 631
Cdd:PRK11300 101 LlvaqhqqlktglfsgllktpAFRR--AESEALDRAA-------------TWLERVGLLEHanrqagNLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 632 RALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
479-702 |
2.33e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVG--FAYPT----RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIsTYN 552
Cdd:PRK15112 2 ETLLEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 VHQWRSH-FGLVGQEPvlfSGTIgeniaygksNASQE--EIEDAAKRANCSFVLSFPEKWST----QVGTRGLQ------ 619
Cdd:PRK15112 81 DYSYRSQrIRMIFQDP---STSL---------NPRQRisQILDFPLRLNTDLEPEQREKQIIetlrQVGLLPDHasyyph 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 -LSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:PRK15112 149 mLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEV 228
|
....*
gi 19112543 698 LEQGS 702
Cdd:PRK15112 229 VERGS 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
481-697 |
2.82e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 75.68 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIS---TYNVHQWR 557
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQE---------------PVLFSGTIGENIAYGKSNA-SQEEIEDAAKrancsfvlSFPekwstqvgtrgLQLS 621
Cdd:PRK10908 79 RQIGMIFQDhhllmdrtvydnvaiPLIIAGASGDDIRRRVSAAlDKVGLLDKAK--------NFP-----------IQLS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 622 GGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmhNRSMTTITIA-HKLATI-RRADQIIVVGDGKV 697
Cdd:PRK10908 140 GGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRVGVTVLMAtHDIGLIsRRSYRMLTLSDGHL 215
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
490-690 |
3.29e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.58 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 490 AYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYnVHQwRSHfglvgqEPVL 569
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAY-VPQ-RSE------VPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 570 FSGTIGENIAYGK----------SNASQEEIEDAAKRancsfvlsfpekwstqVGTRGL------QLSGGQKQRIAIARA 633
Cdd:NF040873 70 LPLTVRDLVAMGRwarrglwrrlTRDDRAAVDDALER----------------VGLADLagrqlgELSGGQRQRALLAQG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 634 LLRNPAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRRADQII 690
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCV 189
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
499-708 |
3.48e-15 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 75.25 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRSHFGLV----GQE--PVLfsg 572
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIAyvpqGREifPRL--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIAYGKSN---ASQEEIEDAakrancsFVLsFPekwstqV-----GTRGLQLSGGQKQRIAIARALLRNPAFLILD 644
Cdd:TIGR03410 91 TVEENLLTGLAAlprRSRKIPDEI-------YEL-FP------VlkemlGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 645 EATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERLSR 708
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDE 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
475-701 |
4.34e-15 |
|
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: 78.69 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 475 VTVGKAILSFRNVGFAYPT--RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILA----DGVDI 548
Cdd:TIGR03269 273 VEVGEPIIKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 549 STYNVH---QWRSHFGLVGQEPVLFS-GTIGENIaygkSNASQEEIEDAAKRANCSFVL---SFPEKWSTQVGTR-GLQL 620
Cdd:TIGR03269 353 TKPGPDgrgRAKRYIGILHQEYDLYPhRTVLDNL----TEAIGLELPDELARMKAVITLkmvGFDEEKAEEILDKyPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 621 SGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLE 699
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVK 508
|
..
gi 19112543 700 QG 701
Cdd:TIGR03269 509 IG 510
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
482-696 |
4.47e-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: 72.87 E-value: 4.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGvdistynvhqwrshfg 561
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 lvgqepvlfsgtiGENIAYgksnasqeeiedaakrancsfvlsFPekwstqvgtrglQLSGGQKQRIAIARALLRNPAFL 641
Cdd:cd03221 62 -------------TVKIGY------------------------FE------------QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 642 ILDEATSALDGEaevmvdkTIQSL---MHNRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:cd03221 93 LLDEPTNHLDLE-------SIEALeeaLKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
478-697 |
4.69e-15 |
|
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: 74.01 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 478 GKAILSFRNVgfaypTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW- 556
Cdd:cd03215 1 GEPVLEVRGL-----SVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 ----------RSHFGLVGQEPvlfsgtIGENIAygksnasqeeiedaakrancsfvLSFpekwstqvgtrglQLSGGQKQ 626
Cdd:cd03215 74 ragiayvpedRKREGLVLDLS------VAENIA-----------------------LSS-------------LLSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 627 RIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA-DAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
501-702 |
9.39e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.04 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTI----SQLLLRFYAPSSGKILADGVDISTY------------NVHQWRSHFGLVG 564
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLvthfNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkikNFKELRRRVSMVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 565 QEP--VLFSGTIGENIAYGKSNASQEEIEdAAKRAncSFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLI 642
Cdd:PRK13631 123 QFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLA--KFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 643 LDEATSALD--GEAEvMVDKTIQSLMHNRsmTTITIAHKLATIRR-ADQIIVVGDGKVLEQGS 702
Cdd:PRK13631 200 FDEPTAGLDpkGEHE-MMQLILDAKANNK--TVFVITHTMEHVLEvADEVIVMDKGKILKTGT 259
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
499-663 |
9.55e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.75 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIsTYNVHQWRSHFglVGQ----EPVLfsgTI 574
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-DDPDVAEACHY--LGHrnamKPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GENIAYGKS--NASQEEIEDAAKRANCSFVLSFPEKWstqvgtrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDG 652
Cdd:PRK13539 91 AENLEFWAAflGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170
....*....|.
gi 19112543 653 EAEVMVDKTIQ 663
Cdd:PRK13539 161 AAVALFAELIR 171
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
501-709 |
1.13e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYaPS------SGKILADGVDISTYNVHQWRSHFG----LVGQEPVLF 570
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPMVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 571 SG---TIGENIAYGKS-------NASQEE---------IEDAAKRANcsfvlSFPEkwstqvgtrglQLSGGQKQRIAIA 631
Cdd:PRK15134 105 LNplhTLEKQLYEVLSlhrgmrrEAARGEilncldrvgIRQAAKRLT-----DYPH-----------QLSGGERQRVMIA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 632 RALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL-SRP 709
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLfSAP 248
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
496-700 |
1.14e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.08 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 496 SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVH---QWRSH-FGLVGQ-EPVLF 570
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRNQkLGFIYQfHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 571 SGTIGENIAY----GKSNASQeeiedAAKRANCSFVLSFPEKWSTQvgtRGLQLSGGQKQRIAIARALLRNPAFLILDEA 646
Cdd:PRK11629 101 DFTALENVAMplliGKKKPAE-----INSRALEMLAAVGLEHRANH---RPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19112543 647 TSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQ 700
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
499-654 |
1.45e-14 |
|
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: 72.78 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQ-----WRSHfgLVGQEPVLfsgT 573
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPhenilYLGH--LPGLKPEL---S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 IGENIAYGK--SNASQEEIEDAAkrancsfvlsfpekwsTQVGTRGL------QLSGGQKQRIAIARALLRNPAFLILDE 645
Cdd:TIGR01189 90 ALENLHFWAaiHGGAQRTIEDAL----------------AAVGLTGFedlpaaQLSAGQQRRLALARLWLSRRPLWILDE 153
|
....*....
gi 19112543 646 ATSALDGEA 654
Cdd:TIGR01189 154 PTTALDKAG 162
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
482-699 |
2.38e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 76.55 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 482 LSFRNVGFAYPTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG 561
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 562 LVGQEPVLFSGTIGEniayGKSNASQEEIEDAAKRancsfvLSFPEKWSTQVGT-RGLQLSGGQKQRIAIARALLRNPAF 640
Cdd:PRK10522 401 AVFTDFHLFDQLLGP----EGKPANPALVEKWLER------LKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 641 LILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLE 699
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
480-701 |
2.54e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.07 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTrpsASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYAP----SSGKILADGVDIStyNVHQ 555
Cdd:PRK11000 2 ASVTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKST----LLRMIAGlediTSGDLFIGEKRMN--DVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQEPVLFSG-TIGENIAYGK--SNASQEEIEdaaKRANcsfvlsfpekwstQVgTRGLQL-----------S 621
Cdd:PRK11000 73 AERGVGMVFQSYALYPHlSVAENMSFGLklAGAKKEEIN---QRVN-------------QV-AEVLQLahlldrkpkalS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 622 GGQKQRIAIARALLRNPAFLILDEATSALDgeAEVMVDKTIQ-SLMHNR-SMTTITIAH-KLATIRRADQIIVVGDGKVL 698
Cdd:PRK11000 136 GGQRQRVAIGRTLVAEPSVFLLDEPLSNLD--AALRVQMRIEiSRLHKRlGRTMIYVTHdQVEAMTLADKIVVLDAGRVA 213
|
...
gi 19112543 699 EQG 701
Cdd:PRK11000 214 QVG 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
499-706 |
3.74e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 73.08 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIS----------TYNVHQW---RSHFGLVGQ 565
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkVADKNQLrllRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 566 EPVLFSG-TIGENIAYGKSNASQEEIEDAAKRAncsfvlsfpEKWSTQVGTRG-------LQLSGGQKQRIAIARALLRN 637
Cdd:PRK10619 100 HFNLWSHmTVLENVMEAPIQVLGLSKQEARERA---------VKYLAKVGIDEraqgkypVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLMHnRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAE-EGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
499-701 |
4.78e-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: 71.79 E-value: 4.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGvDIStynvhqWRSHFG------LVGQEPVLFSG 572
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVS------SLLGLGggfnpeLTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIgeniaYGKSNASQEEIEDaakrancsFVLSF---PEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:cd03220 110 RL-----LGLSRKEIDEKID--------EIIEFselGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 650 ldGEAEVMvDKTIQSL--MHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03220 173 --GDAAFQ-EKCQRRLreLLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
501-710 |
5.04e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 5.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAP----SSGKILADGVDI------------------STYN-VHQWR 557
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapcalrgrkiatimqnprSAFNpLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHfglvGQEPVLFSGTIGeniaygkSNASQEEIEDAAKRANCSFVL-SFPekwstqvgtrgLQLSGGQKQRIAIARALLR 636
Cdd:PRK10418 100 TH----ARETCLALGKPA-------DDATLTAALEAVGLENAARVLkLYP-----------FEMSGGMLQRMMIALALLC 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 637 NPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL-SRPG 710
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLfNAPK 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
481-713 |
5.82e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.73 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG--VDISTYNVHQWRS 558
Cdd:PRK13638 1 MLATSDLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 HFGLVGQEP--VLFSGTIGENIAYGKSNASQEEiEDAAKRANCSFVLSFPEKWSTQvgtrGLQ-LSGGQKQRIAIARALL 635
Cdd:PRK13638 78 QVATVFQDPeqQIFYTDIDSDIAFSLRNLGVPE-AEITRRVDEALTLVDAQHFRHQ----PIQcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 636 RNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITiAHKLATIRR-ADQIIVVGDGKVLEQGSferlsrPGTNF 713
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIS-SHDIDLIYEiSDAVYVLRQGQILTHGA------PGEVF 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
474-703 |
8.54e-14 |
|
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: 74.48 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 474 PVTVGKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFY-APSSGKILADGVDISTYN 552
Cdd:TIGR02633 250 PHEIGDVILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDIRN 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 -----------VHQWRSHFGLVgqePVLfsgTIGENIAYG--KSNASQEEIEDAAKRancSFVLSFPEKWSTQVGTRGL- 618
Cdd:TIGR02633 330 paqairagiamVPEDRKRHGIV---PIL---GVGKNITLSvlKSFCFKMRIDAAAEL---QIIGSAIQRLKVKTASPFLp 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 --QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHnRSMTTITIAHKLATIRR-ADQIIVVGDG 695
Cdd:TIGR02633 401 igRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGlSDRVLVIGEG 479
|
....*...
gi 19112543 696 KVleQGSF 703
Cdd:TIGR02633 480 KL--KGDF 485
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
493-711 |
9.90e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 9.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 493 TRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGLVGQEPVL-FS 571
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 572 GTIGENIAYGKS----------NASQEEIEDAAKRANcsfVLSFPEKWSTQvgtrglqLSGGQKQRIAIARALLRNPAFL 641
Cdd:PRK09536 92 FDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTG---VAQFADRPVTS-------LSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 642 ILDEATSALDgeaevmVDKTIQSLMHNRSM-----TTITIAHKL-ATIRRADQIIVVGDGKVLEQGSFERLSRPGT 711
Cdd:PRK09536 162 LLDEPTASLD------INHQVRTLELVRRLvddgkTAVAAIHDLdLAARYCDELVLLADGRVRAAGPPADVLTADT 231
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
481-680 |
1.06e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADgvdistynvHQWRshF 560
Cdd:PRK09544 4 LVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--I 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSG---TIGENIAYgKSNASQEEIEDAAKRANCSFVLSFPEKwstqvgtrglQLSGGQKQRIAIARALLRN 637
Cdd:PRK09544 70 GYVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQ----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19112543 638 PAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKL 680
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
485-702 |
1.34e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 485 RNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKST----ISQLLlrfyAPSSGKILADGVDISTYNVHQWRSHF 560
Cdd:COG4604 5 KNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTllsmISRLL----PPDSGEVLVDGLDVATTPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSG-TIGENIAYGK--------SNASQEEIEDAAKRancsFVLsfpekwsTQVGTRGL-QLSGGQKQRIAI 630
Cdd:COG4604 78 AILRQENHINSRlTVRELVAFGRfpyskgrlTAEDREIIDEAIAY----LDL-------EDLADRYLdELSGGQRQRAFI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 631 ARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKL-ATIRRADQIIVVGDGKVLEQGS 702
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDInFASCYADHIVAMKDGRVVAQGT 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
473-706 |
1.56e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.93 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 473 VPVTVGKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqLL--LRFYAPS----SGKILADGV 546
Cdd:TIGR00955 14 VAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTT---LMnaLAFRSPKgvkgSGSVLLNGM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 547 --------DISTYnVHQWRSHFG-LVGQEPVLFSGTI--GENIAYGKSNASQEEIEDAAKRANCSfvlsfpekwSTQVGT 615
Cdd:TIGR00955 91 pidakemrAISAY-VQQDDLFIPtLTVREHLMFQAHLrmPRRVTKKEKRERVDEVLQALGLRKCA---------NTRIGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 616 RGLQ--LSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATI-RRADQIIVV 692
Cdd:TIGR00955 161 PGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfELFDKIILM 240
|
250
....*....|....
gi 19112543 693 GDGKVLEQGSFERL 706
Cdd:TIGR00955 241 AEGRVAYLGSPDQA 254
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
501-706 |
1.67e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKST----ISQLLLrfyaPSSGKILADGVDIstynvhqWR------SHFGLV-GQE--- 566
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRVLGYVP-------FKrrkefaRRIGVVfGQRsql 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 567 ----PVLFSGTIGENIaYgksnasqeEIEDAAKRAN---CSFVLSFPEKWSTQVgtRglQLSGGQKQRIAIARALLRNPA 639
Cdd:COG4586 108 wwdlPAIDSFRLLKAI-Y--------RIPDAEYKKRldeLVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 640 FLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEEL 242
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
156-455 |
2.60e-13 |
|
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: 71.30 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 156 WNFFIAgsllLVSSGVTMSIPYIVGKILD---AGSSG--DSSVTHIMGIPSGTFYIGLlglfFLGSACNFGRIITLRLLS 230
Cdd:cd18554 3 ITIVIG----LVRFGIPLLLPLILKYIVDdviQGSSLtlDEKVYKLFTIIGIMFFIFL----ILRPPVEYYRQYFAQWIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 231 ERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSL 310
Cdd:cd18554 75 NKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 311 IVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFG 390
Cdd:cd18554 155 IFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFS 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 391 STGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18554 235 AVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
479-701 |
2.78e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.91 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPtrpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQ-WR 557
Cdd:PRK11614 3 KVMLSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 558 SHFGLVGQEPVLFSG-TIGENIAYGKSNASQEEIEDAAKRANCSFVLSFpEKWSTQVGTrglqLSGGQKQRIAIARALLR 636
Cdd:PRK11614 80 EAVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYELFPRLH-ERRIQRAGT----MSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 637 NPAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTTITIAhklatiRRADQIIVVGD-GKVLEQG 701
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVE------QNANQALKLADrGYVLENG 213
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
160-455 |
3.12e-13 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 70.94 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 160 IAGSLLLVSSGVTMSI--PYIVGKILdagSSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:cd18570 8 LLLSLLITLLGIAGSFffQILIDDII---PSGDINLLNIISI-------GLILLYLFQSLLSYIRSYLLLKLSQKLDIRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTtDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIAL 317
Cdd:cd18570 78 ILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 318 GAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVN----RYNDYIRNLFVLAKREAFASGIffgsTG 393
Cdd:cd18570 157 IILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKkiekKFSKLLKKSFKLGKLSNLQSSI----KG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 394 FLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
480-713 |
4.03e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.41 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPTRpsASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYAP----SSGKILADG--V------- 546
Cdd:PRK11650 2 AGLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKST----LLRMVAGleriTSGEIWIGGrvVnelepad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 547 -DIStynvhqwrshfgLVGQEPVLFSG-TIGENIAYGKSNA--SQEEIE----DAAKrancsfVL---SFPEKwstqvgt 615
Cdd:PRK11650 76 rDIA------------MVFQNYALYPHmSVRENMAYGLKIRgmPKAEIEervaEAAR------ILelePLLDR------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 616 RGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLmHNRSMTT-ITIAH-KLATIRRADQIIVVG 693
Cdd:PRK11650 131 KPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRL-HRRLKTTsLYVTHdQVEAMTLADRVVVMN 209
|
250 260
....*....|....*....|..
gi 19112543 694 DGkVLEQ-GS-FERLSRPGTNF 713
Cdd:PRK11650 210 GG-VAEQiGTpVEVYEKPASTF 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
503-717 |
5.47e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 5.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 503 LSFDIHPGTNVAIVAPSGGGKST----ISQLLlrfyaPSSGKILADGVDISTYNVHQWRSHFG-LVGQEPVLFSGTIGEN 577
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAyLSQQQTPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 IA-YGKSNASQEEIEDAAKRAnCSFvLSFPEKWSTQVGtrglQLSGGQKQRIAIARALLR-----NPA--FLILDEATSA 649
Cdd:PRK03695 90 LTlHQPDKTRTEAVASALNEV-AEA-LGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPAgqLLLLDEPMNS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 650 LDGEAEVMVDKTIqSLMHNRSMTTITIAHKLA-TIRRADQIIVVGDGKVLEQGSF------ERLSRP-GTNFYKLM 717
Cdd:PRK03695 164 LDVAQQAALDRLL-SELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRdevltpENLAQVfGVNFRRLD 238
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
478-703 |
8.58e-13 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 71.81 E-value: 8.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 478 GKAILSFRNVGFAYPTRPSasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKIL-ADGVDISTYNVHqw 556
Cdd:PLN03073 505 GPPIISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrSAKVRMAVFSQH-- 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 rsHF-GL-VGQEPVLFsgtigenIAYGKSNASQEEIedaakRANC-SFVLSfpekwstqvGTRGLQ----LSGGQKQRIA 629
Cdd:PLN03073 581 --HVdGLdLSSNPLLY-------MMRCFPGVPEQKL-----RAHLgSFGVT---------GNLALQpmytLSGGQKSRVA 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 630 IARALLRNPAFLILDEATSALDGEAevmVDKTIQSLMHNRSmTTITIAHKLATIR-RADQIIVVGDGKVLE-QGSF 703
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVLFQG-GVLMVSHDEHLISgSVDELWVVSEGKVTPfHGTF 709
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
514-706 |
1.03e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 514 AIVAPSGGGKSTISQLLLRFY-----APSSGKILADGVDISTYNVH--QWRSHFGLVGQEPVLFSG-TIGENIAYG-KSN 584
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFPHlTIYDNVAIGvKLN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 585 A---SQEEIED----AAKRAncsfvlSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVM 657
Cdd:PRK14267 114 GlvkSKKELDErvewALKKA------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAK 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19112543 658 VDKTIQSLmhNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERL 706
Cdd:PRK14267 188 IEELLFEL--KKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
501-701 |
1.13e-12 |
|
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: 68.13 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHFGLV-GQE-------PVLFSG 572
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVfGQKtqlwwdlPVIDSF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIaYGksnasqeeIEDAAKRAN---CSFVLSFPEKWSTQVgtRglQLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:cd03267 117 YLLAAI-YD--------LPPARFKKRldeLSELLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 650 LDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQG 701
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
503-702 |
1.65e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.12 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 503 LSFDIHPGTNVAIVAPSGGGKSTI----SQLLLRFYAPSSG-KILADGVDIS---TYNVHQWRSHFGLVGQEPVLFSG-T 573
Cdd:PRK09984 23 VDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGSHiELLGRTVQREgrlARDIRKSRANTGYIFQQFNLVNRlS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 IGENIAYGKSNA-----------SQEEIEDAAKRANCSFVLSFPEKwstQVGTrglqLSGGQKQRIAIARALLRNPAFLI 642
Cdd:PRK09984 103 VLENVLIGALGStpfwrtcfswfTREQKQRALQALTRVGMVHFAHQ---RVST----LSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 643 LDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKL-ATIRRADQIIVVGDGKVLEQGS 702
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVdYALRYCERIVALRQGHVFYDGS 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
499-699 |
2.19e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYapsSGKILADGVDIstynvhqWRSHFGlvGQEPVLfsgtigENI 578
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVDV-------PDNQFG--REASLI------DAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 579 AYGKS-NASQEEIEDAAKRANCSFVLSFPEkwstqvgtrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVM 657
Cdd:COG2401 107 GRKGDfKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 19112543 658 VDKTIQSLMHNRSMTTITIAHKlATIRRA---DQIIVVGDGKVLE 699
Cdd:COG2401 175 VARNLQKLARRAGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
501-708 |
2.92e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 68.61 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKStISQLLLRFYAPSSGKILAD-----GVDISTYNVHQWRSHFG----LVGQEPVLF- 570
Cdd:PRK11022 24 DRISYSVKQGEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMAEklefnGQDLQRISEKERRNLVGaevaMIFQDPMTSl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 571 --SGTIGENIA------YGKSNASQEE----------IEDAAKRANCsfvlsFPEkwstqvgtrglQLSGGQKQRIAIAR 632
Cdd:PRK11022 103 npCYTVGFQIMeaikvhQGGNKKTRRQraidllnqvgIPDPASRLDV-----YPH-----------QLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19112543 633 ALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFERLSR 708
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
471-653 |
3.97e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.19 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 471 IPVPVTVGKAILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDIS 549
Cdd:TIGR03719 312 IPPGPRLGDKVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeIGETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 550 tYnVHQWRSHFglvgqEPvlfSGTIGENIAYGksnasQEEIE----DAAKRANCSfvlSFPEKWSTQ---VGtrglQLSG 622
Cdd:TIGR03719 389 -Y-VDQSRDAL-----DP---NKTVWEEISGG-----LDIIKlgkrEIPSRAYVG---RFNFKGSDQqkkVG----QLSG 446
|
170 180 190
....*....|....*....|....*....|.
gi 19112543 623 GQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
502-704 |
5.78e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 67.59 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFDIH---PGTNV-AIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDISTYN-----VHQwrSHFGLVGQEPVLFS 571
Cdd:PRK11144 12 DLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIvLNGRVLFDAEKgiclpPEK--RRIGYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 572 G-TIGENIAYGKSNASQEE---------IEDAAKRancsfvlsFPekwstqvgtrgLQLSGGQKQRIAIARALLRNPAFL 641
Cdd:PRK11144 90 HyKVRGNLRYGMAKSMVAQfdkivallgIEPLLDR--------YP-----------GSLSGGEKQRVAIGRALLTAPELL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 642 ILDEATSALD--GEAEVMvdKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKVLEQGSFE 704
Cdd:PRK11144 151 LMDEPLASLDlpRKRELL--PYLERLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFGPLE 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
501-695 |
6.30e-12 |
|
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: 65.95 E-value: 6.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIS-----------TYNVHQWRshfglvgqepvl 569
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdrmvvfqNYSLLPWL------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 570 fsgTIGENIAYgksnASQEEIEDAAKRANCSFVlsfpEKWSTQVGTRGL------QLSGGQKQRIAIARALLRNPAFLIL 643
Cdd:TIGR01184 70 ---TVRENIAL----AVDRVLPDLSKSERRAIV----EEHIALVGLTEAadkrpgQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 644 DEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKL-ATIRRADQIIVVGDG 695
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
494-657 |
6.69e-12 |
|
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: 65.21 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 494 RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADG--VDISTYNVHQ---WRSHfgLVGQEPV 568
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgpLDFQRDSIARgllYLGH--APGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 569 LfsgTIGENIAYGKSNASQEEIEDAAkrancsfvlsfpekwsTQVGTRGL------QLSGGQKQRIAIARALLRNPAFLI 642
Cdd:cd03231 88 L---SVLENLRFWHADHSDEQVEEAL----------------ARVGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWI 148
|
170
....*....|....*..
gi 19112543 643 LDEATSALD--GEAEVM 657
Cdd:cd03231 149 LDEPTTALDkaGVARFA 165
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
156-445 |
8.28e-12 |
|
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: 66.76 E-value: 8.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 156 WNFFIAGSLLLVSSGVTMSIPYIVGKILDAG-SSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIV 234
Cdd:cd18555 2 KLLISILLLSLLLQLLTLLIPILTQYVIDNViVPGNLNLLNVLGI-------GILILFLLYGLFSFLRGYIIIKLQTKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 235 SRLRARLFAKCMSLDGAFFDFHKHGDLISRLTtDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPP 314
Cdd:cd18555 75 KSLMSDFFEHLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 315 IALGAFFYGEYVRKLsrtTQDALGDLTRVSE---EKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGS 391
Cdd:cd18555 154 IVLLLLLTRKKIKKL---NQEEIVAQTKVQSyltETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 19112543 392 TGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDI 445
Cdd:cd18555 231 SSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQF 284
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
481-702 |
9.38e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSAS-------------------IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI 541
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 542 LADG-----VDISTynvhqwrshfGLVGQepvlFSGTigENI-----AYGKSNASQEEIEDaakrancsFVLSFPE---K 608
Cdd:COG1134 84 EVNGrvsalLELGA----------GFHPE----LTGR--ENIylngrLLGLSRKEIDEKFD--------EIVEFAElgdF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 609 WSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSAldGEAEVM--VDKTIQSLMhNRSMTTITIAHKLATIRR- 685
Cdd:COG1134 140 IDQPVKT----YSSGMRARLAFAVATAVDPDILLVDEVLAV--GDAAFQkkCLARIRELR-ESGRTVIFVSHSMGAVRRl 212
|
250
....*....|....*..
gi 19112543 686 ADQIIVVGDGKVLEQGS 702
Cdd:COG1134 213 CDRAIWLEKGRLVMDGD 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
499-651 |
9.39e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA----PSSGKILADGVDIST----YnvHQ---WRSHfgLVGQEP 567
Cdd:PRK13538 16 LFSGLSFTLNAGELVQIEGPNGAGKTS----LLRILAglarPDAGEVLWQGEPIRRqrdeY--HQdllYLGH--QPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 568 VLfsgTIGENIAY---GKSNASQEEIEDAakrancsfvLSfpekwstQVGTRGL------QLSGGQKQRIAIARALLRNP 638
Cdd:PRK13538 88 EL---TALENLRFyqrLHGPGDDEALWEA---------LA-------QVGLAGFedvpvrQLSAGQQRRVALARLWLTRA 148
|
170
....*....|...
gi 19112543 639 AFLILDEATSALD 651
Cdd:PRK13538 149 PLWILDEPFTAID 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
499-704 |
1.01e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.82 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRF--YAPSSGKILADGVDISTYNVHQwRSHFG--LVGQEPVLFSGTI 574
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPEE-RAHLGifLAFQYPIEIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GEN---IAYgksNASQEEIEDAAKRAncsfvLSFPEKWSTQVGTRGLQ-----------LSGGQKQRIAIARALLRNPAF 640
Cdd:CHL00131 101 NADflrLAY---NSKRKFQGLPELDP-----LEFLEIINEKLKLVGMDpsflsrnvnegFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 641 LILDEATSALDGEAEVMVDKTIQSLMH-NRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFE 704
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTsENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
501-696 |
1.79e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 67.16 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSS--GKILADGVDISTYNVHQW-RSHFGLVGQEPVLFSG-TIGE 576
Cdd:TIGR02633 18 DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 577 NIAYGksnasqEEIEDAAKRANCSFVLSFPEKWSTQVG------TRGL-QLSGGQKQRIAIARALLRNPAFLILDEATSA 649
Cdd:TIGR02633 98 NIFLG------NEITLPGGRMAYNAMYLRAKNLLRELQldadnvTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19112543 650 L-DGEAEVMVDktIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:TIGR02633 172 LtEKETEILLD--IIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
164-445 |
1.94e-11 |
|
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: 65.56 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 164 LLLVSSGVTMSIPYIVGKILD-AGSSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLF 242
Cdd:cd18567 10 LSLALELFALASPLYLQLVIDeVIVSGDRDLLTVLAI-------GFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 243 AKCMSLDGAFFDFHKHGDLISRLttdSSI--VGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGymslivppIALGAF 320
Cdd:cd18567 83 RHLLRLPLSYFEKRHLGDIVSRF---GSLdeIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLAL--------IVLAAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 321 FYgeYV-------RKLSRTTQDALGDLTRVSE---EKLANVRTTQAFLGERQEVNRYndyiRNLFVLAKREAFASG---I 387
Cdd:cd18567 152 AL--YAllrlalyPPLRRATEEQIVASAKEQShflETIRGIQTIKLFGREAEREARW----LNLLVDAINADIRLQrlqI 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 388 FFGS-TGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDI 445
Cdd:cd18567 226 LFSAaNGLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFEL 284
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
232-424 |
3.21e-11 |
|
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: 64.83 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 232 RIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSI----VGKSLSMYLsDGLRSSVSaiagIGMMLYVSMRLTGY 307
Cdd:cd18588 72 RIDAELGARLFRHLLRLPLSYFESRQVGDTVARVRELESIrqflTGSALTLVL-DLVFSVVF----LAVMFYYSPTLTLI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 308 MSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYN----DYIRNLFVLAKREAF 383
Cdd:cd18588 147 VLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEellaRYVKASFKTANLSNL 226
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19112543 384 ASGIffgsTGFLGNATVIAILALGGRMVAAGDITVGQLSSF 424
Cdd:cd18588 227 ASQI----VQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
503-679 |
3.31e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.70 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 503 LSFDIHPGTNVAIVAPSGGGKSTISQLLL--------RFYAPSSGKILadgvdistynvhqwrshfgLVGQEPVLFSGTI 574
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLF-------------------YVPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GENIAY----------GKSNASQEEIEDAAKRANcsfVLSFPEKWSTQVGTRGLqLSGGQKQRIAIARALLRNPAFLILD 644
Cdd:TIGR00954 532 RDQIIYpdssedmkrrGLSDKDLEQILDNVQLTH---ILEREGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....*
gi 19112543 645 EATSALdgeaEVMVDKTIQSLMHNRSMTTITIAHK 679
Cdd:TIGR00954 608 ECTSAV----SVDVEGYMYRLCREFGITLFSVSHR 638
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
498-701 |
3.62e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 498 SIFDNLSFDIHPGTNVAIVAPSGGGKST-ISQLLLRFYAPS-SGKILADGVDISTynvhQWRSHFGLVGQEPVLFSG-TI 574
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTlLNALAGRIQGNNfTGTILANNRKPTK----QILKRTGFVTQDDILYPHlTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GENIAY------GKSNASQEEIEdAAKRANCSFVLSFPEkwSTQVGT---RGLqlSGGQKQRIAIARALLRNPAFLILDE 645
Cdd:PLN03211 158 RETLVFcsllrlPKSLTKQEKIL-VAESVISELGLTKCE--NTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 646 ATSALDGEAEVMVDKTIQSLMHnRSMTTITIAHKLAT--IRRADQIIVVGDGKVLEQG 701
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQ-KGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
166-440 |
5.07e-11 |
|
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: 64.15 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 166 LVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMgipsgtFYIGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKC 245
Cdd:cd18782 12 FVVQLLGLANPLLFQVIIDKVLVQQDLATLYV------IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 246 MSLDGAFFDFHKHGDLISRL----TTDSSIVGKSLSMYLSdglrsSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFF 321
Cdd:cd18782 86 LRLPLGFFDKRPVGELSTRIseldTIRGFLTGTALTTLLD-----VLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 322 YGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGE---RQEV-NRYNDYIRNLFVLAKreafaSGIFFGSTG-FLG 396
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAElkaRWRWqNRYARSLGEGFKLTV-----LGTTSGSLSqFLN 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19112543 397 NATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSG 440
Cdd:cd18782 236 KLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLST 279
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
501-695 |
5.13e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 5.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNvHQWRSHFGL--VGQE-PVLFSGTIGEN 577
Cdd:PRK09700 22 KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQLGIgiIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 IAYGKSNASQE---EIEDAAKRANCSFVLSFPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDgEA 654
Cdd:PRK09700 101 LYIGRHLTKKVcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT-NK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19112543 655 EVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDG 695
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
473-697 |
5.32e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.72 E-value: 5.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 473 VPVTVGKAILSFRNVGFAYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFY-APSSGKILADGVDISTY 551
Cdd:PRK13549 251 EPHTIGEVILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPVKIR 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 552 NVHQW-----------RSHFGLVgqePVLfsgTIGENI---AYGK--------SNASQEEIEDAAKRanCSFVLSFPEkw 609
Cdd:PRK13549 331 NPQQAiaqgiamvpedRKRDGIV---PVM---GVGKNItlaALDRftggsridDAAELKTILESIQR--LKVKTASPE-- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 610 sTQVGtrglQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIR-RADQ 688
Cdd:PRK13549 401 -LAIA----RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLgLSDR 474
|
....*....
gi 19112543 689 IIVVGDGKV 697
Cdd:PRK13549 475 VLVMHEGKL 483
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
509-695 |
1.02e-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: 60.46 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 509 PGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFGlvgqepvlfsgtigeniaygksnasqe 588
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 589 eiedaakrancsfvlsfpekwstqVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHN 668
Cdd:smart00382 54 ------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180 190
....*....|....*....|....*....|....*...
gi 19112543 669 RS-----------MTTITIAHKLATIRRADQIIVVGDG 695
Cdd:smart00382 110 LLkseknltviltTNDEKDLGPALLRRRFDRRIVLLLI 147
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
501-702 |
1.47e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPS---SGKILADGVDISTYNVHQW---RS-HFGLVGQEPVlfsgT 573
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELnklRAeQISMIFQDPM----T 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 -------IGENIA--------YGKSNASQEEIE--DAAKrancsfvlsFPEKwSTQVGTRGLQLSGGQKQRIAIARALLR 636
Cdd:PRK09473 109 slnpymrVGEQLMevlmlhkgMSKAEAFEESVRmlDAVK---------MPEA-RKRMKMYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 637 NPAFLILDEATSALDgeaeVMVDKTIQSLMHN--RSMTT--ITIAHKL---ATIrrADQIIVVGDGKVLEQGS 702
Cdd:PRK09473 179 RPKLLIADEPTTALD----VTVQAQIMTLLNElkREFNTaiIMITHDLgvvAGI--CDKVLVMYAGRTMEYGN 245
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
501-699 |
1.69e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 501 DNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSS--GKILADGvdistyNVHQWRS-----HFGLV--GQE----P 567
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG------EVCRFKDirdseALGIViiHQElaliP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 568 VLfsgTIGENIAYGKSNAS------QEEIEDAA---KRANCSfvlsfpEKWSTQVGTRGLqlsgGQKQRIAIARALLRNP 638
Cdd:NF040905 92 YL---SIAENIFLGNERAKrgvidwNETNRRARellAKVGLD------ESPDTLVTDIGV----GKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 639 AFLILDEATSAL-DGEAEVMVDktiqsLMH---NRSMTTITIAHKLATIRR-ADQIIVVGDGKVLE 699
Cdd:NF040905 159 KLLILDEPTAALnEEDSAALLD-----LLLelkAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-701 |
1.84e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.04 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 506 DIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIStYNVHQWRSHF-GLVgqEPVLFSGTIGeniaYGKSN 584
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYeGTV--RDLLSSITKD----FYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 585 ASQEEIEDaakrancsfvlsfPEKWSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQS 664
Cdd:cd03237 94 YFKTEIAK-------------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 19112543 665 LMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQG 701
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPSVNG 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
481-653 |
3.24e-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: 63.42 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPtrPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRfyapssgkILAdGVDiSTYNVHQWRS-- 558
Cdd:TIGR03719 4 IYTMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST----LLR--------IMA-GVD-KDFNGEARPQpg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 559 -HFGLVGQEPVL-FSGTIGENI-------------------AYGKSNAS-------QEEIEDAAKRAN----------CS 600
Cdd:TIGR03719 68 iKVGYLPQEPQLdPTKTVRENVeegvaeikdaldrfneisaKYAEPDADfdklaaeQAELQEIIDAADawdldsqleiAM 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19112543 601 FVLSFPEkWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:TIGR03719 148 DALRCPP-WDADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
478-653 |
3.36e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.43 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 478 GKAILSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDISTYNvhQW 556
Cdd:PRK11147 316 GKIVFEMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhCGTKLEVAYFD--QH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 557 RSHFglvgqEPvlfSGTIGENIAYGKsnasQEEIEDAAKRANCSFVLSF---PEKWSTQVGTrglqLSGGQKQRIAIARA 633
Cdd:PRK11147 391 RAEL-----DP---EKTVMDNLAEGK----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPVKA----LSGGERNRLLLARL 454
|
170 180
....*....|....*....|
gi 19112543 634 LLRNPAFLILDEATSALDGE 653
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVE 474
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
499-702 |
3.43e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLL--LRFYAPSSGKIL---------------------------------A 543
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 544 DGVDIS---TYNVHQ-----WRSHFGLVGQEPVLfsgtigENIAYGKSNASQEEiEDAAKRAncsfvLSFPEKwsTQVGT 615
Cdd:TIGR03269 95 DFWNLSdklRRRIRKriaimLQRTFALYGDDTVL------DNVLEALEEIGYEG-KEAVGRA-----VDLIEM--VQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 616 R----GLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQII 690
Cdd:TIGR03269 161 RithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDlSDKAI 240
|
250
....*....|..
gi 19112543 691 VVGDGKVLEQGS 702
Cdd:TIGR03269 241 WLENGEIKEEGT 252
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
494-709 |
5.49e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 5.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 494 RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqLLLRFYAPSSGKILADGVDIS---TYN------------------ 552
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKST---LLKALAGDLTGGGAPRGARVTgdvTLNgeplaaidaprlarlrav 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 -VHQWRSHFGLVGQEPVLFsGTIGENIAYGKSNASQEEIEDAA-KRANCSfvlsfpekwsTQVGTRGLQLSGGQKQRIAI 630
Cdd:PRK13547 88 lPQAAQPAFAFSAREIVLL-GRYPHARRAGALTHRDGEIAWQAlALAGAT----------ALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 631 ARAL---------LRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAH--KLATiRRADQIIVVGDGKVLE 699
Cdd:PRK13547 157 ARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHdpNLAA-RHADRIAMLADGAIVA 235
|
250
....*....|
gi 19112543 700 QGSFERLSRP 709
Cdd:PRK13547 236 HGAPADVLTP 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
507-691 |
5.90e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.52 E-value: 5.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 507 IHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADgVDIStYNVHQWRSHF-GLVGQepVLFSgtIGENIAygkSNA 585
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS-YKPQYIKPDYdGTVED--LLRS--ITDDLG---SSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 586 SQEEIedaAKRancsfvLSFPEKWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSL 665
Cdd:PRK13409 433 YKSEI---IKP------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180
....*....|....*....|....*..
gi 19112543 666 MHNRSMTTITIAHKLATIRR-ADQIIV 691
Cdd:PRK13409 500 AEEREATALVVDHDIYMIDYiSDRLMV 526
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
159-455 |
6.75e-10 |
|
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: 60.65 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 159 FIAgSLLLVSSGVtmSIPYIVGKILD-AGSSGDSSVTHIMGIpsgtfyiGLLGLFFLGSACNFGRIITLRLLSERIVSRL 237
Cdd:cd18568 8 LLA-SLLLQLLGL--ALPLFTQIILDrVLVHKNISLLNLILI-------GLLIVGIFQILLSAVRQYLLDYFANRIDLSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 238 RARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSI----VGKSLSMYLSdglrsSVSAIAGIGMMLYVSMRLTGYMSLIVP 313
Cdd:cd18568 78 LSDFYKHLLSLPLSFFASRKVGDIITRFQENQKIrrflTRSALTTILD-----LLMVFIYLGLMFYYNLQLTLIVLAFIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 314 PIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRY-NDYIRNLFVLAKREAFASGIFFGSt 392
Cdd:cd18568 153 LYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWeNKFAKALNTRFRGQKLSIVLQLIS- 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19112543 393 GFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGSIVGLSGCFTDIMKGLGAASRL 455
Cdd:cd18568 232 SLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
480-696 |
6.87e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGFAYPtrpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNV------ 553
Cdd:PRK11288 3 PYLSFDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtaalaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 -----HQwrsHFGLVgqePVLfsgTIGENIAYGKSNASQEEIEDAAKRANCSFVLSF------PEkwsTQVGTrglqLSG 622
Cdd:PRK11288 80 gvaiiYQ---ELHLV---PEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHlgvdidPD---TPLKY----LSI 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 623 GQKQRIAIARALLRNPAFLILDEATSALDG-EAEVMVdKTIQSLmhnRSMTT--ITIAHKLATI-RRADQIIVVGDGK 696
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF-RVIREL---RAEGRviLYVSHRMEEIfALCDAITVFKDGR 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
474-651 |
2.47e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 474 PVTVGKAILSFRNVGFAyPTRPSASIfDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNV 553
Cdd:COG3845 250 PAEPGEVVLEVENLSVR-DDRGVPAL-KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 554 HQW-----------RSHFGLVGqepvlfSGTIGENIA---YGKSNAS------QEEIEDAAKRAncsfVLSFpekwstQV 613
Cdd:COG3845 328 RERrrlgvayipedRLGRGLVP------DMSVAENLIlgrYRRPPFSrggfldRKAIRAFAEEL----IEEF------DV 391
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19112543 614 GTRGLQ-----LSGGQKQRIAIARALLRNPAFLILDEATSALD 651
Cdd:COG3845 392 RTPGPDtparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
481-653 |
2.52e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.52 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPtrPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYA----PSSGK-ILADGVDIstynvhq 555
Cdd:PRK11819 6 IYTMNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAgvdkEFEGEaRPAPGIKV------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 wrshfGLVGQEPVL-FSGTIGENI-------------------AYGKSNAS-----------QEEI------------ED 592
Cdd:PRK11819 73 -----GYLPQEPQLdPEKTVRENVeegvaevkaaldrfneiyaAYAEPDADfdalaaeqgelQEIIdaadawdldsqlEI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112543 593 AAKRANCsfvlsfPEkWSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:PRK11819 148 AMDALRC------PP-WDAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
506-691 |
3.00e-09 |
|
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: 60.18 E-value: 3.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 506 DIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADgVDIStYNvHQWRSH--FGLVGQepvLFSGTIGENIAygkS 583
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKIS-YK-PQYISPdyDGTVEE---FLRSANTDDFG---S 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 584 NASQEEIedaAKRANCSFVLsfpEKwstQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQ 663
Cdd:COG1245 433 SYYKTEI---IKPLGLEKLL---DK---NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180
....*....|....*....|....*....
gi 19112543 664 SLMHNRSMTTITIAHKLATIRR-ADQIIV 691
Cdd:COG1245 500 RFAENRGKTAMVVDHDIYLIDYiSDRLMV 528
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
618-709 |
4.29e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.43 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 618 LQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGkv 697
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG-- 147
|
90
....*....|..
gi 19112543 698 lEQGSFERLSRP 709
Cdd:cd03222 148 -EPGVYGIASQP 158
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
498-700 |
4.74e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 498 SIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRS-----HFGLVGQEPVLFSg 572
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA-RAklrakHVGFVFQSFMLIP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIG--ENI---AYGKSNASQEEIEDAAKRAncsfvlsfpekwsTQVGTRG------LQLSGGQKQRIAIARALLRNPAFL 641
Cdd:PRK10584 102 TLNalENVelpALLRGESSRQSRNGAKALL-------------EQLGLGKrldhlpAQLSGGEQQRVALARAFNGRPDVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 642 ILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQ 700
Cdd:PRK10584 169 FADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
500-697 |
8.20e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.52 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 500 FDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQwRSHFGLV-----GQEPVLF-SGT 573
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 574 IGENI---AYGKSNASQEEIEDAAK----RANCSFVLSFPEKwstQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEA 646
Cdd:PRK15439 358 LAWNVcalTHNRRGFWIKPARENAVleryRRALNIKFNHAEQ---AART----LSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 647 TSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
619-692 |
1.09e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 1.09e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 619 QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMttITIAHKLATIRR-ADQIIVV 692
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYV--LVVEHDLAVLDYlADNVHIA 284
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
472-647 |
1.73e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 472 PVPVTVGKAILSFRNVgfaypTRPSAsiFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTY 551
Cdd:COG1129 247 KRAAAPGEVVLEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 552 NVHQ-WRSHFGLV----GQEPVLFSGTIGENIAYGKSNA--------SQEEIEDAakrancsfvlsfpEKWSTQVG--TR 616
Cdd:COG1129 320 SPRDaIRAGIAYVpedrKGEGLVLDLSIRENITLASLDRlsrgglldRRRERALA-------------EEYIKRLRikTP 386
|
170 180 190
....*....|....*....|....*....|....*.
gi 19112543 617 GL-----QLSGGQKQRIAIARALLRNPAFLILDEAT 647
Cdd:COG1129 387 SPeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
471-653 |
1.79e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.82 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 471 IPVPVTVGKAILSFRNVGFAYPTRpsaSIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDIS 549
Cdd:PRK11819 314 IPPGPRLGDKVIEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkIGETVKLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 550 tYnVHQWRSHFglvgqEPvlfSGTIGENIAYGksnasQEEIE----DAAKRANCSfvlSFPEKWSTQ---VGtrglQLSG 622
Cdd:PRK11819 391 -Y-VDQSRDAL-----DP---NKTVWEEISGG-----LDIIKvgnrEIPSRAYVG---RFNFKGGDQqkkVG----VLSG 448
|
170 180 190
....*....|....*....|....*....|.
gi 19112543 623 GQKQRIAIARALLRNPAFLILDEATSALDGE 653
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
158-331 |
2.87e-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: 55.97 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKILDAGSSGDSSvthimgiPSGTFYIGLLGLFFLGSA-CNFGRIITLRLLSERIVSR 236
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNS-------SSGYYLGVYAALLVLASVlLVLLRWLLFVLAGLRASRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVsmrlTGYMSLIVPPIA 316
Cdd:cd18580 74 LHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIV----SPYFLIVLPPLL 149
|
170
....*....|....*
gi 19112543 317 LGAFFYGEYVRKLSR 331
Cdd:cd18580 150 VVYYLLQRYYLRTSR 164
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
164-421 |
5.25e-08 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 55.20 E-value: 5.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 164 LLLVSSGVTMSIPYIVGKILDAGSSGDSSVTHIMgipsgTFYIGLLGLF-FLGSACNFGRIITLRLLSERIVSRLRARLF 242
Cdd:cd18582 4 LLVLAKLLNVAVPFLLKYAVDALSAPASALLAVP-----LLLLLAYGLArILSSLFNELRDALFARVSQRAVRRLALRVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 243 AKCMSLDGAFFDFHKHGDL---ISRLTtdssivgKSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGA 319
Cdd:cd18582 79 RHLHSLSLRFHLSRKTGALsraIERGT-------RGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 320 -----FFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDyirnlfVLAKREAfASGIFFGSTGF 394
Cdd:cd18582 152 yvaftIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDK------ALAKYEK-AAVKSQTSLAL 224
|
250 260 270
....*....|....*....|....*....|....
gi 19112543 395 LG-------NATVIAILALGGRMVAAGDITVGQL 421
Cdd:cd18582 225 LNigqaliiSLGLTAIMLLAAQGVVAGTLTVGDF 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
495-696 |
6.70e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 495 PSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN-----------VHQwrsHFGLV 563
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSskealengismVHQ---ELNLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 564 GQEPVLFSGTIG----------ENIAYGKSNASQEEIE-DAAKRancsfvlsfpEKWSTqvgtrglqLSGGQKQRIAIAR 632
Cdd:PRK10982 86 LQRSVMDNMWLGryptkgmfvdQDKMYRDTKAIFDELDiDIDPR----------AKVAT--------LSVSQMQMIEIAK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19112543 633 ALLRNPAFLILDEATSALDgEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGK 696
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLT-EKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDGQ 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
486-704 |
9.03e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 486 NVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDISTY------------N 552
Cdd:PRK15064 324 NLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGYYaqdhaydfendlT 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 VHQWRSHFGLVGQEPVLFSGTIGENIaygksnASQEEIEDAAKrancsfvlsfpekwstqvgtrglQLSGGQKQRIAIAR 632
Cdd:PRK15064 401 LFDWMSQWRQEGDDEQAVRGTLGRLL------FSQDDIKKSVK-----------------------VLSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 633 ALLRNPAFLILDEATSALDGEAevmvdktIQSL---MHNRSMTTITIAH------KLATirradQIIVVGDGKVLE-QGS 702
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMES-------IESLnmaLEKYEGTLIFVSHdrefvsSLAT-----RIIEITPDGVVDfSGT 519
|
..
gi 19112543 703 FE 704
Cdd:PRK15064 520 YE 521
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
494-714 |
9.85e-08 |
|
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: 55.79 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 494 RPSAsifDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHFGLVGQEPVLFSG- 572
Cdd:TIGR01257 943 RPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 573 TIGENIAY-----GKS-NASQEEIEDAAKRANcsfvLSFPEKWSTQvgtrglQLSGGQKQRIAIARALLRNPAFLILDEA 646
Cdd:TIGR01257 1019 TVAEHILFyaqlkGRSwEEAQLEMEAMLEDTG----LHHKRNEEAQ------DLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19112543 647 TSALDGEAEvmvdKTIQS-LMHNRSMTTITIA--HKLATIRRADQIIVVGDGKVLEQGSFERLSRP-GTNFY 714
Cdd:TIGR01257 1089 TSGVDPYSR----RSIWDlLLKYRSGRTIIMSthHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCfGTGFY 1156
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
499-703 |
1.29e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLL--RFYAPSSGKILADGVDISTYNVHQwRSHFG--LVGQEPVLFSGTI 574
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGifMAFQYPVEIPGVS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 575 GENIAYGKSNA-----SQEE---------IEDAAKrancsfVLSFPEKWSTQVGTRGLqlSGGQKQRIAIARALLRNPAF 640
Cdd:PRK09580 95 NQFFLQTALNAvrsyrGQEPldrfdfqdlMEEKIA------LLKMPEDLLTRSVNVGF--SGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19112543 641 LILDEATSALDGEAEVMVDKTIQSLMH-NRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSF 703
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
504-681 |
2.05e-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: 52.75 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 504 SFDIH------PGTNVAIVAPSGGGKSTISQLL--------------------LRFYAPSS-----GKILADGVDIST-- 550
Cdd:cd03236 14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILagklkpnlgkfddppdwdeiLDEFRGSElqnyfTKLLEGDVKVIVkp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 551 -YnvhqwrshfglVGQEPVLFSGTIGENIAYGKSNASQEEIEDaakrancsfVLSFpekwsTQVGTRGL-QLSGGQKQRI 628
Cdd:cd03236 94 qY-----------VDLIPKAVKGKVGELLKKKDERGKLDELVD---------QLEL-----RHVLDRNIdQLSGGELQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19112543 629 AIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLM-HNRSMttITIAHKLA 681
Cdd:cd03236 149 AIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAeDDNYV--LVVEHDLA 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
480-701 |
2.65e-07 |
|
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: 51.88 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 480 AILSFRNVGF-AYPTRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLL---LRFYAPSSGKILADGVDISTyNVHQ 555
Cdd:cd03233 2 STLSWRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKE-FAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 556 WRSHFGLVGQE----PVLfsgTIgeniaygksnasQEEIEDAAKRANCSFVlsfpekwstqvgtRGLqlSGGQKQRIAIA 631
Cdd:cd03233 81 YPGEIIYVSEEdvhfPTL---TV------------RETLDFALRCKGNEFV-------------RGI--SGGERKRVSIA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19112543 632 RALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTItiahklATIRRA--------DQIIVVGDGKVLEQG 701
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTF------VSLYQAsdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
493-682 |
5.54e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 5.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 493 TRPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSHFG-LVGQEPVLfs 571
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGhLPGLKADL-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 572 gTIGENIAYgkSNASQeeiedaAKRANcsfvlSFPEKWSTQVGTRGL------QLSGGQKQRIAIARALLRNPAFLILDE 645
Cdd:PRK13543 98 -STLENLHF--LCGLH------GRRAK-----QMPGSALAIVGLAGYedtlvrQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 19112543 646 ATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLAT 682
Cdd:PRK13543 164 PYANLDLEGITLVNRMISAHLRGGGAALVTTHGAYAA 200
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
481-687 |
7.41e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHF 560
Cdd:PRK13540 1 MLDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQE----PVLfsgTIGENIAYGKSNASQE-EIEDAAKRANCSFVLSFPekwstqvgtRGLqLSGGQKQRIAIARALL 635
Cdd:PRK13540 77 CFVGHRsginPYL---TLRENCLYDIHFSPGAvGITELCRLFSLEHLIDYP---------CGL-LSSGQKRQVALLRLWM 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19112543 636 RNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITiAHKLATIRRAD 687
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLT-SHQDLPLNKAD 194
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
479-665 |
1.03e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPT-RPSASIFDNLSFDIHPGTNVAIVAPSGGGKSTisqlLLRFYAPS------SGKILADGVDISTY 551
Cdd:cd03232 1 GSVLTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGRktagviTGEILINGRPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 552 nvhqWRSHFGLVGQEPVLFSG-TIGENIAYGksnasqeeiedaakrANCsfvlsfpekwstqvgtRGLQLSggQKQRIAI 630
Cdd:cd03232 77 ----FQRSTGYVEQQDVHSPNlTVREALRFS---------------ALL----------------RGLSVE--QRKRLTI 119
|
170 180 190
....*....|....*....|....*....|....*
gi 19112543 631 ARALLRNPAFLILDEATSALDGEAEVMVDKTIQSL 665
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
620-701 |
1.09e-06 |
|
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: 49.24 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 LSGGQKQRIAIARALLRNP--AFLILDEATSALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRRADQIIVVG---- 693
Cdd:cd03238 88 LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLI-DLGNTVILIEHNLDVLSSADWIIDFGpgsg 166
|
90
....*....|
gi 19112543 694 --DGKVLEQG 701
Cdd:cd03238 167 ksGGKVVFSG 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
496-705 |
1.14e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 496 SASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQW-----------RSHFGLVg 564
Cdd:PRK10762 264 SGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyisedRKRDGLV- 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 565 qepvlFSGTIGENI----------AYGKSNASQEEIedaakrANCSFVLSFPEKWSTQVGTRGLqLSGGQKQRIAIARAL 634
Cdd:PRK10762 343 -----LGMSVKENMsltalryfsrAGGSLKHADEQQ------AVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGL 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 635 LRNPAFLILDEATSALDgeaeVMVDKTIQSLMhNR----SMTTITIAHKLATIR-RADQIIVVGDGKVleQGSFER 705
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD----VGAKKEIYQLI-NQfkaeGLSIILVSSEMPEVLgMSDRILVMHEGRI--SGEFTR 479
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
619-706 |
1.31e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 50.96 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
....*....
gi 19112543 698 LEQGSFERL 706
Cdd:PRK15093 238 VETAPSKEL 246
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
481-675 |
1.42e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 481 ILSFRNVGFAYPTRPSASIfDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTyNVHQWRSHF 560
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 561 GLVGQEPVLFSGTIGENIAYGKSNASQEEIEDAAKRANcsfvlsfpekWSTQvgTRGLQL---------SGGQKQRIAIA 631
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVAN----------WSIQ--SLGLSLyadrlagtySGGNKRKLSTA 2082
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19112543 632 RALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTIT 675
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT 2126
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
619-714 |
1.43e-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: 51.71 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLM-HNRSMttITIAHKLATIRR-ADQI-IVVGdg 695
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAeEGKYV--LVVEHDLAILDYlADYVhILYG-- 287
|
90 100
....*....|....*....|....
gi 19112543 696 kvlEQGSFERLSRP-----GTNFY 714
Cdd:COG1245 288 ---EPGVYGVVSKPksvrvGINQY 308
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
620-707 |
2.14e-06 |
|
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: 51.17 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 LSGGQKQRIAIARALLR---NPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSmTTITIAHKLATIRRADQIIVVG--- 693
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIKTADYIIDLGpeg 908
|
90
....*....|....*..
gi 19112543 694 ---DGKVLEQGSFERLS 707
Cdd:TIGR00630 909 gdgGGTVVASGTPEEVA 925
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
499-697 |
1.04e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 499 IFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKI-LADGVDISTYNVHQWrsHFGLVGQEPVlfsgtigEN 577
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQL--EFLRADESPL-------QH 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 578 IAYGKSNASQEEIEDaakrancsFVLSFPEKwSTQVGTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALD------ 651
Cdd:PRK10636 398 LARLAPQELEQKLRD--------YLGGFGFQ-GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDldmrqa 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19112543 652 -GEAEVMVDKTIQSLMHNRSMTTITiahklatirrADQIIVVGDGKV 697
Cdd:PRK10636 469 lTEALIDFEGALVVVSHDRHLLRST----------TDDLYLVHDGKV 505
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
206-445 |
1.60e-05 |
|
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: 47.19 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 206 IGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLttdssivgKSLSM---YLSD 282
Cdd:cd18566 46 IGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL--------NSLEQireFLTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 283 GLRSSVSAIAGIGMMLYVSMRLTGYMSLIvpPIALGAFFYGEYVRkLSRTTQDALGDLTRVSE-------EKLANVRTTQ 355
Cdd:cd18566 118 QALLALLDLPFVLIFLGLIWYLGGKLVLV--PLVLLGLFVLVAIL-LGPILRRALKERSRADErrqnfliETLTGIHTIK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 356 AFLGERQEVNRY----NDYIRNLFVLAKREAFASGiffgSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYA 431
Cdd:cd18566 195 AMAMEPQMLRRYerlqANAAYAGFKVAKINAVAQT----LGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRV 270
|
250
....*....|....
gi 19112543 432 GGSIVGLSGCFTDI 445
Cdd:cd18566 271 LQPLQRAFGLWTRF 284
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
485-652 |
2.11e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 485 RNVGFAYPTRPsasIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLlrfyapssgkiladgvdistynvhqwrshfglVG 564
Cdd:PRK10938 264 NNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI--------------------------------TG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 565 QEPVLFSGTIgenIAYGKSNASQEEIEDAAK-------------RANCSF---VLS------------------FPEKWS 610
Cdd:PRK10938 309 DHPQGYSNDL---TLFGRRRGSGETIWDIKKhigyvssslhldyRVSTSVrnvILSgffdsigiyqavsdrqqkLAQQWL 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19112543 611 TQVGTRGLQ-------LSGGQkQRIA-IARALLRNPAFLILDEATSALDG 652
Cdd:PRK10938 386 DILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
502-704 |
3.90e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 46.03 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDIstyNVHQWRSHFGLVGQ------------EPVL 569
Cdd:PRK15056 25 DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT---RQALQKNLVAYVPQseevdwsfpvlvEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 570 FSGTIGENIAYGKSNASQEEIEDAA-KRANcsfVLSFPEKwstQVGtrglQLSGGQKQRIAIARALLRNPAFLILDEATS 648
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVTAAlARVD---MVEFRHR---QIG----ELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19112543 649 ALDGEAEVMVDKTIQSLmHNRSMTTITIAHKLATIRRADQIIVVGDGKVLEQGSFE 704
Cdd:PRK15056 172 GVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
479-696 |
3.97e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 479 KAILSFRNVGFAYPtrpSASIFDNLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYN------ 552
Cdd:PRK10762 2 QALLQLKGIDKAFP---GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpkssqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 -----VHQwrsHFGLVGQEpvlfsgTIGENI--------AYGKSNASQ--EEIEDAAKRANCSFvlsfpeKWSTQVGtrg 617
Cdd:PRK10762 79 agigiIHQ---ELNLIPQL------TIAENIflgrefvnRFGRIDWKKmyAEADKLLARLNLRF------SSDKLVG--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 618 lQLSGGQKQRIAIARALLRNPAFLILDEATSAL-DGEAEVMVdKTIQSLmHNRSMTTITIAHKLATIRR-ADQIIVVGDG 695
Cdd:PRK10762 141 -ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIREL-KSQGRGIVYISHRLKEIFEiCDDVTVFRDG 217
|
.
gi 19112543 696 K 696
Cdd:PRK10762 218 Q 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
614-706 |
5.93e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.88 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 614 GTRGLQLSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQSLMHNRSMTTITIAHKLATIRRADQIIVVG 693
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVID 218
|
90
....*....|...
gi 19112543 694 DGKVLEQGSFERL 706
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
163-428 |
6.66e-05 |
|
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: 45.29 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 163 SLLLVSSGVTMSIPYIVGKILDAGSSGDSSVThimgiPSGTFYIGLLGLF-FLGSACNFGRIITLRLLSERIVSRLRARL 241
Cdd:cd18560 3 LLLILGKACNVLAPLFLGRAVNALTLAKVKDL-----ESAVTLILLYALLrFSSKLLKELRSLLYRRVQQNAYRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 242 FAKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSLSMYLSDGLRSSVSAIAGIGMMLYVSMRLTG-YMSLIVppiALGAF 320
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTE----SANTLLSYLVFYLVPTLLELIVVSVVFAFHFGaWLALIV---FLSVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 321 FYG-------EYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNLFVLAkREAFASGIFFGST- 392
Cdd:cd18560 151 LYGvftikvtEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSS-VKVQASLSLLNVGq 229
|
250 260 270
....*....|....*....|....*....|....*.
gi 19112543 393 GFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYT 428
Cdd:cd18560 230 QLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYI 265
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
166-424 |
8.32e-05 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain] Cd Length: 289 Bit Score: 45.31 E-value: 8.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 166 LVSSGVTMSIPYIVGKILDAGSSGdSSVTHIMGIPSGtfyiglLGLFflgsacNFGRIITLRLLSERIVSRLR----ARL 241
Cdd:cd18562 9 VALAGVQFAEPVLFGRVVDALSSG-GDAFPLLALWAA------LGLF------SILAGVLVALLADRLAHRRRlavmASY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 242 FAKCMSLDGAFFDFHKHGDLISRLTTDSSivgkSL-SMYLSdGLRSSVSAIAGIGMMLYVSMRLTGYMSLIVppIALGAF 320
Cdd:cd18562 76 FEHVITLPLSFHSQRGSGRLLRIMLRGTD----ALfGLWLG-FFREHLAALVSLIVLLPVALWMNWRLALLL--VVLAAV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 321 FYGEYVRKLSRTT--QDALGDL-TRVSE---EKLANVRTTQAFLGERQEVNRYNDYIRNLfvLAKRE------AFASGIF 388
Cdd:cd18562 149 YAALNRLVMRRTKagQAAVEEHhSALSGrvgDVIGNVTVVQSYTRLAAETSALRGITRRL--LAAQYpvlnwwALASVLT 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 19112543 389 FGSTGFlgnaTVIAILALGGRMVAAGDITVGQLSSF 424
Cdd:cd18562 227 RAASTL----TMVAIFALGAWLVQRGELTVGEIVSF 258
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
202-445 |
1.01e-04 |
|
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: 44.81 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 202 GTFY---IGLLGLFFLGSACNFGRIITLRLLSERIVSRLRARLFAKCMSLDGAFFDFHKHGDLISRLTTDSSI----VGK 274
Cdd:cd18783 39 STLYvltIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHMQQIERIrqflTGQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 275 SLSMYLSdglrsSVSAIAGIGMMLYVSMRLTGYMSLIVPPIALGAFFYGEYVRKLSRTTQDALGDLTRVSEEKLANVRTT 354
Cdd:cd18783 119 LFGTLLD-----ATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 355 QAFLGERQEVNRYNDYIRNLFVLAKREAFASGIFFGSTGFLGNATVIAILALGGRMVAAGDITVGQLSSFLLYTVYAGGS 434
Cdd:cd18783 194 KSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGP 273
|
250
....*....|.
gi 19112543 435 IVGLSGCFTDI 445
Cdd:cd18783 274 LVQLAGLVQEY 284
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
502-697 |
1.63e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 502 NLSFDIHPGTNVAIVAPSGGGKSTISQLLLRFYAPSSGKILADGVDISTYNVHQWRSH-FGLVGQE----------PVLF 570
Cdd:PRK10982 266 DVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgFALVTEErrstgiyaylDIGF 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 571 SGTIGENIAYGKSNA--SQEEIEDAAKRANCSFVLSFPEKwSTQVGTrglqLSGGQKQRIAIARALLRNPAFLILDEATS 648
Cdd:PRK10982 346 NSLISNIRNYKNKVGllDNSRMKSDTQWVIDSMRVKTPGH-RTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19112543 649 ALDGEAEVMVDKTIQSLMhNRSMTTITIAHKLATIRR-ADQIIVVGDGKV 697
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELA-KKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
620-697 |
2.05e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 LSGGQKQRIAIARALLRNPAFLILDEATSALDgeaevmVDkTIQSL---MHNRSMTTITIAHKLATIRR-ADQIIVVGDG 695
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD------IE-TIEWLegfLKTFQGSIIFISHDRSFIRNmATRIVDLDRG 229
|
..
gi 19112543 696 KV 697
Cdd:PRK11147 230 KL 231
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
620-692 |
2.53e-04 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 42.84 E-value: 2.53e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 620 LSGGQKQRIAIAR--ALLR-NPA-FLILDEATSALDgeaEVMVDKTIQsLMHNRSMTT--ITIAHKLATIRRADQIIVV 692
Cdd:cd03278 114 LSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALD---DANVERFAR-LLKEFSKETqfIVITHRKGTMEAADRLYGV 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-692 |
2.67e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 2.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19112543 619 QLSGGQKQRIAIAR--ALLR-NPA-FLILDEATSALDgeaEVMVDKTIQSLMHNRSMTT-ITIAHKLATIRRADQIIVV 692
Cdd:TIGR02168 1089 LLSGGEKALTALALlfAIFKvKPApFCILDEVDAPLD---DANVERFANLLKEFSKNTQfIVITHNKGTMEVADQLYGV 1164
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
498-693 |
3.78e-04 |
|
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: 41.58 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 498 SIFDNLSFDIHPGTNVAIVAPSGGGKSTI-SQLLLrfyapssgkiladgvdISTYNVHQWRSHFGlvgqepvlfsGTIGE 576
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTIlDAIGL----------------ALGGAQSATRRRSG----------VKAGC 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 577 NIAYgksnasqEEIEdaakrancsFVLSFPekwstqvgtrglQLSGGQKQRIAIARAL---LRNPA-FLILDEATSALDG 652
Cdd:cd03227 63 IVAA-------VSAE---------LIFTRL------------QLSGGEKELSALALILalaSLKPRpLYILDEIDRGLDP 114
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19112543 653 -EAEVMVDKTIQSLMHNRsmTTITIAHKLATIRRADQIIVVG 693
Cdd:cd03227 115 rDGQALAEAILEHLVKGA--QVIVITHLPELAELADKLIHIK 154
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
583-690 |
5.25e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 583 SNASQEEIEDAAKRANC--SFVLSFPEKWSTQVGtrglQLSGGQKQRIAIA--RALLR-NPA-FLILDEATSALDgEAEV 656
Cdd:pfam02463 1043 GGSAELRLEDPDDPFSGgiEISARPPGKGVKNLD----LLSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALD-DQNV 1117
|
90 100 110
....*....|....*....|....*....|....*.
gi 19112543 657 mvdKTIQSLMHNRSMTT--ITIAHKLATIRRADQII 690
Cdd:pfam02463 1118 ---SRVANLLKELSKNAqfIVISLREEMLEKADKLV 1150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
474-694 |
7.33e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.17 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 474 PVTVGKAILSFRNVGFAYPTRPSA-SIFDNLSFDIHPGTNVAIVAPSGGGKSTisqLLLRFYAPSSGKILADGVDIStyN 552
Cdd:TIGR00956 752 EKESGEDIFHWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLV--N 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 553 VHQWRSHF----GLVGQEPV-LFSGTIGENIAYGKSNASQEEIEDAAKRANCSFVLSFPEKWSTQ---VGTRGLQLSGGQ 624
Cdd:TIGR00956 827 GRPLDSSFqrsiGYVQQQDLhLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYAdavVGVPGEGLNVEQ 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 625 KQRIAIARALLRNPAFLI-LDEATSALDGEAEVMVDKTIQSL----------MHNRSMTTITIAHKLATIRRADQIIVVG 693
Cdd:TIGR00956 907 RKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLadhgqailctIHQPSAILFEEFDRLLLLQKGGQTVYFG 986
|
.
gi 19112543 694 D 694
Cdd:TIGR00956 987 D 987
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
620-702 |
7.92e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 LSGGQKQRIAIARALLR---NPAFLILDEATSALD-GEAEVMVDkTIQSLMhNRSMTTITIAHKLATIRRADQIIVVG-- 693
Cdd:cd03271 170 LSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHfHDVKKLLE-VLQRLV-DKGNTVVVIEHNLDVIKCADWIIDLGpe 247
|
90
....*....|...
gi 19112543 694 ----DGKVLEQGS 702
Cdd:cd03271 248 ggdgGGQVVASGT 260
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
613-693 |
8.38e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.91 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 613 VGTRGLQ-LSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIQS----------LMHNRSMTTITIAHKLA 681
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNtvdtgrtvvcTIHQPSIDIFEAFDELL 1091
|
90
....*....|..
gi 19112543 682 TIRRADQIIVVG 693
Cdd:PLN03140 1092 LMKRGGQVIYSG 1103
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
619-654 |
1.19e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 1.19e-03
10 20 30
....*....|....*....|....*....|....*.
gi 19112543 619 QLSGGQKQRIAIARALLRNPAFLILDEATSALDGEA 654
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
620-693 |
1.68e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 LSGGQKQRIAIARALL---RNPAFLILDEATSAL---DGEAEVMVdktIQSLMHnRSMTTITIAHKLATIRRADQIIVVG 693
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYV---LQSLTH-QGHTVVIIEHNMHVVKVADYVLELG 885
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
620-695 |
2.00e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 40.32 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 620 LSGGQKQRIAIARALLRNPAFL--ILDEATSALDgEAEvmVDKTIQSLMHNRSM--TTITIAHKLATIRRADQIIVVGDG 695
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVlyVLDEPSIGLH-PRD--NDRLIETLKRLRDLgnTVLVVEHDEDTIRAADHVIDIGPG 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
611-702 |
2.25e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 611 TQVGT---RGLqlSGGQKQRIAIARALLRNPAFLILDEATSALDGEAEVMVDKTIqslmhnRSMTTITIAHKLATIRRA- 686
Cdd:TIGR00956 200 TKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRAL------KTSANILDTTPLVAIYQCs 271
|
90 100
....*....|....*....|...
gi 19112543 687 -------DQIIVVGDGKVLEQGS 702
Cdd:TIGR00956 272 qdayelfDKVIVLYEGYQIYFGP 294
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
164-427 |
2.98e-03 |
|
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: 40.20 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 164 LLLVSSGVTMSIPYIVGKILDA--GSSGDSSVTHIMgipsgtFYIGLlglFFLGSACNFGRI-----ITLRLLSERIVSR 236
Cdd:cd18583 4 CLLAERVLNVLVPRQLGIIVDSlsGGSGKSPWKEIG------LYVLL---RFLQSGGGLGLLrswlwIPVEQYSYRALST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LrarLFAKCMSLDGAFFDFHKHGDLISRLttdssIVGKSLSMYLSDGLRSSVSAIAGIGM-MLYVSMRLTGYMSLIVppI 315
Cdd:cd18583 75 A---AFNHVMNLSMDFHDSKKSGEVLKAI-----EQGSSINDLLEQILFQIVPMIIDLVIaIVYLYYLFDPYMGLIV--A 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 316 ALGAFFY------GEYVRKLSRTTQDALGDLTRVSEEKLANVRTTQAFLGERQEVNRYNDYIRNlFVLAKREAFASGiff 389
Cdd:cd18583 145 VVMVLYVwstiklTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKN-YQKAERKYLFSL--- 220
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 19112543 390 gstgFLGNATVIAILALG--------GRMVAAGDITVGQLSSFLLY 427
Cdd:cd18583 221 ----NLLNAVQSLILTLGllagcflaAYQVSQGQATVGDFVTLLTY 262
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
619-692 |
4.63e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 4.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 619 QLSGGQKQ------RIAIARALLRNPAFLILDEATSALDGE--AEVMVDkTIQSLMHNRSMTTITIAHKLATIRRADQII 690
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEniEESLAE-IIEERKSQKNFQLIVITHDEELVDAADHIY 193
|
..
gi 19112543 691 VV 692
Cdd:cd03240 194 RV 195
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
158-327 |
6.28e-03 |
|
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: 39.37 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 158 FFIAGSLLLVSSGVTMSIPYIVGKIldaGSSGDSSVTHIMGIPSGTFYIGL-LGLFFLGSACNFGRIITLRLLSerivsr 236
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIW---ASAYETSSALPPSEVSVLYYLGIyALISLLSVLLGTLRYLLFFFGS------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112543 237 LRA--RLFAKCM-SLDGA---FFDFHKHGDLISRLTTDSSIVGKSLSMYLSDGLRSSVSAIAGIGMMLYVSMrltgYMSL 310
Cdd:cd18604 72 LRAsrKLHERLLhSVLRAplrWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSP----AFLL 147
|
170
....*....|....*...
gi 19112543 311 IVPPIALGAFFYGE-YVR 327
Cdd:cd18604 148 PAVVLAALYVYIGRlYLR 165
|
|
| |
