|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-718 |
0e+00 |
|
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: 799.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 5 KKYYCVKQHDIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEeiFNNLPTP 84
Cdd:COG2274 2 RKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEE--LAELPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 85 LIAHViiDDvlLHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFLTPTAKFEKGDETKGIFQRFWGLVKVQK 164
Cdd:COG2274 80 AILHW--DG--NHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKRGEKPFGLRWFLRLLRRYR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 165 GLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGY 244
Cdd:COG2274 156 RLLLQVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 245 YNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGF 324
Cdd:COG2274 236 FRHLLRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 325 KNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGIC 404
Cdd:COG2274 316 QPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 405 LLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELEKSDDES-IKPETLAGCIS 483
Cdd:COG2274 396 LLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSkLSLPRLKGDIE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 484 LENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYIS 562
Cdd:COG2274 476 LENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVL 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 563 QDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIM 642
Cdd:COG2274 556 QDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILIL 635
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 643 DEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQT 718
Cdd:COG2274 636 DEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
12-715 |
0e+00 |
|
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: 609.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 12 QHDIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEEIFNNLPTPLIAHVII 91
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADMSLFEDKNLPLPFIAHVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 92 DDVLLHFVVVHKITKKYILIADPGR--GMIKYKPDEFFKIWSDVLIFLTPTAKFEKGDETKGIFQRFWGLVKVQKGLLLN 169
Cdd:TIGR01193 81 NGKLPHYYVVYGVTKNHLIIADPDPtvGITKISKEDFYEEWTGIAIFISPTPEYKPIKEKENSLLKFIPLITRQKKLIVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVV 249
Cdd:TIGR01193 161 IVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 250 KLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLK 329
Cdd:TIGR01193 241 ELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 330 KVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGICLLWFG 409
Cdd:TIGR01193 321 KLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 410 GSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELEKSDDESI-KPETLAGCISLENVS 488
Cdd:TIGR01193 401 AYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRtELNNLNGDIVINDVS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 489 FAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFF 568
Cdd:TIGR01193 481 YSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 569 SGTIKENLeFVG--DDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:TIGR01193 561 SGSILENL-LLGakENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 647 SNLDSITERAIQRTLEECTENvTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWT 715
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
148-721 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 563.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 148 ETKGIFQRFWGLVKVQKGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKT 227
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 228 LLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKL 306
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLtNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 307 FFTCFVPIVLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYT 386
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 387 YNVQGTLMDTISGGFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELE 466
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 467 KSD-DESIKPETLAGCISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYY 545
Cdd:COG1132 324 IPDpPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 546 IDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQ 625
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLD 705
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
570
....*....|....*.
gi 336293682 706 KGGYYYRLWTEQTLDD 721
Cdd:COG1132 564 RGGLYARLYRLQFGEE 579
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-718 |
2.37e-147 |
|
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: 446.11 E-value: 2.37e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 19 GPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEeiFNNLPTPliahVIIDDVLLHF 98
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKVSIGR--LNKLPLP----ALIDGEGGWF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 99 VVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFLTPTAKfeKGDETKGIFQRFWGLVKVQKGLLLNIFIASILVT 178
Cdd:TIGR01846 75 VLGKLTANGVTIYDPPGDAPEVLSREVLEALWSGTVILLATRSV--AGKALKFGFSWFIPAIIRYRKQFREVLLISLALQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 179 ILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGT 258
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFES 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 259 RKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVMED 338
Cdd:TIGR01846 233 RRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 339 NASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGICLLWFGGSLVLKGEV 418
Cdd:TIGR01846 313 SAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGAL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 419 TIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELEKSDDESIKPETLAGCISLENVSFAYGMRD-NV 497
Cdd:TIGR01846 393 SPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSpEV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLE 577
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 578 FVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAI 657
Cdd:TIGR01846 553 LCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALI 632
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 658 QRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQT 718
Cdd:TIGR01846 633 MRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
18-713 |
1.37e-142 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 434.37 E-value: 1.37e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 18 CGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRtsKKEEIFNNLPTPLIAHVIIDdvllH 97
Cdd:TIGR03796 13 CGAASLAMILAYYGRYVPLEELREECGVSRDGSKASNLLKAARSYGLEAKGFR--KELDALAELPLPYIVFWNFN----H 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 98 FVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFLTPTAKFEKGDETKGIFQRFWGLVKVQKGLLLNIFIASILV 177
Cdd:TIGR03796 87 FVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVVLTFEPGPEFQKGGRKPSLLRALWRRLRGSRGALLYLLLAGLLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 178 TILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFG 257
Cdd:TIGR03796 167 VLPGLVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 258 TRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVME 337
Cdd:TIGR03796 247 QRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 338 DNASLTSYLVESLEGIETVKAFNGEglvrlktENKFLKFMKSYFKhgyTYNVQ----------GTLMDTISGGFGICLLW 407
Cdd:TIGR03796 327 DAGKLTGVAISGLQSIETLKASGLE-------SDFFSRWAGYQAK---LLNAQqelgvltqilGVLPTLLTSLNSALILV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 408 FGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILD-------LELEKSDDESIKPETLAG 480
Cdd:TIGR03796 397 VGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvdpllEEPEGSAATSEPPRRLSG 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 481 CISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKIS 559
Cdd:TIGR03796 477 YVELRNITFGYSPLEPpLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVA 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEI 639
Cdd:TIGR03796 557 MVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSI 636
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 640 LIMDEATSNLDSITERAIQRTLEEctENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRL 713
Cdd:TIGR03796 637 LILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
164-457 |
1.44e-130 |
|
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: 388.34 E-value: 1.44e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18570 241 LILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
150-708 |
6.20e-109 |
|
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: 342.12 E-value: 6.20e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 150 KGIFQRFWGLVKVQKGLLLNIFIASILVTILGIAGSFYYEFLIDDILpnNLKASLHSIS---IAMLILLLFKIVTEFFRK 226
Cdd:COG4988 2 KPLDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLI--IGGAPLSALLpllGLLLAVLLLRALLAWLRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 227 TLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRFNDG-DKIRN----AISSVTLTLMIDVLMAVVggaiLYL 301
Cdd:COG4988 80 RAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGvEALDGyfarYLPQLFLAALVPLLILVA----VFP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 302 QNLK--LFFTCFVP-IVLYLILVfGFKnkLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEG----LVRLKTEN--- 371
Cdd:COG4988 156 LDWLsgLILLVTAPlIPLFMILV-GKG--AAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKaeaeRIAEASEDfrk 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 372 ---KFLK--FMKSyfkhgytynvqgTLMDTI-SGGFGICLLWFGGSLvLKGEVTIGELIsFNALLA--YFiQPIgRlinl 443
Cdd:COG4988 233 rtmKVLRvaFLSS------------AVLEFFaSLSIALVAVYIGFRL-LGGSLTLFAAL-FVLLLApeFF-LPL-R---- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 444 qpQL-------QEAIVASDRLGEILDLELEKSDDESIK-PETLAGCISLENVSFAYGMRDNVLNDINISIHNGEKIALVG 515
Cdd:COG4988 293 --DLgsfyharANGIAAAEKIFALLDAPEPAAPAGTAPlPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 516 ESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKA 595
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 596 HIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAH 675
Cdd:COG4988 451 GLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH 530
|
570 580 590
....*....|....*....|....*....|...
gi 336293682 676 RLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGG 708
Cdd:COG4988 531 RLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
152-717 |
2.04e-106 |
|
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: 335.92 E-value: 2.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 152 IFQRFWGLVKVQKGLLLnifIASILVTILGIAGSFYYEF---LIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTL 228
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLV---LAGVAMILVAATESTLAALlkpLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 229 LLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVtLTLMIDVLMAVVG--GAILYLQ-NL 304
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRItFDSEQVASAATDA-FIVLVRETLTVIGlfIVLLYYSwQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 305 KLFFTCFVPIVLYLILVFgfKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRL---KTENKFLKFMKSYF 381
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRV--SKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRrfdAVSNRNRRLAMKMT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 382 KHGYTYNVQGTLMDTISGGFgicLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEIL 461
Cdd:TIGR02203 235 SAGSISSPITQLIASLALAV---VLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 462 DLELEKsDDESIKPETLAGCISLENVSFAYGMRD-NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKII 540
Cdd:TIGR02203 312 DSPPEK-DTGTRAIERARGDVEFRNVTFRYPGRDrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 541 LNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEF-VGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNL 619
Cdd:TIGR02203 391 LDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYgRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 620 SGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGS 699
Cdd:TIGR02203 471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGT 550
|
570
....*....|....*...
gi 336293682 700 HRELLDKGGYYYRLWTEQ 717
Cdd:TIGR02203 551 HNELLARNGLYAQLHNMQ 568
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
245-714 |
1.09e-102 |
|
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: 326.34 E-value: 1.09e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 245 YNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRN---------------AISSVTLTLMIDVLMAVVGGAILylqnlkLFF 308
Cdd:COG4987 95 YRRLEPLAPAGLARLRSGDLLNRLvADVDALDNlylrvllpllvallvILAAVAFLAFFSPALALVLALGL------LLA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 309 TCFVPIVLYLILvfgfknklKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYN 388
Cdd:COG4987 169 GLLLPLLAARLG--------RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 389 VQGTLMDTISGGFGICLLWFGGSLVLKGEVTIGELISFnAL--LAYF--IQPIGRLINlqpQLQEAIVASDRLGEILDLE 464
Cdd:COG4987 241 LAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL-VLaaLALFeaLAPLPAAAQ---HLGRVRAAARRLNELLDAP 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 465 LEKSDDESIKPETLAGCISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNN 543
Cdd:COG4987 317 PAVTEPAEPAPAPGGPSLELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 544 YYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQ 623
Cdd:COG4987 397 VDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|.
gi 336293682 704 LDKGGYYYRLW 714
Cdd:COG4987 557 LAQNGRYRQLY 567
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
482-714 |
4.45e-101 |
|
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: 309.93 E-value: 4.45e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISY 560
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLW 714
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
247-724 |
2.59e-100 |
|
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: 321.00 E-value: 2.59e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 247 HVVKLPMNFFGTRKVGE---IISRfndGdkiRNAISSVTLTLMIDVL-----MAVVGGAILYLQNLKLFFTCFVPIVLYL 318
Cdd:COG5265 120 HLHALSLRFHLERQTGGlsrDIER---G---TKGIEFLLRFLLFNILptlleIALVAGILLVKYDWWFALITLVTVVLYI 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 319 ILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRlkteNKFLKFMKSY----FKHGYTYNV----Q 390
Cdd:COG5265 194 AFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREA----RRYDEALARYeraaVKSQTSLALlnfgQ 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 391 GTLmdtISGGFGIcLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELEKSDD 470
Cdd:COG5265 270 ALI---IALGLTA-MMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 471 ESIKPETL-AGCISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDI 549
Cdd:COG5265 346 PDAPPLVVgGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 550 DKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSI 629
Cdd:COG5265 426 TQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAI 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGY 709
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGL 585
|
490
....*....|....*
gi 336293682 710 YYRLWTEQTLDDEEQ 724
Cdd:COG5265 586 YAQMWARQQEEEEAE 600
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
482-717 |
1.86e-99 |
|
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: 306.08 E-value: 1.86e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILI 641
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 642 MDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQ 717
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
482-717 |
2.07e-96 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 298.30 E-value: 2.07e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN--VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKIS 559
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEI 639
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 640 LIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQ 717
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
129-713 |
3.16e-94 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 308.19 E-value: 3.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 129 IWSDVLIFLTPTAKFEKGD-ETKGIFQRFWGLVKVQKGLLLNIFIASILVTILGIAGSFYYEFLIDDILPnnlKASLHSI 207
Cdd:TIGR00958 124 LWAVLSSAGASEKEAEQGQsETADLLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGG---DKGPPAL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 208 SIAMLILLLFKI---VTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISsVTL 283
Cdd:TIGR00958 201 ASAIFFMCLLSIassVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSsDTQTMSRSLS-LNV 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 284 TLMIDVLMAVVGGAILYLQ---NLKLFFTCFVPIVLYLILVFGfkNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFN 360
Cdd:TIGR00958 280 NVLLRNLVMLLGLLGFMLWlspRLTMVTLINLPLVFLAEKVFG--KRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFA 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 361 GEGlVRLKTENKFLKFMKS-YFKHGYTYNVQGTLMDTISGGFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGR 439
Cdd:TIGR00958 358 AEE-GEASRFKEALEETLQlNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRV 436
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 440 LINLQPQLQEAIVASDRLGEILDLELEKSDDESIKPETLAGCISLENVSFAYGMRDN--VLNDINISIHNGEKIALVGES 517
Cdd:TIGR00958 437 LSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSFSYPNRPDvpVLKGLTFTLHPGEVVALVGPS 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 518 GSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHI 597
Cdd:TIGR00958 517 GSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANA 596
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 598 HEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTleECTENVTTIVIAHRL 677
Cdd:TIGR00958 597 HDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES--RSRASRTVLLIAHRL 674
|
570 580 590
....*....|....*....|....*....|....*.
gi 336293682 678 STIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRL 713
Cdd:TIGR00958 675 STVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
167-713 |
5.01e-94 |
|
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: 306.88 E-value: 5.01e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 167 LLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYN 246
Cdd:TIGR03797 138 LLAILAMGLLGTLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 247 HVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAIL--YLQNLKLFFTCFVPIVLYLILVFGF 324
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMfyYSWKLALVAVALALVAIAVTLVLGL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 325 KNkLKKVnRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGIC 404
Cdd:TIGR03797 298 LQ-VRKE-RRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLPVLTSAA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 405 LLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELEkSDDESIKPETLAGCISL 484
Cdd:TIGR03797 376 LFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPE-VDEAKTDPGKLSGAIEV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 485 ENVSFAYgmRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:TIGR03797 455 DRVTFRY--RPDgplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVV 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSGTIKENLeFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILI 641
Cdd:TIGR03797 533 LQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILL 611
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 642 MDEATSNLDSITERAIQRTLEecTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRL 713
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLE--RLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
480-708 |
7.99e-92 |
|
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: 286.04 E-value: 7.99e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 480 GCISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKIS 559
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEI 639
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 640 LIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGG 708
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
144-717 |
6.03e-88 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 287.69 E-value: 6.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 144 EKGDETKGIFQRFWGLVKVQK-GLllnifIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAM----LILLLFK 218
Cdd:PRK11176 4 DKDLSTWQTFRRLWPTIAPFKaGL-----IVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMplvvIGLMILR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 219 IVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISSVTLTLM-----IDVLMA 292
Cdd:PRK11176 79 GITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVregasIIGLFI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 293 VVggaILYLQNLKLFFTCFVPIVLYLILVFgfKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEgLVRLKTENK 372
Cdd:PRK11176 159 MM---FYYSWQLSLILIVIAPIVSIAIRVV--SKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQ-EVETKRFDK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 373 FLKFMKSyfkhgytynvQGTLM---DTISGGFGICLLWFGGSLVL--------KGEVTIGEL-ISFNALLAyFIQPIGRL 440
Cdd:PRK11176 233 VSNRMRQ----------QGMKMvsaSSISDPIIQLIASLALAFVLyaasfpsvMDTLTAGTItVVFSSMIA-LMRPLKSL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 441 INLQPQLQEAIVASDRLGEILDLELEKsDDESIKPETLAGCISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGS 519
Cdd:PRK11176 302 TNVNAQFQRGMAACQTLFAILDLEQEK-DEGKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGS 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 520 GKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDV-TYEKMVDACKKAHIH 598
Cdd:PRK11176 381 GKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAM 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 599 EYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLS 678
Cdd:PRK11176 461 DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS 540
|
570 580 590
....*....|....*....|....*....|....*....
gi 336293682 679 TIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQ 717
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
482-693 |
9.79e-81 |
|
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: 254.62 E-value: 9.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISY 560
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIKENLefvgddvtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGR 693
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
240-725 |
1.07e-79 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 266.06 E-value: 1.07e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 240 LLLGYYNHVVKLPMNFFGTRKVGEIISRFNDGDkirNAISSVTLTLMIDVLMAVVGGAIL-----YLqNLKLFFTCFVPI 314
Cdd:PRK13657 91 VLTEYFERIIQLPLAWHSQRGSGRALHTLLRGT---DALFGLWLEFMREHLATLVALVVLlplalFM-NWRLSLVLVVLG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 315 VLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNgeglvRLKTENKFLkfmksyfkHGYTYNV---Q- 390
Cdd:PRK13657 167 IVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYN-----RIEAETQAL--------RDIADNLlaaQm 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 391 --------GTLMDTISGGFGI-CLLWFGGSLVLKGEVTIGELISFNALLAYFIqpiGRL------INL----QPQLQEAI 451
Cdd:PRK13657 234 pvlswwalASVLNRAASTITMlAILVLGAALVQKGQLRVGEVVAFVGFATLLI---GRLdqvvafINQvfmaAPKLEEFF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 452 VASDRLGEILDLEleksddESIKPETLAGCISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGF 531
Cdd:PRK13657 311 EVEDAVPDVRDPP------GAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRV 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 532 YKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTP 611
Cdd:PRK13657 385 FDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTV 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 612 LEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDK 691
Cdd:PRK13657 465 VGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
490 500 510
....*....|....*....|....*....|....*.
gi 336293682 692 GRIIEEGSHRELLDKGGYYYRLWTEQ--TLDDEEQK 725
Cdd:PRK13657 545 GRVVESGSFDELVARGGRFAALLRAQgmLQEDERRK 580
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
482-717 |
1.59e-78 |
|
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: 251.25 E-value: 1.59e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRD-NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISY 560
Cdd:cd03252 1 ITFEHVRFRYKPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQ 717
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
164-457 |
1.39e-74 |
|
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: 242.85 E-value: 1.39e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18568 241 AVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
182-722 |
5.93e-73 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 248.09 E-value: 5.93e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 182 IAGSFYYEFLIDDI-----LPNNLKASLhsiSIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFF 256
Cdd:PRK10790 40 VSGPLLISYFIDNMvakgnLPLGLVAGL---AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 257 GTRKVGEIISRF-NDGDKIRNAISSVTLTlmidVL--MAVVGGAILYLQNLK----LFFTCFVPIVLYLILVFgfKNKLK 329
Cdd:PRK10790 117 DTQPVGQLISRVtNDTEVIRDLYVTVVAT----VLrsAALIGAMLVAMFSLDwrmaLVAIMIFPAVLVVMVIY--QRYST 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 330 KVNRRVmednaslTSYLVESLEGIETVkaFNGEGLVR-LKTENKFLKFMKSYFKHGYTYNVQ-----GTLMDTISGGFG- 402
Cdd:PRK10790 191 PIVRRV-------RAYLADINDGFNEV--INGMSVIQqFRQQARFGERMGEASRSHYMARMQtlrldGFLLRPLLSLFSa 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 403 --IC--LLWFGGSLVlkGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELEK--SDDESIKpe 476
Cdd:PRK10790 262 liLCglLMLFGFSAS--GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQygNDDRPLQ-- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 477 tlAGCISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRS 556
Cdd:PRK10790 338 --SGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 557 KISYISQDSFFFSGTIKENLEfVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKK 636
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVT-LGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTE 716
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQL 574
|
....*.
gi 336293682 717 QTLDDE 722
Cdd:PRK10790 575 QLAGEE 580
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
480-699 |
1.60e-72 |
|
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: 234.70 E-value: 1.60e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 480 GCISLENVSFAYgmRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRS 556
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 557 KISYISQDSFFFSGTIKENLEFVG--DDvtyEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALL 634
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLDPFGeySD---EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 635 KKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGS 699
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
164-706 |
4.36e-72 |
|
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: 244.56 E-value: 4.36e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:TIGR01842 5 KRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNffgtRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFT----CFVPIVLYLI 319
Cdd:TIGR01842 85 IFAASFSATLR----RGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILalggAVVLVGLALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 320 LVFGFKNKLKKVNRRVMEDNASLTSylveSLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISG 399
Cdd:TIGR01842 161 NNRATKKPLKEATEASIRANNLADS----ALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 400 GFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLELEKSDDESI-KPEtl 478
Cdd:TIGR01842 237 VLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLpEPE-- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 479 aGCISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSK 557
Cdd:TIGR01842 315 -GHLSVENVTIVPpGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKP 637
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 638 EILIMDEATSNLDSITERAIQRTLEEC-TENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:TIGR01842 474 KLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
159-706 |
5.57e-72 |
|
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: 244.66 E-value: 5.57e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 159 LVKVQKGLLLNIFIASILVTILGIAGSFY----YefliDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQ 234
Cdd:COG4618 14 ALRACRRAFLSVGLFSFFINLLMLTPPLYmlqvY----DRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 235 NIDVPLLLGYYNHVVKLPMNFFGTRKVgeiiSRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPI 314
Cdd:COG4618 90 RLDRRLGPRVFDAAFRAALRGGGGAAA----QALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLGLLALVGA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 315 VLylILVFGF------KNKLKKVNRRVMEDNASLTSylveSLEGIETVKAF-NGEGLVR--LKTENKFLKFmksyfkhgy 385
Cdd:COG4618 166 LV--LVALALlnerltRKPLKEANEAAIRANAFAEA----ALRNAEVIEAMgMLPALRRrwQRANARALAL--------- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 386 tynvQGTLMDtISGGFG-----------ICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVAS 454
Cdd:COG4618 231 ----QARASD-RAGGFSalskflrlllqSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAY 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 455 DRLGEILdlELEKSDDESIKPETLAGCISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYK 533
Cdd:COG4618 306 RRLNELL--AAVPAEPERMPLPRPKGRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 534 IDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENL-EFvgDDVTYEKMVDACKKAHIHEYIESLPLKYKTPL 612
Cdd:COG4618 384 PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRF--GDADPEKVVAAAKLAGVHEMILRLPDGYDTRI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 613 EEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTIKKCQKIYVMDK 691
Cdd:COG4618 462 GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlKARGATVVVITHRPSLLAAVDKLLVLRD 541
|
570
....*....|....*
gi 336293682 692 GRIIEEGSHRELLDK 706
Cdd:COG4618 542 GRVQAFGPRDEVLAR 556
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
472-694 |
1.87e-67 |
|
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: 221.58 E-value: 1.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 472 SIKPETLAGCISLENVSFAYGMRD--NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDI 549
Cdd:cd03248 2 SLAPDHLKGIVKFQNVTFAYPTRPdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 550 DKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSI 629
Cdd:cd03248 82 EHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRI 694
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
167-457 |
2.43e-66 |
|
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: 220.89 E-value: 2.43e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 167 LLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYN 246
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 247 HVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFK 325
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLtSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 326 NKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGICL 405
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 336293682 406 LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
164-457 |
3.23e-66 |
|
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: 220.84 E-value: 3.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18555 161 TRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18555 241 LILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
7-142 |
8.79e-66 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239099 [Multi-domain] Cd Length: 136 Bit Score: 213.61 E-value: 8.79e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 7 YYCVKQHDIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEEIFNNLPTPLI 86
Cdd:cd02418 1 YPYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVKADMDLFELKDIPLPFI 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 87 AHVIIDDVLLHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFLTPTAK 142
Cdd:cd02418 81 AHVIKEWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFLEPTPN 136
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
278-714 |
1.31e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 222.01 E-value: 1.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 278 ISSVTLTLM-IDVLMAVVGGAILylqnlkLFFTCFVPIVLYLIlvfGfknklKKVNRRVMEDNASLTSYLVESLEGIETV 356
Cdd:PRK11160 148 ILVLTIGLSfFDLTLALTLGGIL------LLLLLLLPLLFYRL---G-----KKPGQDLTHLRAQYRVQLTEWLQGQAEL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 357 KAFNGEGLVRLKTENKFLKFMKSYFKHGytyNVQG---TLMdTISGGFGICL-LWFGGSLVlKGEVTIGELIS--FNALL 430
Cdd:PRK11160 214 TLFGAEDRYRQQLEQTEQQWLAAQRRQA---NLTGlsqALM-ILANGLTVVLmLWLAAGGV-GGNAQPGALIAlfVFAAL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 431 AYF--IQPIGRLINlqpQLQEAIVASDRLGEILDLELEKSDDESIKPETLAGCISLENVSFAY-GMRDNVLNDINISIHN 507
Cdd:PRK11160 289 AAFeaLMPVAGAFQ---HLGQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 508 GEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEK 587
Cdd:PRK11160 366 GEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEA 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 588 MVDACKKAHIHEYIESL-PLKykTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE 666
Cdd:PRK11160 446 LIEVLQQVGLEKLLEDDkGLN--AWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 336293682 667 NVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLW 714
Cdd:PRK11160 524 NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
480-698 |
2.55e-62 |
|
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: 207.83 E-value: 2.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 480 GCISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKI 558
Cdd:cd03245 1 GRIEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPE 638
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 639 ILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEG 698
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
448-689 |
2.59e-59 |
|
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: 209.45 E-value: 2.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 448 QEAIVASDRLGEILDL-ELEKSDDESIkPETLAGCISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAK 526
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAaPRPLAGKAPV-TAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 527 LLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPL 606
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQ 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 607 KYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKI 686
Cdd:TIGR02857 447 GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRI 526
|
...
gi 336293682 687 YVM 689
Cdd:TIGR02857 527 VVL 529
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
164-457 |
3.59e-58 |
|
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: 199.26 E-value: 3.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18588 1 KKLLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18588 81 LFRHLLRLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18588 161 VTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18588 241 AILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
248-713 |
1.91e-55 |
|
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: 206.34 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 248 VVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISSVTLTLMiDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFK- 325
Cdd:TIGR00957 1048 KLRSPMSFFERTPSGNLVNRFSkELDTVDSMIPPVIKMFM-GSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYv 1126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 326 ------NKLKKVNRrvmednASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYfkhgYTYNVQGTLMDTISG 399
Cdd:TIGR00957 1127 assrqlKRLESVSR------SPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAY----YPSIVANRWLAVRLE 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 400 GFGICLLWFGGSLVLKGEVT-----IGELISFNALLAYFIQpigRLINLQPQLQEAIVASDRLGEILDLELEK--SDDES 472
Cdd:TIGR00957 1197 CVGNCIVLFAALFAVISRHSlsaglVGLSVSYSLQVTFYLN---WLVRMSSEMETNIVAVERLKEYSETEKEApwQIQET 1273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 473 IKPETL--AGCISLENVSFAY--GMrDNVLNDINISIHNGEKIALVGESGSGKTTiakLLMGFYKIDQ---GKIILNNYY 545
Cdd:TIGR00957 1274 APPSGWppRGRVEFRNYCLRYreDL-DLVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFRINEsaeGEIIIDGLN 1349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 546 IDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDdVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQ 625
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ-YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQ 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLD 705
Cdd:TIGR00957 1429 LVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
|
....*...
gi 336293682 706 KGGYYYRL 713
Cdd:TIGR00957 1509 QRGIFYSM 1516
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
448-720 |
4.20e-55 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 198.92 E-value: 4.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 448 QEAIVASDRLGEILDLELEKSDDESIKPETLAGC-ISLENVSfAYGMRDNVLND-INISIHNGEKIALVGESGSGKTTIA 525
Cdd:PRK11174 315 AQAVGAAESLVTFLETPLAHPQQGEKELASNDPVtIEAEDLE-ILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 526 KLLMGF--YkidQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIES 603
Cdd:PRK11174 394 NALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPL 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 604 LPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKC 683
Cdd:PRK11174 471 LPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW 550
|
250 260 270
....*....|....*....|....*....|....*..
gi 336293682 684 QKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQTLD 720
Cdd:PRK11174 551 DQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
209-724 |
1.77e-54 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 196.86 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 209 IAMLILLLfkivtEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISR-FNDGDKIRNAISSVTLTLmI 287
Cdd:PRK10789 45 IAVVVYLL-----RYVWRVLLFGASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARaTNDVDRVVFAAGEGVLTL-V 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 288 DVLmaVVGGAILYLQN------LKLFFTCFVPIVLYLILVFGfkNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFng 361
Cdd:PRK10789 119 DSL--VMGCAVLIVMStqiswqLTLLALLPMPVMAIMIKRYG--DQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAF-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 362 eGLVRLKTeNKFLKFMK-SYFKHGYTYNVQGTLMDTISGGFGIC-LLWFGGS--LVLKGEVTIGELISFNALLAYFIQPI 437
Cdd:PRK10789 193 -GLEDRQS-ALFAADAEdTGKKNMRVARIDARFDPTIYIAIGMAnLLAIGGGswMVVNGSLTLGQLTSFVMYLGLMIWPM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 438 GRLINLQPQLQEAIVASDRLGEILDLELEKSDDESIKPETlAGCISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGE 516
Cdd:PRK10789 271 LALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEG-RGELDVNIRQFTYPQTDHpALENVNFTLKPGQMLGICGP 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 517 SGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAH 596
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLAS 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 597 IHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHR 676
Cdd:PRK10789 430 VHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHR 509
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 336293682 677 LSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYY---YRLWT-EQTLDDEEQ 724
Cdd:PRK10789 510 LSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYrdmYRYQQlEAALDDAPE 561
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
164-457 |
2.04e-53 |
|
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: 186.26 E-value: 2.04e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18782 81 IIDHLLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18782 241 LVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
475-699 |
1.54e-52 |
|
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: 180.69 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 475 PETlaGCISLENVSFAYGMR-DNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET 553
Cdd:cd03369 2 PEH--GEIEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 554 LRSKISYISQDSFFFSGTIKENLEfvgddvTYEKMVDAckkahihEYIESLPLKyktpleEKGSNLSGGQRQRLSIARAL 633
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLD------PFDEYSDE-------EIYGALRVS------EGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 634 LKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGS 699
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
482-698 |
4.37e-50 |
|
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: 175.00 E-value: 4.37e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY---GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---R 555
Cdd:cd03257 2 LEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQDSFF-----FS--GTIKENLEFVGDDVTYEKmvdacKKAHIHEYIESLPL------KYktPLEekgsnLSGG 622
Cdd:cd03257 82 KEIQMVFQDPMSslnprMTigEQIAEPLRIHGKLSKKEA-----RKEAVLLLLVGVGLpeevlnRY--PHE-----LSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 623 QRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIV-IAHRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlQEELGLTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
405-677 |
9.11e-49 |
|
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: 179.86 E-value: 9.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 405 LLWFGGSLVLKGEVTiGELISFNAL--LAYFiQPIGRLINLQPQLQEAIVASDRLGEILDLELEKSDDESIKPETLAGC- 481
Cdd:TIGR02868 255 ALWAGGPAVADGRLA-PVTLAVLVLlpLAAF-EAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGk 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 --ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKIS 559
Cdd:TIGR02868 333 ptLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEI 639
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
250 260 270
....*....|....*....|....*....|....*...
gi 336293682 640 LIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRL 677
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
482-704 |
9.67e-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: 171.36 E-value: 9.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQ--DSFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARAL 633
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFgpenlgLPREEIRERVEEALELVGLEHLADRPP-----------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 634 LKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTI-KKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVF 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
482-694 |
1.01e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:COG4619 1 LELEGLSFRVGGK-PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSGTIKENLEFV----GDDVTYEKMVDACKKAHIHEYIeslplkyktpLEEKGSNLSGGQRQRLSIARALLKKP 637
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPfqlrERKFDRERALELLERLGLPPDI----------LDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 638 EILIMDEATSNLDS----ITERAIQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:COG4619 150 DVLLLDEPTSALDPentrRVEELLREYLAE--EGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
171-457 |
1.59e-48 |
|
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: 172.61 E-value: 1.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYY----EFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNI--DVPLLLgy 244
Cdd:cd18552 1 LALAILGMILVAATTAALawllKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVvrDLRNDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 245 YNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFV--PIVLYLILV 321
Cdd:cd18552 79 FDKLLRLPLSFFDRNSSGDLISRItNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVvlPLAALPIRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 322 FGfkNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGF 401
Cdd:cd18552 159 IG--KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 402 GICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18552 237 IALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
482-694 |
1.35e-47 |
|
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: 165.85 E-value: 1.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISY 560
Cdd:cd03246 1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIKENLefvgddvtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTE-NVTTIVIAHRLSTIKKCQKIYVMDKGRI 694
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
304-689 |
6.79e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 180.22 E-value: 6.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 304 LKLFFTCFVPivlyLILVFG-FKNKLKKVNRRV-MEDNASLTSYLVESLEGIETVKAFNGEGLVRlkteNKFLKFMKSYF 381
Cdd:PTZ00265 199 LTLCITCVFP----LIYICGvICNKKVKINKKTsLLYNNNTMSIIEEALVGIRTVVSYCGEKTIL----KKFNLSEKLYS 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 382 KhgytYNVQGTLMDTISGGF--GICL------LWFGGSLVL--------KGEVTIGELIS--FNALLAYFIQPIgrlinL 443
Cdd:PTZ00265 271 K----YILKANFMESLHIGMinGFILasyafgFWYGTRIIIsdlsnqqpNNDFHGGSVISilLGVLISMFMLTI-----I 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 444 QPQLQE---AIVASDRLGEILDLE--LEKSDDESIKPETLAgcISLENVSFAYGMRDNV--LNDINISIHNGEKIALVGE 516
Cdd:PTZ00265 342 LPNITEymkSLEATNSLYEIINRKplVENNDDGKKLKDIKK--IQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 517 SGSGKTTIAKLLMGFYKIDQGKIILNNYY-IDDIDKETLRSKISYISQDSFFFSGTIKEN----------LEFVGDDV-- 583
Cdd:PTZ00265 420 SGCGKSTILKLIERLYDPTEGDIIINDSHnLKDINLKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdLEALSNYYne 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 584 ----TYE-----------------------------------------KMVDACKKAHIHEYIESLPLKYKTPLEEKGSN 618
Cdd:PTZ00265 500 dgndSQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASK 579
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 619 LSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLSTIKKCQKIYVM 689
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
164-442 |
1.57e-46 |
|
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: 167.25 E-value: 1.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18567 161 LYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENI 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLIN 442
Cdd:cd18567 241 LVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLID 279
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
482-705 |
2.59e-46 |
|
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: 172.78 E-value: 2.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN----VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET---L 554
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 RSKISYISQD---SFFFSGTIKENLEFVGDdvTYEKMVDACKKAHIHEYIES--LPLKYKT--PLEekgsnLSGGQRQRL 627
Cdd:COG1123 341 RRRVQMVFQDpysSLNPRMTVGDIIAEPLR--LHGLLSRAERRERVAELLERvgLPPDLADryPHE-----LSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTE-NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRElGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
.
gi 336293682 705 D 705
Cdd:COG1123 494 A 494
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
482-706 |
5.57e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 163.70 E-value: 5.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYyidDIDKET--LRSKIS 559
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPaeVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFFFSG-TIKENLEFVGDdvtYEKMVDACKKAHIHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLKKPE 638
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFFAR---LYGLPRKEARERIDELLELFGLTDA--ADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 639 ILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
170-708 |
1.14e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 176.71 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHsisIAMLILLLFKIVT-----EFFRKTLLLYMAQNIDVPLLlgy 244
Cdd:PLN03232 917 LLVCYLTTEVLRVSSSTWLSIWTDQSTPKSYSPGFY---IVVYALLGFGQVAvtftnSFWLISSSLHAAKRLHDAML--- 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 245 yNHVVKLPMNFFGTRKVGEIISRFND--GDKIRNAISSVTLTL-----------MIDVLMAVVGGAILYLqnLKLFFTCF 311
Cdd:PLN03232 991 -NSILRAPMLFFHTNPTGRVINRFSKdiGDIDRNVANLMNMFMnqlwqllstfaLIGTVSTISLWAIMPL--LILFYAAY 1067
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 312 vpivLYlilvfgFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFngeglvrlKTENKFLKFMKSYFKHgytyNVQG 391
Cdd:PLN03232 1068 ----LY------YQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY--------KAYDRMAKINGKSMDN----NIRF 1125
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 392 TLMDTISGGF--------GICLLWFGGSLVLKG----EVTIGELISFNALLAYFIQPIGRLINLQPQLQEA---IVASDR 456
Cdd:PLN03232 1126 TLANTSSNRWltirletlGGVMIWLTATFAVLRngnaENQAGFASTMGLLLSYTLNITTLLSGVLRQASKAensLNSVER 1205
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 457 LGEILDLELEKSD-DESIKPET---LAGCISLENVSFAY--GMrDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMG 530
Cdd:PLN03232 1206 VGNYIDLPSEATAiIENNRPVSgwpSRGSIKFEDVHLRYrpGL-PPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 531 FYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEkMVDACKKAHIHEYIESLPLKYKT 610
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDA 1363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 611 PLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMD 690
Cdd:PLN03232 1364 EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
570
....*....|....*...
gi 336293682 691 KGRIIEEGSHRELLDKGG 708
Cdd:PLN03232 1444 SGQVLEYDSPQELLSRDT 1461
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
6-142 |
2.41e-45 |
|
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as precursor peptides containing N-terminal extensions (leader peptides) which are cleaved off during maturation. Most non-lantibiotics and also some lantibiotics have leader peptides of the so-called double-glycine type. These leader peptides share consensus sequences and also a common processing site with two conserved glycine residues in positions -1 and -2. The double- glycine-type leader peptides are unrelated to the N-terminal signal sequences which direct proteins across the cytoplasmic membrane via the sec pathway. Their processing sites are also different from typical signal peptidase cleavage sites, suggesting that a different processing enzyme is involved. Peptide bacteriocins are exported across the cytoplasmic membrane by a dedicated ATP-binding cassette (ABC) transporter. The ABC transporter is the maturation protease and its proteolytic domain resides in the N-terminal part of the protein. This peptidase domain is found in a wide range of ABC transporters, however the presumed catalytic cysteine and histidine are not conserved in all members of this family.
Pssm-ID: 367483 [Multi-domain] Cd Length: 133 Bit Score: 158.16 E-value: 2.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 6 KYYCVKQHDIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEeiFNNLPTPL 85
Cdd:pfam03412 1 KYKIVLQVDENDCGLACLAMILKYYGSNVSLEELRELAGTPAEGTSLLGLKKAAEKLGFKAKAIKADLSE--LKELPLPF 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 86 IAHviIDDVLLHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFLTPTAK 142
Cdd:pfam03412 79 IAH--WDGNGGHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLVAPKPS 133
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
482-698 |
6.06e-45 |
|
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: 159.02 E-value: 6.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIdKETLRSKISY 560
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIKENLefvgddvtyekmvdackkahiheyieslplkyktpleekGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEG 698
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
164-457 |
8.87e-45 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 162.33 E-value: 8.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18779 81 FLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18779 161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18779 241 VLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
166-704 |
1.46e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 173.29 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 166 LLLNIFIASILVTILGIAGSFYYEFLIDDIlpnNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYY 245
Cdd:PTZ00265 830 IALSILVAGGLYPVFALLYAKYVSTLFDFA---NLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLF 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 246 NHVVKLPMNFFgtrkvgeiisrfnDGDKIRNAISSVTLTLMIDVL-MAVVGGAILYLQNLKLFFTC------FVPIV--- 315
Cdd:PTZ00265 907 ENILYQEISFF-------------DQDKHAPGLLSAHINRDVHLLkTGLVNNIVIFTHFIVLFLVSmvmsfyFCPIVaav 973
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 316 ---LYLIL--VFGFKNKL---KKVNRRvmEDNASLTSYLVESLEGIETVKAF-------NGEGLVRLKTENKFLKFMKSY 380
Cdd:PTZ00265 974 ltgTYFIFmrVFAIRARLtanKDVEKK--EINQPGTVFAYNSDDEIFKDPSFliqeafyNMNTVIIYGLEDYFCNLIEKA 1051
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 381 FKHGYTYNVQGTLMDTISGGFGICL--------LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIV 452
Cdd:PTZ00265 1052 IDYSNKGQKRKTLVNSMLWGFSQSAqlfinsfaYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKL 1131
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 453 ASDRLGEILDLE--LEKSDDESIKPET---LAGCISLENVSFAYGMRDNV--LNDINISIHNGEKIALVGESGSGKTTIA 525
Cdd:PTZ00265 1132 SFEKYYPLIIRKsnIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVM 1211
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 526 KLLMGFYKI------------------------------------------------------DQGKIILNNYYIDDIDK 551
Cdd:PTZ00265 1212 SLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNL 1291
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 552 ETLRSKISYISQDSFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIAR 631
Cdd:PTZ00265 1292 KDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIAR 1371
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 632 ALLKKPEILIMDEATSNLDSITERAIQRTLEECTENV--TTIVIAHRLSTIKKCQKIYVMDK----GRIIE-EGSHRELL 704
Cdd:PTZ00265 1372 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELL 1451
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
482-705 |
6.87e-44 |
|
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: 158.43 E-value: 6.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKI 558
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSF-----FFS--GTIKENLEFVGDDVTYEKMVDACKKAHiheyiesLP--LKYKTPLEekgsnLSGGQRQRLSI 629
Cdd:COG1124 82 QMVFQDPYaslhpRHTvdRILAEPLRIHGLPDREERIAELLEQVG-------LPpsFLDRYPHQ-----LSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLD 705
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
167-437 |
1.10e-43 |
|
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: 158.58 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 167 LLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSI--SIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGY 244
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNvySLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 245 YNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFF--TCFVPIVLYLILV 321
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLtNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLvlLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 322 FGfkNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGF 401
Cdd:pfam00664 161 FA--KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLS 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 336293682 402 GICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPI 437
Cdd:pfam00664 239 YALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
498-647 |
9.34e-43 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 151.65 E-value: 9.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSG-TIKENL 576
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 577 EFVGDDVTYEKMVdacKKAHIHEYIESLPLKY--KTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATS 647
Cdd:pfam00005 81 RLGLLLKGLSKRE---KDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
483-693 |
1.01e-42 |
|
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: 153.78 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGMRD-NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:cd03225 1 ELKNLSFSYPDGArPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQ--DSFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARAL 633
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 634 LKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGR 693
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
230-708 |
6.60e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 164.91 E-value: 6.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 230 LYMAQNIDVPLLlgyyNHVVKLPMNFFGTRKVGEIISRF--NDGDKIRNA-------ISSVTLTLMIDVLMAVVGG---- 296
Cdd:PLN03130 982 LYAAKRLHDAML----GSILRAPMSFFHTNPLGRIINRFakDLGDIDRNVavfvnmfLGQIFQLLSTFVLIGIVSTislw 1057
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 297 AILYLqnLKLFFTCFvpivLYlilvfgFKNKLKKVNRrvMEdnaSLTSYLV-----ESLEGIETVKAFngeglvrlkten 371
Cdd:PLN03130 1058 AIMPL--LVLFYGAY----LY------YQSTAREVKR--LD---SITRSPVyaqfgEALNGLSTIRAY------------ 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 372 kflkfmKSYFKHGytyNVQGTLMDT--------ISGG---------FGICLLWFGGSLVLKGEV----------TIGELI 424
Cdd:PLN03130 1109 ------KAYDRMA---EINGRSMDNnirftlvnMSSNrwlairletLGGLMIWLTASFAVMQNGraenqaafasTMGLLL 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 425 SFNALLAYFIQPIGRLINLQpqlQEAIVASDRLGEILDLELEKSDD-ESIKPET---LAGCISLENVSFAYgmRDN---V 497
Cdd:PLN03130 1180 SYALNITSLLTAVLRLASLA---ENSLNAVERVGTYIDLPSEAPLViENNRPPPgwpSSGSIKFEDVVLRY--RPElppV 1254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLe 577
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL- 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 578 fvgDDVTYEKMVD---ACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITE 654
Cdd:PLN03130 1334 ---DPFNEHNDADlweSLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 655 RAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGG 708
Cdd:PLN03130 1411 ALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
482-708 |
7.42e-42 |
|
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: 152.70 E-value: 7.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtLRSKISYI 561
Cdd:COG4555 2 IEVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG-TIKENLEFVGddvTYEKMVDACKKAHIHEYIESLPLKykTPLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFA---ELYGLFDEELKKRIEELIELLGLE--EFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDKGG 708
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
482-697 |
1.26e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 151.35 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---- 554
Cdd:COG1136 5 LELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 RSKISYISQDSFFFSG-TIKENLEFVgddVTYEKMVDACKKAHIHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARAL 633
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALP---LLLAGVSRKERRERARELLERVGLGDR--LDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 634 LKKPEILIMDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEE 697
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
164-450 |
2.01e-41 |
|
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: 153.06 E-value: 2.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGI 403
Cdd:cd18783 161 FLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 336293682 404 CLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEA 450
Cdd:cd18783 241 GVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEA 287
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
191-457 |
3.02e-41 |
|
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: 152.25 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 191 LIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRF-N 269
Cdd:cd18576 22 LIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLsN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 270 DGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKL--FFTCFVPIVLYLILVFGfkNKLKKVNRRVMEDNASLTSYLV 347
Cdd:cd18576 102 DVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLtlLMLATVPVVVLVAVLFG--RRIRKLSKKVQDELAEANTIVE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 348 ESLEGIETVKAFNGEGLVRlkteNKFLKFMKSYFKHGYTY-NVQGTLMDTIS-GGFG--ICLLWFGGSLVLKGEVTIGEL 423
Cdd:cd18576 180 ETLQGIRVVKAFTREDYEI----ERYRKALERVVKLALKRaRIRALFSSFIIfLLFGaiVAVLWYGGRLVLAGELTAGDL 255
|
250 260 270
....*....|....*....|....*....|....*
gi 336293682 424 ISFnALLAYFI-QPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18576 256 VAF-LLYTLFIaGSIGSLADLYGQLQKALGASERV 289
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
483-693 |
8.48e-41 |
|
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: 146.62 E-value: 8.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYIS 562
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 563 QdsfffsgtikenlefvgddvtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEILIM 642
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 643 DEATSNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTIKK-CQKIYVMDKGR 693
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELaADRVIVLKDGK 157
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
171-457 |
1.41e-40 |
|
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: 150.66 E-value: 1.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVK 250
Cdd:cd18542 5 ILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 251 LPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKL--FFTCFVPIVLYLILVFGfkNK 327
Cdd:cd18542 85 LSFSFHDKARTGDLMSRCtSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtlISLAIIPFIALFSYVFF--KK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 328 LKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEglvrlKTE-NKFLKFMKSYFKHGY-TYNVQGT---LMDTISGGFG 402
Cdd:cd18542 163 VRPAFEEIREQEGELNTVLQENLTGVRVVKAFARE-----DYEiEKFDKENEEYRDLNIkLAKLLAKywpLMDFLSGLQI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 403 ICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPI---GRLINLqpqLQEAIVASDRL 457
Cdd:cd18542 238 VLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVrqlGRLIND---MSRASASAERI 292
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
482-693 |
2.20e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 147.23 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN----VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddidketlrSK 557
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------------GS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSGTIKENLEFvG---DDVTYEKMVDACkkaHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALL 634
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILF-GkpfDEERYEKVIKAC---ALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 635 KKPEILIMDEATSNLDSITERAIqrtLEEC-----TENVTTIVIAHRLSTIKKCQKIYVMDKGR 693
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHI---FENCilgllLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
482-705 |
3.13e-39 |
|
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: 145.12 E-value: 3.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---RSK 557
Cdd:COG1127 6 IEVRNLTKSFG--DRvVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKENLEF-------VGDDVTyEKMVDAC-KKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLS 628
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFplrehtdLSEAEI-RELVLEKlELVGLPGAADKMP-----------SELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 629 IARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLD 705
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
482-703 |
5.16e-39 |
|
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: 143.86 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKI-----DQGKIILN--NYYIDDIDKETL 554
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDgkDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 RSKISYISQDSFFFSGTIKENLEFV-------GDDVTYEKMVDACKKAHIHEYIeslplkyKTPLeeKGSNLSGGQRQRL 627
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEV-------KDRL--HALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKC-QKIYVMDKGRIIEEGSHREL 703
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
171-456 |
6.08e-39 |
|
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: 145.99 E-value: 6.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYYEFLIDDILPNNLK--ASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNI------DVplll 242
Cdd:cd18544 5 LLLLLLATALELLGPLLIKRAIDDYIVPGQGdlQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIiydlrrDL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 243 gyYNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILV 321
Cdd:cd18544 81 --FSHIQRLPLSFFDRTPVGRLVTRVtNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLAT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 322 FGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGlvrlKTENKF----LKFMKSYFKHGYTYNVQGTLMDTI 397
Cdd:cd18544 159 YLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREK----REFEEFdeinQEYRKANLKSIKLFALFRPLVELL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 398 SGGFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18544 235 SSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAER 293
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
482-705 |
8.84e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 150.82 E-value: 8.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID---QGKIILNNYYIDDIDKETLRSK 557
Cdd:COG1123 5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQD--SFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSI 629
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEalenlgLSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTI-KKCQKIYVMDKGRIIEEGSHRELLD 705
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
170-456 |
1.35e-38 |
|
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: 144.92 E-value: 1.35e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVV 249
Cdd:cd18545 5 ALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 250 KLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKL 328
Cdd:cd18545 85 KLSFSFFDSRPVGKILSRViNDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 329 KKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGlvrlKTENKF----LKFMKSYFKHGYTYNVQGTLMDTISgGFGIC 404
Cdd:cd18545 165 RKAWQRVRKKISNLNAYLHESISGIRVIQSFARED----ENEEIFdelnRENRKANMRAVRLNALFWPLVELIS-ALGTA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 405 L-LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18545 240 LvYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAER 292
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
482-698 |
1.42e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.50 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET---LRSKI 558
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQD-SFFFSGTIKENLEFVGdDVTYEKMVDAckKAHIHEYIESLPLKYKT---PLEekgsnLSGGQRQRLSIARALL 634
Cdd:COG2884 82 GVVFQDfRLLPDRTVYENVALPL-RVTGKSRKEI--RRRVREVLDLVGLSDKAkalPHE-----LSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 635 KKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKKCQK-IYVMDKGRIIEEG 698
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
482-694 |
2.29e-38 |
|
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: 141.86 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNN---YYIDDIDKETLR 555
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 -SKISYISQD----SFFfsgTIKENLEFVgddVTYEKMVDACKKAHIHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIA 630
Cdd:cd03255 81 rRHIGFVFQSfnllPDL---TALENVELP---LLLAGVPKKERRERAEELLERVGLGDR--LNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEECTENV-TTIVIA-HRLSTIKKCQKIYVMDKGRI 694
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
482-694 |
2.32e-38 |
|
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: 140.23 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDiDKETLRSKISYI 561
Cdd:cd03230 1 IEVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG-TIKENLEfvgddvtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03230 79 PEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRI 694
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
482-693 |
3.90e-38 |
|
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: 139.63 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET--LRSKIS 559
Cdd:cd03229 1 LELKNVSKRYGQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFFFSG-TIKENLEFVgddvtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPE 638
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 639 ILIMDEATSNLDSITERAIQRTLEECTEN--VTTIVIAHRLSTIKK-CQKIYVMDKGR 693
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
482-704 |
4.25e-38 |
|
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: 141.56 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---R 555
Cdd:cd03258 2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQD-SFFFSGTIKENlefvgddVTYEKMVDACKKAHIHEYIESLpLKYkTPLEEKG----SNLSGGQRQRLSIA 630
Cdd:cd03258 82 RRIGMIFQHfNLLSSRTVFEN-------VALPLEIAGVPKAEIEERVLEL-LEL-VGLEDKAdaypAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEE--CTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
482-705 |
2.32e-37 |
|
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: 139.56 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDD---IDKETLRSKI 558
Cdd:cd03261 1 IELRGLTKSFGGR-TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-TIKENLEFvgddvtyekmvdackkahiheyieslPLKYKTPLEEK-------------G-------- 616
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAF--------------------------PLREHTRLSEEeireivlekleavGlrgaedly 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 617 -SNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKG 692
Cdd:cd03261 134 pAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDG 213
|
250
....*....|...
gi 336293682 693 RIIEEGSHRELLD 705
Cdd:cd03261 214 KIVAEGTPEELRA 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
482-697 |
3.05e-37 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 138.76 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtlrskI 558
Cdd:cd03293 1 LEVRNVSKTYGGGGGavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQ-DSFFFSGTIKEN----LEFVGddvtyekMVDACKKAHIHEYIESLPLK---YKTPLEekgsnLSGGQRQRLSIA 630
Cdd:cd03293 76 GYVFQqDALLPWLTVLDNvalgLELQG-------VPKAEARERAEELLELVGLSgfeNAYPHQ-----LSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEE--CTENVTTIVIAHRLS-TIKKCQKIYVMDK--GRIIEE 697
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
164-457 |
5.50e-37 |
|
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: 140.41 E-value: 5.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMID--------VLMAVVGGAILylqnlklfftcFVPIV 315
Cdd:cd18566 81 AFEHLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDlpfvliflGLIWYLGGKLV-----------LVPLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 316 LYLILVFG-------FKNKLKKVNRRvmedNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYN 388
Cdd:cd18566 150 LLGLFVLVaillgpiLRRALKERSRA----DERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINA 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 389 VQGTLMDTISGGFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18566 226 VAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
482-705 |
7.98e-37 |
|
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: 140.57 E-value: 7.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYK---IDQGKIILNNYYIDDIDKETLR 555
Cdd:COG0444 2 LEVRNLKVYFPTRRGvvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 S----KISYISQDSF------FfsgTIKENLE-------FVGDDVTYEKMVDACKKAHIHEYIESLPlKYktPLEekgsn 618
Cdd:COG0444 82 KirgrEIQMIFQDPMtslnpvM---TVGDQIAeplrihgGLSKAEARERAIELLERVGLPDPERRLD-RY--PHE----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 619 LSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIV-IAHRLSTIKK-CQKIYVMDKGRII 695
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlQRELGLAILfITHDLGVVAEiADRVAVMYAGRIV 230
|
250
....*....|
gi 336293682 696 EEGSHRELLD 705
Cdd:COG0444 231 EEGPVEELFE 240
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
481-694 |
1.04e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 481 CISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKETLRSKISY 560
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTV-----RLFGKPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQ-----DSFFFSGtikenLEFVG-------------DDVTYEKMVDACKKAHIHEYIeslplkyKTPLeekgSNLSGG 622
Cdd:COG1121 80 VPQraevdWDFPITV-----RDVVLmgrygrrglfrrpSRADREAVDEALERVGLEDLA-------DRPI----GELSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 623 QRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
482-704 |
5.34e-36 |
|
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: 135.89 E-value: 5.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISY- 560
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIKENLEFVgddVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03295 81 IQQIGLFPHMTVEENIALV---PKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENV--TTIVIAHRL-STIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
253-703 |
8.32e-36 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 146.08 E-value: 8.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 253 MNFFGTRKVGEIISRFN-DGDKIRNAISSVTLTLMiDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKV 331
Cdd:PTZ00243 1046 MSFFDTTPLGRILNRFSrDIDILDNTLPMSYLYLL-QCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFYNSANRE 1124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 332 NRRVME-DNASLTSYLVESLEGIETVKAFNGEGLVRLKTenkfLKFMKSYFKHGYTYNVQ----GTLMDTISG--GFGIC 404
Cdd:PTZ00243 1125 IRRIKSvAKSPVFTLLEEALQGSATITAYGKAHLVMQEA----LRRLDVVYSCSYLENVAnrwlGVRVEFLSNivVTVIA 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 405 LLWFGGSLVLKGEVTIGeLISFNALLA----------------------------YFIQPIGRliNLQPQLQEAI----- 451
Cdd:PTZ00243 1201 LIGVIGTMLRATSQEIG-LVSLSLTMAmqttatlnwlvrqvatveadmnsverllYYTDEVPH--EDMPELDEEVdaler 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 452 ---VASDRLGEILdleLEKSDDESIKPETL-AGCISLENVSFAYgmRDN---VLNDINISIHNGEKIALVGESGSGKTTi 524
Cdd:PTZ00243 1278 rtgMAADVTGTVV---IEPASPTSAAPHPVqAGSLVFEGVQMRY--REGlplVLRGVSFRIAPREKVGIVGRTGSGKST- 1351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 525 akLLMGFYKIDQ---GKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKEN---------------LEFVG--DDVT 584
Cdd:PTZ00243 1352 --LLLTFMRMVEvcgGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNvdpfleassaevwaaLELVGlrERVA 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 585 YEKmvdackkahihEYIESLPLkyktpleEKGSNLSGGQRQRLSIARALLKKPEILI-MDEATSNLDSITERAIQRTLEE 663
Cdd:PTZ00243 1430 SES-----------EGIDSRVL-------EGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQATVMS 1491
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 336293682 664 CTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:PTZ00243 1492 AFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
482-704 |
1.62e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.50 E-value: 1.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG-MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISY 560
Cdd:PRK13632 8 IKVENVSFSYPnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQ--DSFFFSGTIKENLEFVGDD--VTYEKM----VDACKKAHIHEYIESLPLkyktpleekgsNLSGGQRQRLSIARA 632
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGLENkkVPPKKMkdiiDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 633 LLKKPEILIMDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
170-456 |
2.13e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 136.10 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILVTILGIAGSFYYEFLIDDILPNN-LKASLHSISIAMLILLLFKIVTEFF---RKTLLLYMAQNIDVPLLLGYY 245
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDDVLIQLgPGGNTSLLLLLVLGLAGAYVLSALLgilRGRLLARLGERITADLRRDLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 246 NHVVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGF 324
Cdd:cd18563 84 EHLQRLSLSFFDKRQTGSLMSRVTsDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 325 KNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEG--LVRLKTENKflKFMKSYFKHGYTYNVQGTLMDTISGGFG 402
Cdd:cd18563 164 WKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKreIKRFDEANQ--ELLDANIRAEKLWATFFPLLTFLTSLGT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 403 ICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18563 242 LIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAER 295
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
483-683 |
2.87e-35 |
|
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: 132.77 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDKETLRSKISYIS 562
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 563 QDS--FFFSGTIKENLEFvGDDVTYEKMVDA---CKKAHIHEYIESLPLkyktpleekgsNLSGGQRQRLSIARALLKKP 637
Cdd:cd03226 78 QDVdyQLFTDSVREELLL-GLKELDAGNEQAetvLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 336293682 638 EILIMDEATSNLDSITERAIQRTLEECT-ENVTTIVIAHRLSTIKKC 683
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKV 192
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
478-706 |
3.91e-35 |
|
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: 133.88 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 478 LAGCISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRS 556
Cdd:cd03288 16 LGGEIKIHDLCVRYeNNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 557 KISYISQDSFFFSGTIKENLE---FVGDDVTYEkmvdACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARAL 633
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDpecKCTDDRLWE----ALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 634 LKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:cd03288 172 VRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
164-457 |
9.08e-34 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 131.06 E-value: 9.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFG 323
Cdd:cd18569 81 FFWHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAfNGeglvrlkTENKFlkfmksyFKH--GY---------TYNVQGT 392
Cdd:cd18569 161 VSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKA-SG-------AESDF-------FSRwaGYqakvlnaqqELGRTNQ 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 393 LMDTI----SGGFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18569 226 LLGALptllSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
482-705 |
3.23e-33 |
|
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: 127.55 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDK----ETLRSK 557
Cdd:cd03224 1 LEVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG---RDITGlpphERARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKENLEfVGddvtyekmVDACKKAHIHEYIESL----P-LKYKtpLEEKGSNLSGGQRQRLSIAR 631
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLL-LG--------AYARRRAKRKARLERVyelfPrLKER--RKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 632 ALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVIAHRLstiKKCQKI----YVMDKGRIIEEGSHRELLD 705
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNA---RFALEIadraYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
482-698 |
3.92e-33 |
|
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: 126.87 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKETL---RSKI 558
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-----LIDGRDVTGVppeRRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQD-SFFFSGTIKENLEFVGDDvtyEKMVDACKKAHIHEYIESLPLKykTPLEEKGSNLSGGQRQRLSIARALLKKP 637
Cdd:cd03259 75 GMVFQDyALFPHLTVAENIAFGLKL---RGVPKAEIRARVRELLELVGLE--GLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 638 EILIMDEATSNLDSITERAIQRTLEECTEN--VTTIVIAH------RLSTikkcqKIYVMDKGRIIEEG 698
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHdqeealALAD-----RIAVMNEGRIVQVG 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
482-707 |
4.07e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.98 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDidkET---LRSK 557
Cdd:PRK13635 6 IRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE---ETvwdVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQ--DSFFFSGTikenlefVGDDVTY---------EKMV----DACKKAHIHEYIESLPlkyktpleekgSNLSGG 622
Cdd:PRK13635 83 VGMVFQnpDNQFVGAT-------VQDDVAFglenigvprEEMVervdQALRQVGMEDFLNREP-----------HRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 623 QRQRLSIARALLKKPEILIMDEATSNLDSITER---AIQRTLEEcTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGS 699
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRRevlETVRQLKE-QKGITVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
|
....*...
gi 336293682 700 HRELLDKG 707
Cdd:PRK13635 224 PEEIFKSG 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
483-698 |
5.21e-33 |
|
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: 125.24 E-value: 5.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYIS 562
Cdd:cd03214 1 EVENLSVGYGGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 563 QdsfffsgtikeNLEFVGddvtyekmvdackkahiheyIESLPLKyktPLEEkgsnLSGGQRQRLSIARALLKKPEILIM 642
Cdd:cd03214 80 Q-----------ALELLG--------------------LAHLADR---PFNE----LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 643 DEATSNLD-----SITERAIQRTLEectENVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEG 698
Cdd:cd03214 122 DEPTSHLDiahqiELLELLRRLARE---RGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
482-706 |
5.30e-33 |
|
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: 127.30 E-value: 5.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---RSKI 558
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDsFFFSG--TIKENL--EFVGDDVTYEKMVDACKKAHIHEYIESLPlkyKTPLEEKG----SNLSGGQRQRLSIA 630
Cdd:cd03256 81 GMIFQQ-FNLIErlSVLENVlsGRLGRRSTWRSLFGLFPKEEKQRALAALE---RVGLLDKAyqraDQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTE-NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRiNREeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
482-697 |
7.95e-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: 7.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtlrskI 558
Cdd:COG1116 8 LELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDsffFS----GTIKENLEFVGDDVTYEKmvdACKKAHIHEYIESLPL-----KYktPLEekgsnLSGGQRQRLSI 629
Cdd:COG1116 83 GVVFQE---PAllpwLTVLDNVALGLELRGVPK---AERRERARELLELVGLagfedAY--PHQ-----LSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEE--CTENVTTIVIAH------RLStikkcQKIYVMDK--GRIIEE 697
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLA-----DRVVVLSArpGRIVEE 222
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-456 |
1.27e-32 |
|
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: 128.04 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYYEFLIDDIL-PNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVV 249
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVTiGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 250 KLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKL 328
Cdd:cd18778 85 RLSLRYFDDRQTGDLMSRViNDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 329 KKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGICLLWF 408
Cdd:cd18778 165 RPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGF 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 336293682 409 GGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18778 245 GGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAER 292
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
171-457 |
2.11e-32 |
|
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: 127.16 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLI-LLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVV 249
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVaLFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 250 KLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKL 328
Cdd:cd18551 81 RLPVSFFDRRRSGDLVSRVtNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 329 KKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGICLLWF 408
Cdd:cd18551 161 RKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 336293682 409 GGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18551 241 GGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
494-697 |
2.12e-32 |
|
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: 126.46 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 494 RDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNN---YYIDDIDKETLRSKISYISQDSFFFSG 570
Cdd:TIGR02769 23 RAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGqdlYQLDRKQRRAFRRDVQLVFQDSPSAVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 TIKENLEFVGDDVT-YEKMVDACKKAHIHEYIESLPLKYKTpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNL 649
Cdd:TIGR02769 103 PRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSED-ADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 336293682 650 DSITERAIQRTLEECTENVTT--IVIAHRLSTIKK-CQKIYVMDKGRIIEE 697
Cdd:TIGR02769 182 DMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
482-706 |
3.56e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 3.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKETLRSK---I 558
Cdd:COG3839 4 LELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI-----LIGGRDVTDLPPKdrnI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQdSF--FFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIA 630
Cdd:COG3839 78 AMVFQ-SYalYPHMTVYENIAFplklrkVPKAEIDRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 631 RALLKKPEILIMDEATSNLDS------ITE-RAIQRTLeecteNVTTIVIAH------RLSTikkcqKIYVMDKGRIIEE 697
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAklrvemRAEiKRLHRRL-----GTTTIYVTHdqveamTLAD-----RIAVMNDGRIQQV 215
|
....*....
gi 336293682 698 GSHRELLDK 706
Cdd:COG3839 216 GTPEELYDR 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
482-699 |
5.18e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 127.50 E-value: 5.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---R 555
Cdd:COG1135 2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQdSF--FFSGTIKEN----LEFVGddvtyekmVDackKAHIHEYIESLpLKYkTPLEEKG----SNLSGGQRQ 625
Cdd:COG1135 82 RKIGMIFQ-HFnlLSSRTVAENvalpLEIAG--------VP---KAEIRKRVAEL-LEL-VGLSDKAdaypSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDSITERAI-------QRTLeecteNVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEE 697
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSIldllkdiNREL-----GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
..
gi 336293682 698 GS 699
Cdd:COG1135 223 GP 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
482-706 |
6.00e-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: 124.37 E-value: 6.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtlRSKISYI 561
Cdd:cd03299 1 LKVENLSKDWK--EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG-TIKENLEFVGDDVTYEKmvdACKKAHIHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGLKKRKVDK---KEIERKVLEIAEMLGIDHL--LNRKPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
483-692 |
8.81e-32 |
|
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: 123.03 E-value: 8.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKETLRSKISYIS 562
Cdd:cd03235 1 EVEDLTVSYGGH-PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSI-----RVFGKPLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 563 QDSFF---FSGTIKEnleFVGDDVTYEK-MVDACKKAHIHEYIESLPlkyKTPLEEKG----SNLSGGQRQRLSIARALL 634
Cdd:cd03235 75 QRRSIdrdFPISVRD---VVLMGLYGHKgLFRRLSKADKAKVDEALE---RVGLSELAdrqiGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 635 KKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTI-KKCQKIYVMDKG 692
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
482-707 |
1.37e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.09 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISY 560
Cdd:PRK13648 8 IVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQ--DSFFFSGTIKENLEFVGDD--VTYEKMVDACKKA----HIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARA 632
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEP-----------NALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 633 LLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKG 707
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
482-705 |
1.41e-31 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 123.62 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:COG1120 2 LEAENLSVGYGGR-PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFF-FSGTIkenLEFVG---------------DDvtYEKMVDACKKAHIHEYIEslplkykTPLEEkgsnLSGGQRQ 625
Cdd:COG1120 81 PQEPPApFGLTV---RELVAlgryphlglfgrpsaED--REAVEEALERTGLEHLAD-------RPVDE----LSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDsIteRAIQRTLEEC-----TENVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGS 699
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLD-L--AHQLEVLELLrrlarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
....*.
gi 336293682 700 HRELLD 705
Cdd:COG1120 222 PEEVLT 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
482-698 |
1.51e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.61 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLL--M-----GFyKIDqGKIILN--NYYIDDIDK 551
Cdd:COG1117 12 IEVRNLNVYYG--DKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMndlipGA-RVE-GEILLDgeDIYDPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 552 ETLRSKISYISQDSFFFSGTIKENlefvgddVTYE-KMVDACKKAHIHEYIESLpLKY-------KTPLEEKGSNLSGGQ 623
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDN-------VAYGlRLHGIKSKSELDEIVEES-LRKaalwdevKDRLKKSALGLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVtTIVI-------AHRLStikkcQKIYVMDKGRIIE 696
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY-TIVIvthnmqqAARVS-----DYTAFFYLGELVE 233
|
..
gi 336293682 697 EG 698
Cdd:COG1117 234 FG 235
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
171-457 |
3.22e-31 |
|
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: 123.68 E-value: 3.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYYEFLIDDILPNNL-KASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVV 249
Cdd:cd18541 5 ILFLILVDLLQLLIPRIIGRAIDALTAGTLtASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 250 KLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKL 328
Cdd:cd18541 85 TLSPSFYQKNRTGDLMARAtNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 329 KKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGlvrlKTENKFLKFMKSYFKHGYTYN-VQGTLMDTISGGFGIC--- 404
Cdd:cd18541 165 HKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEE----AEIERFDKLNEEYVEKNLRLArVDALFFPLIGLLIGLSfli 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 405 LLWFGGSLVLKGEVTIGELISFNALLAYFIQP---IGRLINLqpqLQEAIVASDRL 457
Cdd:cd18541 241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPmmaLGWVINL---IQRGAASLKRI 293
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
497-698 |
7.31e-31 |
|
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: 119.58 E-value: 7.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMG--FYKIDQGKIILNNYyidDIDKETLRSKISYISQDSFFFSG-TIK 573
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPTlTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 574 ENLEFVgddvtyekmvdackkAHIheyieslplkyktpleekgSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSIT 653
Cdd:cd03213 101 ETLMFA---------------AKL-------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 336293682 654 ERAIQRTL-EECTENVTTIVIAHRLST--IKKCQKIYVMDKGRIIEEG 698
Cdd:cd03213 147 ALQVMSLLrRLADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
482-705 |
7.58e-31 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 121.25 E-value: 7.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKE--TLRSKI 558
Cdd:COG1126 2 IEIENLHKSFG--DLeVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQdSFffsgtikeNLeF----VGDDVTYEKMV-------DACKKAHihEYIEslplkyKTPLEEKG----SNLSGGQ 623
Cdd:COG1126 80 GMVFQ-QF--------NL-FphltVLENVTLAPIKvkkmskaEAEERAM--ELLE------RVGLADKAdaypAQLSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLD--SITE--RAIqRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:COG1126 142 QQRVAIARALAMEPKVMLFDEPTSALDpeLVGEvlDVM-RDLAK--EGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEG 218
|
....*..
gi 336293682 699 SHRELLD 705
Cdd:COG1126 219 PPEEFFE 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
482-703 |
1.23e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 120.93 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---RSKI 558
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQD---------------------SFFFSGTikenlefvgddvtyeKMVDACKKAHIHEYIESLPLKYKtpLEEKGS 617
Cdd:COG3638 83 GMIFQQfnlvprlsvltnvlagrlgrtSTWRSLL---------------GLFPPEDRERALEALERVGLADK--AYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 618 NLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTL-EECTE-NVTTIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:COG3638 146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
|
....*....
gi 336293682 695 IEEGSHREL 703
Cdd:COG3638 226 VFDGPPAEL 234
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
482-697 |
2.10e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 120.95 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY--------GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKE- 552
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 553 --TLRSKISYISQDSF-------FFSGTIKENLEFVGDdvtyekMVDACKKAHIHEYIESLPLKyKTPLEEKGSNLSGGQ 623
Cdd:PRK10419 84 rkAFRRDIQMVFQDSIsavnprkTVREIIREPLRHLLS------LDKAERLARASEMLRAVDLD-DSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTT--IVIAHRLSTIKK-CQKIYVMDKGRIIEE 697
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVET 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
482-703 |
2.10e-30 |
|
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: 119.15 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDiDKETLRSKISY 560
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSG-TIKENLEFV----GDDVTYEKMVdackkahIHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLK 635
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYarlkGLPKSEIKEE-------VELLLRVLGLTDK--ANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAH------RLstikkCQKIYVMDKGRIIEEGSHREL 703
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeAL-----CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
171-457 |
2.62e-30 |
|
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: 121.13 E-value: 2.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVK 250
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 251 LPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYL--QNLKLFFTCFVPIVLYLILVFGFKnk 327
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLsSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFIlsWKLTLVLLLVIPLLLIASKIYGRY-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 328 LKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGlvrlKTENKFlkfmKSYFKHGYTYNVQGTLMDTISGGFGICL-- 405
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEE----KEIRRY----SEALDRSYRLARKKALANALFQGITSLLiy 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 406 ------LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18557 232 lslllvLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
248-706 |
2.69e-30 |
|
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: 128.49 E-value: 2.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 248 VVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGgAILYLQNLKLF-FTCFVP-IVLYLILVFGFK 325
Cdd:TIGR01271 968 VLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLG-AIFVVSVLQPYiFIAAIPvAVIFIMLRAYFL 1046
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 326 NKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGL--------VRLKTENKFLkfmksyfkhgYTYNVQGTLM--D 395
Cdd:TIGR01271 1047 RTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYfetlfhkaLNLHTANWFL----------YLSTLRWFQMriD 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 396 TISGGFGICLLWFGGSLVLKGEVTIGELISfnalLAyfiqpigrlINLQPQLQEAIVAS----------DRLGEILDLEL 465
Cdd:TIGR01271 1117 IIFVFFFIAVTFIAIGTNQDGEGEVGIILT----LA---------MNILSTLQWAVNSSidvdglmrsvSRVFKFIDLPQ 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 466 EKSD-DESIKPETLAGCISLEN-------------------VSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIA 525
Cdd:TIGR01271 1184 EEPRpSGGGGKYQLSTVLVIENphaqkcwpsggqmdvqgltAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLL 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 526 KLLMGFYKIDqGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENLEfvgddvTYEKMVD-----ACKKAHIHEY 600
Cdd:TIGR01271 1263 SALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD------PYEQWSDeeiwkVAEEVGLKSV 1335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 601 IESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTI 680
Cdd:TIGR01271 1336 IEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEAL 1415
|
490 500
....*....|....*....|....*.
gi 336293682 681 KKCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:TIGR01271 1416 LECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
164-451 |
2.91e-30 |
|
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: 121.02 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNI------D 237
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIetdmrrD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 238 VplllgyYNHVVKLPMNFFGTRKVGEIISRfndgdkIRNAISSVT-------LTLMIDVLMAVVGGAILYLQNLKLFFTC 310
Cdd:cd18549 81 L------FEHLQKLSFSFFDNNKTGQLMSR------ITNDLFDISelahhgpEDLFISIITIIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 311 FVPIVLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTE---NKFLKFMKSYFKH-GYT 386
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDegnDRFLESKKKAYKAmAYF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 387 YNVQGTLMDTISggfgICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAI 451
Cdd:cd18549 229 FSGMNFFTNLLN----LVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGM 289
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
412-676 |
3.37e-30 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 126.08 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 412 LVLKGEVTIGELI----SFNAL---LAYFIQPIGRLINLQpqlqeAIVasDRLGEiLDLELEKSDDESIKPETL----AG 480
Cdd:COG4178 290 RYFAGEITLGGLMqaasAFGQVqgaLSWFVDNYQSLAEWR-----ATV--DRLAG-FEEALEAADALPEAASRIetseDG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 481 CISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiddiDKETLrskisY 560
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPA------GARVL-----F 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIKENLEF--VGDDVTYEKMVDACKKAHIHEYIESLplkyktplEEK---GSNLSGGQRQRLSIARALLK 635
Cdd:COG4178 431 LPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL--------DEEadwDQVLSLGEQQRLAFARLLLH 502
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHR 676
Cdd:COG4178 503 KPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
482-686 |
5.25e-30 |
|
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: 117.58 E-value: 5.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDiDKETLRSKISYI 561
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG-TIKENLEFV----GDDVTYEKMVDACKKAHIHEYiESLPLKYktpleekgsnLSGGQRQRLSIARALLKK 636
Cdd:COG4133 81 GHADGLKPElTVRENLRFWaalyGLRADREAIDEALEAVGLAGL-ADLPVRQ----------LSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKKCQKI 686
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
482-704 |
1.12e-29 |
|
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: 117.64 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYyidDIDKETL----RSK 557
Cdd:cd03218 1 LRAENLSKRYGKR-KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ---DITKLPMhkraRLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKEN----LEFVGDDvtyekmvdackKAHIHEYIESLplkyktpLEE---------KGSNLSGGQ 623
Cdd:cd03218 77 IGYLPQEASIFRKlTVEENilavLEIRGLS-----------KKEREEKLEEL-------LEEfhithlrksKASSLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLS-TIKKCQKIYVMDKGRIIEEGSHR 701
Cdd:cd03218 139 RRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPE 218
|
...
gi 336293682 702 ELL 704
Cdd:cd03218 219 EIA 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
482-706 |
1.30e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 120.59 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDK---EtlRSKI 558
Cdd:COG3842 6 LELENVSKRYGDV-TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVTGlppE--KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDsff-fsgTIKENLEFvGddVTYEKMVDACKKAHIHEYIESLPLkykTPLEEKG-SNLSGGQRQRLSIARALLKK 636
Cdd:COG3842 80 GMVFQDyalfphlTVAENVAF-G--LRMRGVPKAEIRARVAELLELVGL---EGLADRYpHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 637 PEILIMDEATSNLDS------ITE-RAIQRTLeecteNVTTIVIAH------RLSTikkcqKIYVMDKGRIIEEGSHREL 703
Cdd:COG3842 154 PRVLLLDEPLSALDAklreemREElRRLQREL-----GITFIYVTHdqeealALAD-----RIAVMNDGRIEQVGTPEEI 223
|
...
gi 336293682 704 LDK 706
Cdd:COG3842 224 YER 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
507-698 |
3.85e-29 |
|
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: 115.47 E-value: 3.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 507 NGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDD----IDKETLRSKISYISQD-SFFFSGTIKENLEFVgd 581
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQyALFPHLNVRENLAFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 582 dvtYEKMVDACKKAHIHEYIESL---PLKYKTPLEekgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQ 658
Cdd:cd03297 100 ---LKRKRNREDRISVDELLDLLgldHLLNRYPAQ-----LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 336293682 659 RTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03297 172 PELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
164-457 |
3.91e-29 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain] Cd Length: 294 Bit Score: 117.93 E-value: 3.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDD-ILPNNLKAsLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLL 242
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKgINNKDLNF-IYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 243 GYYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVF 322
Cdd:cd18571 80 DFLIKLMRLPISFFDTKMTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILWIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 323 GFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFG 402
Cdd:cd18571 160 LFLKKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 403 ICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18571 240 ILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDAKISLERL 294
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
298-729 |
4.37e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 124.70 E-value: 4.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 298 ILYLQNLKLFfTCFVPIVLYLILVFG--FKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTE---NK 372
Cdd:PLN03232 433 VLLYQQLGVA-SLFGSLILFLLIPLQtlIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQgirNE 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 373 FLkfmkSYFKHGYTYNVQGTLMDTiSGGFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIV 452
Cdd:PLN03232 512 EL----SWFRKAQLLSAFNSFILN-SIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANV 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 453 ASDRLGEILdLELEK--SDDESIKPETLAgcISLENVSFAYGMRDN--VLNDINISIHNGEKIALVGESGSGKTTIAKLL 528
Cdd:PLN03232 587 SLQRIEELL-LSEERilAQNPPLQPGAPA--ISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 529 MGFYKIDQGKIILnnyyiddidketLRSKISYISQDSFFFSGTIKENLEFvGDDVTYEKMVDACKKAHIHEYIESLPLKY 608
Cdd:PLN03232 664 LGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILF-GSDFESERYWRAIDVTALQHDLDLLPGRD 730
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 609 KTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS-ITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIY 687
Cdd:PLN03232 731 LTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 336293682 688 VMDKGRIIEEGSHRELLDKGGYYYRLWTEQTLDDEEQKIVSN 729
Cdd:PLN03232 811 LVSEGMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTN 852
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
482-694 |
6.68e-29 |
|
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: 114.66 E-value: 6.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKETLRSK---I 558
Cdd:cd03301 1 VELENVTKRFGNV-TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-----YIGGRDVTDLPPKdrdI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQD-SFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIAR 631
Cdd:cd03301 75 AMVFQNyALYPHMTVYDNIAFglklrkVPKDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 632 ALLKKPEILIMDEATSNLDS---ITERA----IQRTLEectenVTTIVIAH-RLSTIKKCQKIYVMDKGRI 694
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAklrVQMRAelkrLQQRLG-----TTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
497-703 |
8.62e-29 |
|
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: 116.49 E-value: 8.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddidKETLRskISYISQDSFFFSGTIKENL 576
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGR--ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 577 EF--VGDDVTYEKMVDACKkahIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITE 654
Cdd:cd03291 119 IFgvSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 655 RAIqrtLEECT----ENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:cd03291 196 KEI---FESCVcklmANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
482-698 |
1.43e-28 |
|
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: 113.83 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGeKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDID----KETLRSK 557
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTI-----RIDGQDvlkqPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKENLEFVGddvTYEKMVDACKKAHIHEYIESLPLKykTPLEEKGSNLSGGQRQRLSIARALLKK 636
Cdd:cd03264 74 IGYLPQEFGVYPNfTVREFLDYIA---WLKGIPSKEVKARVDEVLELVNLG--DRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 637 PEILIMDEATSNLDsITER-AIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03264 149 PSILIVDEPTAGLD-PEERiRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-703 |
3.71e-28 |
|
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: 121.94 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddidKETLRskISYISQDSFFFSGTIKENL 576
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGR--ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 577 EF--VGDDVTYEKMVDACKkahIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITE 654
Cdd:TIGR01271 508 IFglSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 336293682 655 RAI-QRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:TIGR01271 585 KEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
482-698 |
5.86e-28 |
|
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: 111.93 E-value: 5.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDiDKETLRSKISYI 561
Cdd:cd03268 1 LKTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSGTIKENLEfvgddvTYEKMVDAcKKAHIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSIARALLKKPEILI 641
Cdd:cd03268 79 EAPGFYPNLTARENLR------LLARLLGI-RKKRIDEVLDVVGLKDSA--KKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 642 MDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
170-456 |
6.17e-28 |
|
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: 114.42 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILVTILGIAGSFYYEFLIDDILPNNLK------ASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNI------D 237
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTvydlrkD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 238 VplllgyYNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVL 316
Cdd:cd18547 84 L------FEKLQRLPLSYFDTHSHGDIMSRVtNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 317 YLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGlvrlKTENKFLKFMKSYFKHGYTYNVQGTLMDT 396
Cdd:cd18547 158 SLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREE----EAIEEFDEINEELYKASFKAQFYSGLLMP 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 397 ISGGFG------ICLlwFGGSLVLKGEVTIGELISFnalLAY---FIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18547 234 IMNFINnlgyvlVAV--VGGLLVINGALTVGVIQAF---LQYsrqFSQPINQISQQINSLQSALAGAER 297
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
482-694 |
1.01e-27 |
|
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: 111.47 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKE--TLRSKIS 559
Cdd:cd03262 1 IEIKNLHKSFGDF-HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQdSF--FFSGTIKENLEFVgdDVTYEKMVDACKKAHIHEYIEslplkyKTPLEEKG----SNLSGGQRQRLSIARAL 633
Cdd:cd03262 80 MVFQ-QFnlFPHLTVLENITLA--PIKVKGMSKAEAEERALELLE------KVGLADKAdaypAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 634 LKKPEILIMDEATSNLDSITERAIQRTLEECT-ENVTTIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
482-705 |
1.37e-27 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 114.47 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDD--IDKETLRSKIS 559
Cdd:COG1118 3 IEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG---RDlfTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQD-SFFFSGTIKENLEFvGDDVtyEKMVDACKKAHIHEYIESLPLkykTPLEE-KGSNLSGGQRQRLSIARALLKKP 637
Cdd:COG1118 79 FVFQHyALFPHMTVAENIAF-GLRV--RPPSKAEIRARVEELLELVQL---EGLADrYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 638 EILIMDEATSNLDSIT----ERAIQRTLEEctENVTTIVIAH------RLstikkCQKIYVMDKGRIIEEGSHRELLD 705
Cdd:COG1118 153 EVLLLDEPFGALDAKVrkelRRWLRRLHDE--LGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
482-706 |
1.54e-27 |
|
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: 111.56 E-value: 1.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDkeTLRSKISYI 561
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP--PHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQD-SFFFSGTIKENLEFvgdDVTYEKMVDACKKAHIHEYIESLPLK---YKTPleekgSNLSGGQRQRLSIARALLKKP 637
Cdd:cd03300 78 FQNyALFPHLTVFENIAF---GLRLKKLPKAEIKERVAEALDLVQLEgyaNRKP-----SQLSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 638 EILIMDEATSNLDSITERAIQRTLEECTENV--TTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
482-704 |
1.64e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.77 E-value: 1.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDK-ETLRSKISY 560
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQ--DSFFFSGTIKENLEFVGDD-----VTYEKMVD-ACKKAHIHEYieslplKYKTPleekgSNLSGGQRQRLSIARA 632
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPENlclppIEIRKRVDrALAEIGLEKY------RHRSP-----KTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 633 LLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIV-IAHRLSTIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
482-674 |
2.15e-27 |
|
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: 110.58 E-value: 2.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET---LRSKI 558
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-TIKENLEFvGDDVTYEKMVDACKKahIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSIARALLKKP 637
Cdd:cd03292 81 GVVFQDFRLLPDrNVYENVAF-ALEVTGVPPREIRKR--VPAALELVGLSHKH--RALPAELSGGEQQRVAIARAIVNSP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 336293682 638 EILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA 674
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
498-703 |
2.73e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 113.29 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---RSKISYISQDSFffsG---- 570
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQDPY---Aslnp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 --TIKENLEFVgddVTYEKMVD-ACKKAHIHEYIESLPLK----YKTPLEekgsnLSGGQRQRLSIARALLKKPEILIMD 643
Cdd:COG4608 111 rmTVGDIIAEP---LRIHGLASkAERRERVAELLELVGLRpehaDRYPHE-----FSGGQRQRIGIARALALNPKLIVCD 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 644 EATSNLD-SIteRA--------IQRTLeecteNVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:COG4608 183 EPVSALDvSI--QAqvlnlledLQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
482-703 |
3.64e-27 |
|
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: 110.15 E-value: 3.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDNV-LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYyidDIDKET--LRSKI 558
Cdd:cd03265 1 IEVENLVKKYG--DFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH---DVVREPreVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-TIKENLEFVGDDVTYekmvdacKKAHIHEYIESLpLKYKTPLEEKG---SNLSGGQRQRLSIARALL 634
Cdd:cd03265 76 GIVFQDLSVDDElTGWENLYIHARLYGV-------PGAERRERIDEL-LDFVGLLEAADrlvKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 635 KKPEILIMDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
498-705 |
5.38e-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: 5.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFykID-QGKIILNNYYIDDIDKE---TLRSKISYISQDSFffsG--- 570
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL--IPsEGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDPF---Gsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 -------TIKENLEFVGDDVTY----EKMVDACKK-----AHIHEYieslplkyktPLEekgsnLSGGQRQRLSIARALL 634
Cdd:COG4172 377 prmtvgqIIAEGLRVHGPGLSAaerrARVAEALEEvgldpAARHRY----------PHE-----FSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 635 KKPEILIMDEATSNLDsiteRAIQ-------RTLEEcTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLD 705
Cdd:COG4172 442 LEPKLLVLDEPTSALD----VSVQaqildllRDLQR-EHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
482-706 |
1.21e-26 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 108.97 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDKETLRSK-ISY 560
Cdd:cd03296 3 IEVRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQERnVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQD-SFFFSGTIKENLEFvGDDV--TYEKMVDACKKAHIHEYIESLPLKYktpLEEK-GSNLSGGQRQRLSIARALLKK 636
Cdd:cd03296 79 VFQHyALFRHMTVFDNVAF-GLRVkpRSERPPEAEIRAKVHELLKLVQLDW---LADRyPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
482-705 |
1.34e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDD--IDKETLRSKIS 559
Cdd:PRK09493 2 IEFKNVSKHFGPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFFFSG-TIKENLEFVGDDVTYEKMVDACKKAHiheyieslPLKYKTPLEEKG----SNLSGGQRQRLSIARALL 634
Cdd:PRK09493 81 MVFQQFYLFPHlTALENVMFGPLRVRGASKEEAEKQAR--------ELLAKVGLAERAhhypSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 635 KKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTIKKC-QKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
483-703 |
1.53e-26 |
|
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: 108.38 E-value: 1.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDK----ETLRSKI 558
Cdd:TIGR03410 2 EVSNLNVYYG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDG---EDITKlpphERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-TIKENLEfVGDDVTyekmvdACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKP 637
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLL-TGLAAL------PRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 638 EILIMDEATSNLD-SIT---ERAIQRTLEEctENVTTIVIAHRLSTIKKC-QKIYVMDKGRIIEEGSHREL 703
Cdd:TIGR03410 151 KLLLLDEPTEGIQpSIIkdiGRVIRRLRAE--GGMAILLVEQYLDFARELaDRYYVMERGRVVASGAGDEL 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
483-705 |
1.56e-26 |
|
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: 108.53 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDK----ETLRSKI 558
Cdd:COG0410 5 EVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG---EDITGlpphRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-TIKENLE---FVGDDVTYEKMVdackKAHIHEYiesLPLkyktpLEE----KGSNLSGGQRQRLSIA 630
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLLlgaYARRDRAEVRAD----LERVYEL---FPR-----LKErrrqRAGTLSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 631 RALLKKPEILIMDEATSNLD-SITERaIQRTLEECTENVTTIV-----------IAHRlstikkcqkIYVMDKGRIIEEG 698
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLApLIVEE-IFEIIRRLNREGVTILlveqnarfaleIADR---------AYVLERGRIVLEG 218
|
....*..
gi 336293682 699 SHRELLD 705
Cdd:COG0410 219 TAAELLA 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
480-706 |
2.32e-26 |
|
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: 109.17 E-value: 2.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 480 GCISLENVSFAYGMRDN-VLNDINISIHNGEKIALVGESGSGKTTiakLLMGFYKI--DQGKIILNNYYIDDIDKETLRS 556
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNaVLENISFSISPGQRVGLLGRTGSGKST---LLSAFLRLlnTEGDIQIDGVSWNSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 557 KISYISQDSFFFSGTIKENLEFVGDdVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKK 636
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDPYGK-WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
441-728 |
3.63e-26 |
|
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: 115.43 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 441 INLQPQLQEAIV-ASDRLGEI-LDLELEKSDDESIKPETL----AGCISLENVSFAYGMRDN-VLNDINISIHNGEKIAL 513
Cdd:TIGR00957 590 LNILPMVISSIVqASVSLKRLrIFLSHEELEPDSIERRTIkpgeGNSITVHNATFTWARDLPpTLNGITFSIPEGALVAV 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 514 VGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddidkeTLRSKISYISQDSFFFSGTIKENLEF--VGDDVTYEKMVDA 591
Cdd:TIGR00957 670 VGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFgkALNEKYYQQVLEA 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 592 CKkahIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTL---EECTENV 668
Cdd:TIGR00957 737 CA---LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNK 813
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 669 TTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRLW-----TEQTLDDEEQKIVS 728
Cdd:TIGR00957 814 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLrtyapDEQQGHLEDSWTAL 878
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
498-704 |
4.09e-26 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 108.50 E-value: 4.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRS----KISYISQdSF--FFSGT 571
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQ-SFalLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 572 IKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARALLKKPEILIMDEA 645
Cdd:cd03294 119 VLENVAFglevqgVPRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 646 TSNLDSITERAIQRTLEECTENV--TTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELqkTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
482-697 |
4.69e-26 |
|
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: 107.13 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRD---NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKE---TLR 555
Cdd:COG4181 9 IELRGLTKTVGTGAgelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDaraRLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 S-KISYISQdSFFF--SGTIKEN----LEFVGDDvtyekmvDACKKAhiheyieslplkyKTPLEEKG---------SNL 619
Cdd:COG4181 89 ArHVGFVFQ-SFQLlpTLTALENvmlpLELAGRR-------DARARA-------------RALLERVGlghrldhypAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 620 SGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECT-ENVTTIVIA-HRLSTIKKCQKIYVMDKGRIIEE 697
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVtHDPALAARCDRVLRLRAGRLVED 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
482-702 |
4.98e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtlRSKISYI 561
Cdd:PRK09452 15 VELRGISKSFDGKE-VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQD-SFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARALL 634
Cdd:PRK09452 92 FQSyALFPHMTVFENVAFglrmqkTPAAEITPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 635 KKPEILIMDEATSNLD-------SITERAIQRTLeecteNVTTIVIAH-RLSTIKKCQKIYVMDKGRIIEEGSHRE 702
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrkqmQNELKALQRKL-----GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
482-695 |
6.79e-26 |
|
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: 104.43 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNN--YYIDDIdKETLRSKIS 559
Cdd:cd03216 1 LELRGITKRFGGV-KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASP-RDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQdsfffsgtikenlefvgddvtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEI 639
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 640 LIMDEATSNLdsiTERAIQRTLEE----CTENVTTIVIAHRLSTIKK-CQKIYVMDKGRII 695
Cdd:cd03216 104 LILDEPTAAL---TPAEVERLFKVirrlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
167-457 |
6.95e-26 |
|
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: 108.75 E-value: 6.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 167 LLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHS---------------ISIAMLILLLFKIVTEFFRKTLLLY 231
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLGlapllgpdplallllAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 232 MAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVL-MAVVGGAILYLqNLKLFFT 309
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLtGDVGAIQDLLVSGVLPLLTNLLtLVGMLGVMFWL-DWQLALI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 310 CFVPIVLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLV--RLKTENKflKFMKSYFKhgyTY 387
Cdd:cd18564 160 ALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEerRFARENR--KSLRAGLR---AA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 388 NVQGTLMDTIS--GGFGICL-LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18564 235 RLQALLSPVVDvlVAVGTALvLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
482-703 |
8.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 8.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY-----GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKE---- 552
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-----YVDGLDTSdeen 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 553 --TLRSKISYISQ--DSFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGG 622
Cdd:PRK13633 80 lwDIRNKAGMVFQnpDNQIVATIVEEDVAFgpenlgIPPEEIRERVDESLKKVGMYEYRRHAP-----------HLLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 623 QRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTEN--VTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSH 700
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228
|
...
gi 336293682 701 REL 703
Cdd:PRK13633 229 KEI 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
482-708 |
1.12e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.51 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN--VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKIS 559
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQ--DSFFFSGTIKENLEFVGDD--VTYEKMVDACKKAHihEYIESLPLKYKTPleekgSNLSGGQRQRLSIARALLK 635
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENkgIPHEEMKERVNEAL--ELVGMQDFKEREP-----ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGG 708
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
190-457 |
1.27e-25 |
|
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: 107.89 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 190 FLIDDILPNN---LKASLHSISIAMLI-LLLFKIV---TEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVG 262
Cdd:cd18554 24 YIVDDVIQGSsltLDEKVYKLFTIIGImFFIFLILrppVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 263 EIISR-FNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVMEDNAS 341
Cdd:cd18554 104 EIISRvINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 342 LTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKH----GYTYNVQGTLMDtisggFG-ICLLWFGGSLVLKG 416
Cdd:cd18554 184 VQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHtrwnAKTFSAVNTITD-----LApLLVIGFAAYLVIEG 258
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 336293682 417 EVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18554 259 NLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
482-704 |
1.28e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 107.10 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNV--LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKIS 559
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQ--DSFFFSGTIKENLEFVGDD--VTYEKMVDACKKAHIHeyIESLPLKYKTPleekgSNLSGGQRQRLSIARALLK 635
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLA--VNMLDFKTREP-----ARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
482-699 |
1.36e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.73 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVS--FAYGMRD-NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRS-- 556
Cdd:PRK11153 2 IELKNISkvFPQGGRTiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 557 -KISYISQDsffF----SGTIKEN----LEFVGDDvtyekmvdackKAHIHEYI-ESLPLkykTPLEEKG----SNLSGG 622
Cdd:PRK11153 82 rQIGMIFQH---FnllsSRTVFDNvalpLELAGTP-----------KAEIKARVtELLEL---VGLSDKAdrypAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 623 QRQRLSIARALLKKPEILIMDEATSNLDSITERAI-------QRTLeecteNVTTIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSIlellkdiNREL-----GLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
....*
gi 336293682 695 IEEGS 699
Cdd:PRK11153 220 VEQGT 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
482-702 |
1.55e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 1.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY--GM--RDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDD--IDKETLR 555
Cdd:PRK13637 3 IKIENLTHIYmeGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQ--DSFFFSGTIKENLEF------VGDDVTYEKMVDAckkahiheyIESLPLKYKTPLEEKGSNLSGGQRQRL 627
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFgpinlgLSEEEIENRVKRA---------MNIVGLDYEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRE 702
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
484-650 |
2.20e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.92 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 484 LENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYiddidketlrsKISYISQ 563
Cdd:COG0488 1 LENLSKSFGGRP-LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL-----------RIGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 564 DSFFFSG-TIkenLEFVGDDVT------------YEKMVDACKK----AHIHEYIE-----SLPLKYKT----------P 611
Cdd:COG0488 69 EPPLDDDlTV---LDTVLDGDAelraleaeleelEAKLAEPDEDlerlAELQEEFEalggwEAEARAEEilsglgfpeeD 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 336293682 612 LEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:COG0488 146 LDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
170-457 |
2.89e-25 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 106.37 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILVTILGIAGSFY----YefliDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYY 245
Cdd:cd18587 7 VLLAALLINLFALASPLFvmnvY----DRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSRLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 246 NHVVKLPMNFFgTRKVGEIISRFNDGDKIRNAISSVTLTLMID--------VLMAVVGGAILylqnlklfftcFVPIV-L 316
Cdd:cd18587 83 ERVLGLRLEAR-PASVGSFANNLREFESVRDFFTSATLTALIDlpfvllflAVIALIGGPLA-----------LVPLVaI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 317 YLILVFGF--KNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENkflkfmksYFKHGYTYNVQGTLM 394
Cdd:cd18587 151 PLVLLYGLllQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEE--------AVAALARSSLKSRLL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 395 DTISGGF--------GICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18587 223 SSSATNFaqfvqqlvTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
482-706 |
4.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.04 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY-GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFY--------KIDQGKIILNNYYIDDIdke 552
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnpnsKITVDGITLTAKTVWDI--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 553 tlRSKISYISQ--DSFFFSGTikenlefVGDDVTY---------EKMV----DACKKAHIHEYIESLPlkyktpleekgS 617
Cdd:PRK13640 83 --REKVGIVFQnpDNQFVGAT-------VGDDVAFglenravprPEMIkivrDVLADVGMLDYIDSEP-----------A 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 618 NLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKKCQKIYVMDKGRII 695
Cdd:PRK13640 143 NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
250
....*....|.
gi 336293682 696 EEGSHRELLDK 706
Cdd:PRK13640 223 AQGSPVEIFSK 233
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
482-705 |
2.06e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.41 E-value: 2.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDKETL--RSK-- 557
Cdd:COG1137 4 LEAENLVKSYGKR-TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG---EDITHLPMhkRARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKEN----LEFVGDDvtyekmvdackKAHIHEYIESLplkyktpLEE---------KGSNLSGGQ 623
Cdd:COG1137 80 IGYLPQEASIFRKlTVEDNilavLELRKLS-----------KKEREERLEEL-------LEEfgithlrksKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-H--RlSTIKKCQKIYVMDKGRIIEEGSH 700
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHnvR-ETLGICDRAYIISEGKVLAEGTP 220
|
....*
gi 336293682 701 RELLD 705
Cdd:COG1137 221 EEILN 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
403-713 |
2.21e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.83 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 403 ICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRLGEILDLElEK--SDDESIKPETLAg 480
Cdd:PLN03130 537 VTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAE-ERvlLPNPPLEPGLPA- 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 481 cISLENVSFAYGMRDN--VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIIlnnyyiddidkeTLRSKI 558
Cdd:PLN03130 615 -ISIKNGYFSWDSKAErpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV------------VIRGTV 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSGTIKENLEFVG--DDVTYEKMVDAckkAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKK 636
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSpfDPERYERAIDV---TALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 637 PEILIMDEATSNLDSITERAI-QRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHRELLDKGGYYYRL 713
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
482-692 |
2.24e-24 |
|
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: 102.02 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSK---- 557
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrys 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSGTIKENLEFVG--DDVTYEKMVDACKkahIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLK 635
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSpfNKQRYKAVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 636 KPEILIMDEATSNL-----DSITERAIQRTLEEctENVTTIVIAHRLSTIKKCQKIYVMDKG 692
Cdd:cd03290 158 NTNIVFLDDPFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
482-698 |
2.62e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 101.59 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDketlRSKISYI 561
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQD-SFFFSGTIKENLEFVGDDVTYEKMvDAckKAHIHEYIESLPL--KYKTPLEEkgsnLSGGQRQRLSIARALLKKPE 638
Cdd:cd03269 76 PEErGLYPKMKVIDQLVYLAQLKGLKKE-EA--RRRIDEWLERLELseYANKRVEE----LSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 639 ILIMDEATSNLDSITERAIQRTLEECTENVTTIVI-AHRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
168-457 |
3.04e-24 |
|
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: 103.72 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 168 LNIFIASILVT-ILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYN 246
Cdd:cd18550 1 LALVLLLILLSaLLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 247 HVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQN--LKLFFTCFVPIVLYLILVFG 323
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLnNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDwrLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 fkNKLKKVNRRVMEDNASLTSYLVESLE--GIETVKAFNGEG--LVRLKTENKflKFMKSYFKHGYTYNVQGTLMDTISG 399
Cdd:cd18550 161 --RRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDdeAARFARRSR--ELRDLGVRQALAGRWFFAALGLFTA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 400 GFGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18550 237 IGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
291-644 |
3.17e-24 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 107.58 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 291 MAVVGGAILYLQ--NLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVK-------AFNG 361
Cdd:COG4615 132 VALVLGCLAYLAwlSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnrrrrrAFFD 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 362 EGLVRLKTEnkflkfMKSYFKHGYTYNVqgtlmdtISGGFGIcLLWFG--GSLV----LKGEVTIGELISFNALLAYFIQ 435
Cdd:COG4615 212 EDLQPTAER------YRDLRIRADTIFA-------LANNWGN-LLFFAliGLILfllpALGWADPAVLSGFVLVLLFLRG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 436 PIGRLINLQPQLQEAIVASDRLGEiLDLELEKSDDESIKPETLA-----GCISLENVSFAYGMRDN----VLNDINISIH 506
Cdd:COG4615 278 PLSQLVGALPTLSRANVALRKIEE-LELALAAAEPAAADAAAPPapadfQTLELRGVTYRYPGEDGdegfTLGPIDLTIR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 507 NGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSgtikenlEFVGDDvtye 586
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD-------RLLGLD---- 425
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 587 KMVDAckkAHIHEYIESLPLKYKTPLEEKGS---NLSGGQRQRLSIARALLKKPEILIMDE 644
Cdd:COG4615 426 GEADP---ARARELLERLELDHKVSVEDGRFsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
482-696 |
3.77e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddidkETLrsKISYI 561
Cdd:COG0488 316 LELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG---------ETV--KIGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG--TIKENLEFVGDDVTyekmvdackKAHIHEYIESLPLKYKTpLEEKGSNLSGGQRQRLSIARALLKKPEI 639
Cdd:COG0488 384 DQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFLFSGDD-AFKPVGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 640 LIMDEATSNLDSITERAIQRTLEECTENVttIVIAH-R--LSTIkkCQKIYVMDKGRIIE 696
Cdd:COG0488 454 LLLDEPTNHLDIETLEALEEALDDFPGTV--LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
482-698 |
4.56e-24 |
|
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: 100.91 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG---MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIIlnnyyIDDIDkeTLRSKI 558
Cdd:cd03266 2 ITADALTKRFRdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT-----VDGFD--VVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-------TIKENLEFVGDdvtyekmVDACKKAHIHEYIESLP--LKYKTPLEEKGSNLSGGQRQRLSI 629
Cdd:cd03266 75 EARRRLGFVSDStglydrlTARENLEYFAG-------LYGLKGDELTARLEELAdrLGMEELLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
497-703 |
5.06e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNN--YYIDDIdKETLRSKISYISQD-SFFFSGTIK 573
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAGIAIIHQElNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 574 ENLeFVGDDVTYEKMVDacKKAHIHEYIESL-PLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSnldSI 652
Cdd:COG1129 98 ENI-FLGREPRRGGLID--WRAMRRRARELLaRLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTA---SL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 653 TERAIQ------RTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:COG1129 172 TEREVErlfriiRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
482-705 |
6.00e-24 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 100.98 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG---MRdnvlndINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtlRSKI 558
Cdd:COG3840 2 LRLDDLTYRYGdfpLR------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-TIKENlefVG---------DDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLS 628
Cdd:COG3840 74 SMLFQENNLFPHlTVAQN---IGlglrpglklTAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 629 IARALLKKPEILIMDEATSNLDsITERAIQRTL--EECTE-NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALD-PALRQEMLDLvdELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
.
gi 336293682 705 D 705
Cdd:COG3840 219 D 219
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
482-706 |
8.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 8.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKE--TLRSKIS 559
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQ--DSFFFSGTIKEnlefvgdDVTYEKMVDACKKAHIHEYIESLPLKYK-TPLEEKGSN-LSGGQRQRLSIARALLK 635
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQ-------DVSFGAVNLKLPEDEVRKRVDNALKRTGiEHLKDKPTHcLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTLEECTENV-TTIVIA-HRLSTIK-KCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
167-457 |
1.33e-23 |
|
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: 101.41 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 167 LLNIFIASILVTILGIAGSFyyefLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYN 246
Cdd:cd18575 2 LIALLIAAAATLALGQGLRL----LIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 247 HVVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKL--FFTCFVPIVLYLILVFG 323
Cdd:cd18575 78 HLLRLSPSFFETTRTGEVLSRLTtDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLtlLVLLVIPLVVLPIILFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 324 FKnkLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRlkteNKFLKFMKSYFKHGYTYNVQGTLMDT--ISGGF 401
Cdd:cd18575 158 RR--VRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAER----QRFATAVEAAFAAALRRIRARALLTAlvIFLVF 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 402 G--ICLLWFGGSLVLKGEVTIGELISFnALLAYFI-QPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18575 232 GaiVFVLWLGAHDVLAGRMSAGELSQF-VFYAVLAaGSVGALSEVWGDLQRAAGAAERL 289
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
482-706 |
2.37e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.83 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDiDKETLRSKISYI 561
Cdd:PRK13536 42 IDLAGVSKSYGDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQ-DSFFFSGTIKENLEFVGddvTYEKMvdacKKAHIHEYIESLpLKYKTpLEEKG----SNLSGGQRQRLSIARALLKK 636
Cdd:PRK13536 120 PQfDNLDLEFTVRENLLVFG---RYFGM----STREIEAVIPSL-LEFAR-LESKAdarvSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTENVTTIVI-------AHRLstikkCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
497-699 |
2.55e-23 |
|
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: 99.43 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDID--KETLRSK--ISYisqdSF-----F 567
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG---EDITglPPHEIARlgIGR----TFqiprlF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGTIKENL---------EFVGDDVTYEKMVDACKKAHihEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLKKPE 638
Cdd:cd03219 88 PELTVLENVmvaaqartgSGLLLARARREEREARERAE--ELLERVGLADL--ADRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 639 ILIMDEATSNL-DSITERAIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:cd03219 164 LLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
482-695 |
2.77e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVS--FAYGMRDN--VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDKETLRSK 557
Cdd:COG1101 2 LELKNLSktFNPGTVNEkrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---KDVTKLPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYIS---QDSF---FFSGTIKENL---EFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLS 628
Cdd:COG1101 79 AKYIGrvfQDPMmgtAPSMTIEENLalaYRRGKRRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 629 IARALLKKPEILIMDEATSNLD--------SITERAIQRtleectENVTTIVIAHRLS--------TIkkcqkiyVMDKG 692
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDpktaalvlELTEKIVEE------NNLTTLMVTHNMEqaldygnrLI-------MMHEG 225
|
...
gi 336293682 693 RII 695
Cdd:COG1101 226 RII 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
482-700 |
4.28e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMrDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKI-ILNNYY-----IDDIDKETLR 555
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLnIAGNHFdfsktPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQDSFFFSG-TIKENL-------EFVGDDVTYEKMVDACKKAHIHEYIESLPLkyktpleekgsNLSGGQRQRL 627
Cdd:PRK11124 82 RNVGMVFQQYNLWPHlTVQQNLieapcrvLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 628 SIARALLKKPEILIMDEATSNLD-SITERAIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSH 700
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpEITAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
164-457 |
4.54e-23 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 99.99 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLG 243
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 YYNHVVKLPMNffgTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQN--LKLFFTCFVPIVLYLILV 321
Cdd:cd18586 81 VFRAVLELPLE---SRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHppLGWVALVGAPVLVGLAWL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 322 FGFKnkLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGytyNVQGTLMdTISGGF 401
Cdd:cd18586 158 NHRA--TRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRAS---DLAGAIS-AIGKTL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 402 GICL----LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18586 232 RMALqsliLGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
500-704 |
4.63e-23 |
|
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: 101.34 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 500 DINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDD----IDKETLRSKISYISQDSFFFSG-TIKE 574
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 575 NLEFvgddvTYEKMVDACKKAHIHEYIESLPLKyktPLEEKGSN-LSGGQRQRLSIARALLKKPEILIMDEATSNLDSIT 653
Cdd:TIGR02142 95 NLRY-----GMKRARPSERRISFERVIELLGIG---HLLGRLPGrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 654 ERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:TIGR02142 167 KYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
482-703 |
8.02e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.00 E-value: 8.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDdIDKETL---RSKI 558
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQ--DSFFFSGTIKE-------NLEFVGDDVTyEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSI 629
Cdd:PRK13639 81 GIVFQnpDDQLFAPTVEEdvafgplNLGLSKEEVE-KRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
434-706 |
8.24e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 103.13 E-value: 8.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 434 IQPIGRLinlqPQLQEAIVASDRLGeilDLELEKSDDESIKPETLAGC--ISLENVSFAYGMRDNVLNDINISIHNGEKI 511
Cdd:PRK10522 280 LSAVGAL----PTLLSAQVAFNKLN---KLALAPYKAEFPRPQAFPDWqtLELRNVTFAYQDNGFSVGPINLTIKRGELL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 512 ALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSFFFSGTIKENlefvGDDVtyekmvda 591
Cdd:PRK10522 353 FLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE----GKPA-------- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 592 cKKAHIHEYIESLPLKYKTPLEE-KGSN--LSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAI-QRTLEECTEN 667
Cdd:PRK10522 421 -NPALVEKWLERLKMAHKLELEDgRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEM 499
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 336293682 668 VTTIV-IAHRLSTIKKCQKIYVMDKGRIIE-EGSHRELLDK 706
Cdd:PRK10522 500 GKTIFaISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
482-676 |
8.80e-23 |
|
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: 95.68 E-value: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILnnyyiddidkeTLRSKISYI 561
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSGTIKENLEFVGDDVtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEILI 641
Cdd:cd03223 70 PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 336293682 642 MDEATSNLDSITERAIQRTLEEctENVTTIVIAHR 676
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
513-703 |
1.20e-22 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 99.49 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 513 LVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtLRSkISYISQD-SFFFSGTIKENLEF------VGDDVTY 585
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-LRH-INMVFQSyALFPHMTVEENVAFglkmrkVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 586 EKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECT 665
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 336293682 666 EN--VTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:TIGR01187 148 EQlgITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
482-693 |
1.57e-22 |
|
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: 94.05 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiddidketlRSKISYI 561
Cdd:cd03221 1 IELENLSKTYGGKL-LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQdsfffsgtikenlefvgddvtyekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEILI 641
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 642 MDEATSNLDSITERAIQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGR 693
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE--YPGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
497-698 |
1.70e-22 |
|
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: 96.57 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGfyKIDQGKIILNNYYID--DIDKETLRSKISYISQDSFFFSG-TIK 573
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG--RVEGGGTTSGQILFNgqPRKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 574 ENLEFVGDDVTYEKMVDACKKAHihEYIESLPLKYKTPL-EEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSI 652
Cdd:cd03234 100 ETLTYTAILRLPRKSSDAIRKKR--VEDVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 336293682 653 TERAIQRTLEE-CTENVTTIVIAH--RLSTIKKCQKIYVMDKGRIIEEG 698
Cdd:cd03234 178 TALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
485-677 |
2.39e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 485 ENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAK-------LLMGFYKidQGKIIL--NNYYIDDIDKETLR 555
Cdd:PRK14243 14 ENLNVYYG-SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFhgKNLYAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQDSFFFSGTIKENLEF----VGDDVTYEKMVD-ACKKAHIHEYIeslplkyKTPLEEKGSNLSGGQRQRLSIA 630
Cdd:PRK14243 91 RRIGMVFQKPNPFPKSIYDNIAYgariNGYKGDMDELVErSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRL 677
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
482-705 |
2.58e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.83 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQG-------KIILNNYYIDDIDKETL 554
Cdd:PRK14267 5 IETVNLRVYYG-SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEarvegevRLFGRNIYSPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 RSKISYISQ-DSFFFSGTIKENlefVGDDVTYEKMVDAckKAHIHEYIE------SLPLKYKTPLEEKGSNLSGGQRQRL 627
Cdd:PRK14267 84 RREVGMVFQyPNPFPHLTIYDN---VAIGVKLNGLVKS--KKELDERVEwalkkaALWDEVKDRLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQK----IYVmdkGRIIEEGSHREL 703
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDyvafLYL---GKLIEVGPTRKV 235
|
..
gi 336293682 704 LD 705
Cdd:PRK14267 236 FE 237
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
484-703 |
3.32e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.64 E-value: 3.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 484 LENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYID--DIDKETLRSK-ISY 560
Cdd:PRK11432 9 LKNITKRFG-SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-----FIDgeDVTHRSIQQRdICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSGTIkenlefVGDDVTYEKMVDACKKAHIHEYI-ESLPLKYKTPLEEKG-SNLSGGQRQRLSIARALLKKPE 638
Cdd:PRK11432 83 VFQSYALFPHMS------LGENVGYGLKMLGVPKEERKQRVkEALELVDLAGFEDRYvDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 639 ILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
485-704 |
5.76e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.73 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 485 ENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDID----KETLRSKISY 560
Cdd:PRK10895 7 KNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD---EDISllplHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQD-SFFFSGTIKENLEFV---GDDVTYEKMVDACKKAHIHEYIESLPlkyktplEEKGSNLSGGQRQRLSIARALLKK 636
Cdd:PRK10895 83 LPQEaSIFRRLSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLR-------DSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRL-STIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
497-698 |
6.24e-22 |
|
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: 94.91 E-value: 6.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddidkeTLRSKISYISQDSFFFSG--TIKE 574
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-------------TVRGRVSSLLGLGGGFNPelTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 575 NLEFVGddvTYEKMVDACKKAHIHEYIE--------SLPLKyktpleekgsNLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:cd03220 104 NIYLNG---RLLGLSRKEIDEKIDEIIEfselgdfiDLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 647 SNLD-SITERAIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03220 171 AVGDaAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
482-705 |
7.11e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.80 E-value: 7.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETlRSKISYI 561
Cdd:PRK13537 8 IDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQ-DSFFFSGTIKENLEFVGddvTYEKMVDACKKAHIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:PRK13537 86 PQfDNLDPDFTVRENLLVFG---RYFGLSAAAARALVPPLLEFAKLENKA--DAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 641 IMDEATSNLDSITERAIQRTLEECTENVTTIVI-------AHRLstikkCQKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
482-700 |
8.64e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 8.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYID---DIDKET---LR 555
Cdd:COG4161 3 IQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAirlLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQDSFFFSG-TIKENLefVGDDVTYEKMV--DACKKA-------HIHEYIESLPLkyktpleekgsNLSGGQRQ 625
Cdd:COG4161 82 QKVGMVFQQYNLWPHlTVMENL--IEAPCKVLGLSkeQAREKAmkllarlRLTDKADRFPL-----------HLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLD-SITERAIQRTLEECTENVTTIVIAHRLSTIKK--CQKIYvMDKGRIIEEGSH 700
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDpEITAQVVEIIRELSQTGITQVIVTHEVEFARKvaSQVVY-MEKGRIIEQGDA 225
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
16-136 |
1.10e-21 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239105 [Multi-domain] Cd Length: 126 Bit Score: 91.17 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 16 QDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEeIFNNLPTPLIAHViiDDVl 95
Cdd:cd02425 10 TECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISFKK-NLYPLKLPVIIFW--NNN- 85
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 336293682 96 lHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIF 136
Cdd:cd02425 86 -HFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILT 125
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
499-703 |
1.12e-21 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 96.72 E-value: 1.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 499 NDINISIHNGEKIALVGESGSGKTTIAKLLMGFY----KID-----QGKIILNnyyIDDIDKETLRS-KISYISQD---S 565
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLaangRIGgsatfNGREILN---LPEKELNKLRAeQISMIFQDpmtS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 566 FFFSGTIKENLEFV-------GDDVTYE---KMVDACKKAHIHEYIESLPLKYktpleekgsnlSGGQRQRLSIARALLK 635
Cdd:PRK09473 110 LNPYMRVGEQLMEVlmlhkgmSKAEAFEesvRMLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMALLC 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
482-702 |
2.05e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.18 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrdNV--LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddiDKET------ 553
Cdd:COG3845 6 LELRGITKRFG---GVvaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID-------GKPVrirspr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 554 --LRSKISYISQ-----DSFffsgTIKENLeFVGDDVTYEKMVDAcKKAH--IHEYIESLPLKykTPLEEKGSNLSGGQR 624
Cdd:COG3845 76 daIALGIGMVHQhfmlvPNL----TVAENI-VLGLEPTKGGRLDR-KAARarIRELSERYGLD--VDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 625 QRLSIARALLKKPEILIMDEATSNLdsiTERAIQ---RTLEECTENVTTIV-IAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVL---TPQEADelfEILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVVGTVD 224
|
...
gi 336293682 700 HRE 702
Cdd:COG3845 225 TAE 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
482-704 |
2.88e-21 |
|
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: 93.61 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGF-YKIDQGKIIL--NNYYIDDIDKetLRSKI 558
Cdd:COG1119 4 LELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLfgERRGGEDVWE--LRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQD----------------SFFFsGTIkenleFVGDDVTYEKmvdackKAHIHEYIESLPLKYK--TPLEEkgsnLS 620
Cdd:COG1119 81 GLVSPAlqlrfprdetvldvvlSGFF-DSI-----GLYREPTDEQ------RERARELLELLGLAHLadRPFGT----LS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 621 GGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIV-IAHRLSTIKKC-QKIYVMDKGRIIEE 697
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAA 224
|
....*..
gi 336293682 698 GSHRELL 704
Cdd:COG1119 225 GPKEEVL 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
482-722 |
2.99e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 98.24 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY---GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGF-------YKidQGKIILNNYYIDDIDK 551
Cdd:PRK15134 6 LAIENLSVAFrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvYP--SGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 552 ETLR----SKISYISQD---SFFFSGTIKENLEFV-------GDDVTYEKMVDACKKAHIHEYieslplkyKTPLEEKGS 617
Cdd:PRK15134 84 QTLRgvrgNKIAMIFQEpmvSLNPLHTLEKQLYEVlslhrgmRREAARGEILNCLDRVGIRQA--------AKRLTDYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 618 NLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRC 235
|
250 260
....*....|....*....|....*...
gi 336293682 695 IEEGSHRELLDKGGYYYrlwTEQTLDDE 722
Cdd:PRK15134 236 VEQNRAATLFSAPTHPY---TQKLLNSE 260
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
482-705 |
3.63e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.11 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG---MRdnvlndINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyIDDIDKETLRSKI 558
Cdd:PRK10771 2 LKLTDITWLYHhlpMR------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG--QDHTTTPPSRRPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDSFFFSG-TIKENLEfVG-------DDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIA 630
Cdd:PRK10771 74 SMLFQENNLFSHlTVAQNIG-LGlnpglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTE-NVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK10771 142 RCLVREQPILLLDEPFSALDPALRQEMLTLVSQvCQErQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
497-699 |
4.75e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 97.47 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKiDQGKIILNNYYIDDIDKETL---RSKISYISQD-------SF 566
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnsslnpRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 567 FFSGTIKENLEfvgddVTYEKMVDACKKAHIHEYIESLPL----KYKTPLEekgsnLSGGQRQRLSIARALLKKPEILIM 642
Cdd:PRK15134 380 NVLQIIEEGLR-----VHQPTLSAAQREQQVIAVMEEVGLdpetRHRYPAE-----FSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 643 DEATSNLDSITERAI---QRTLEEcTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:PRK15134 450 DEPTSSLDKTVQAQIlalLKSLQQ-KHQLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGD 509
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
482-707 |
1.45e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRD----NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYI----DDIDKET 553
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 554 LRSKISYISQ--DSFFFSGTIKENLEF------VGDDvtyekmvDACKKAHIHEYIESLPLKY--KTPLEekgsnLSGGQ 623
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFgpmnfgVSEE-------DAKQKAREMIELVGLPEELlaRSPFE-----LSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSH 700
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
....*..
gi 336293682 701 RELLDKG 707
Cdd:PRK13634 231 REIFADP 237
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
171-457 |
3.68e-20 |
|
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: 91.39 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVK 250
Cdd:cd18543 5 LLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 251 LPMNFFGTRKVGEIISRFN-DGDKIRNAISSVtLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLK 329
Cdd:cd18543 85 LDGAFHDRWQSGQLLSRATsDLSLVQRFLAFG-PFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 330 KVNRRVMEDNASLTSYLVESLEGIETVKAFNGEG--LVRLKTENKFLK-------FMKSYFkhgytynvqGTLMDTISG- 399
Cdd:cd18543 164 PASRRAQDQAGDLATVVEESVTGIRVVKAFGRERreLDRFEAAARRLRatrlraaRLRARF---------WPLLEALPEl 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 400 GFGIClLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18543 235 GLAAV-LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
482-699 |
3.84e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.14 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---------------------VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKII 540
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 541 LNnyyiddidketlrSKISyisqdSFF---------FSGtiKENLEFVG-------DDVtyEKMVDACKK-AHIHEYIEs 603
Cdd:COG1134 85 VN-------------GRVS-----ALLelgagfhpeLTG--RENIYLNGrllglsrKEI--DEKFDEIVEfAELGDFID- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 604 LPLKyktpleekgsNLSGGQRQRLSIARALLKKPEILIMDEATSNLD-SITERAIQRtLEECTENVTTIVIA-HRLSTIK 681
Cdd:COG1134 142 QPVK----------TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDaAFQKKCLAR-IRELRESGRTVIFVsHSMGAVR 210
|
250
....*....|....*....
gi 336293682 682 K-CQKIYVMDKGRIIEEGS 699
Cdd:COG1134 211 RlCDRAIWLEKGRLVMDGD 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
482-703 |
4.18e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.61 E-value: 4.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLL--MGFYKID---QGKIILN--NYYIDDIDKETL 554
Cdd:PRK14239 6 LQVSDLSVYYN-KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNghNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 RSKISYISQDSFFFSGTIKENLEF------VGDDVTYEKMVD-ACKKAHIHEYIeslplkyKTPLEEKGSNLSGGQRQRL 627
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVYglrlkgIKDKQVLDEAVEkSLKGASIWDEV-------KDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQM 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
498-710 |
4.61e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 4.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTT----IAKLLMGFYKIdQGKIILNNYyidDIDKETLRSKISYISQDSFFF-SGTI 572
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlmnaLAFRSPKGVKG-SGSVLLNGM---PIDAKEMRAISAYVQQDDLFIpTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 573 KENLEF-----VGDDVTYEKmvdacKKAHIHEYIESLPL------KYKTPLEEKGsnLSGGQRQRLSIARALLKKPEILI 641
Cdd:TIGR00955 117 REHLMFqahlrMPRRVTKKE-----KRERVDEVLQALGLrkcantRIGVPGRVKG--LSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 642 MDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKKCQ--KIYVMDKGRIIEEGSHRELLD---KGGYY 710
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSELFELfdKIILMAEGRVAYLGSPDQAVPffsDLGHP 264
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
502-694 |
5.62e-20 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 89.15 E-value: 5.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 502 NISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKETL---RSKISYISQDSFFFSG-TIKENLE 577
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI-----KVNDQSHTGLapyQRPVSMLFQENNLFAHlTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 578 fVG-------DDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:TIGR01277 93 -LGlhpglklNAEQQEKVVDAAQQVGIADYLDRLP-----------EQLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 336293682 651 -SITERAIQRTLEECTE-NVTTIVIAHRLS-TIKKCQKIYVMDKGRI 694
Cdd:TIGR01277 161 pLLREEMLALVKQLCSErQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
482-699 |
5.76e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG----MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYI--DDIDKE--T 553
Cdd:PRK13649 3 INLQNVSYTYQagtpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 554 LRSKISYISQ--DSFFFSGTIKENLEFVGDD--VTYEKMVD-ACKKAHIHEYIESLplKYKTPLEekgsnLSGGQRQRLS 628
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEAlAREKLALVGISESL--FEKNPFE-----LSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 629 IARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIV-IAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
497-698 |
6.03e-20 |
|
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: 89.70 E-value: 6.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYyIDDIDKETLRSKISYI----SQ--------D 564
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVfgqkTQlwwdlpviD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 565 SFFFSGTIkenleFVGDDVTYEKMVDackkaHIHEYIESLPLkYKTPLEekgsNLSGGQRQRLSIARALLKKPEILIMDE 644
Cdd:cd03267 115 SFYLLAAI-----YDLPPARFKKRLD-----ELSELLDLEEL-LDTPVR----QLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 645 ATSNLDSITERAIQRTL-EECTENVTTIVI-AHRLSTIKK-CQKIYVMDKGRIIEEG 698
Cdd:cd03267 180 PTIGLDVVAQENIRNFLkEYNRERGTTVLLtSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
482-706 |
7.37e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 90.18 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQD--SFFFSGTIKE-------NLEFVGDDVTyEKMVDACKKAHIHEYieslplKYKTPleekgSNLSGGQRQRLSIARA 632
Cdd:PRK13647 85 FQDpdDQVFSSTVWDdvafgpvNMGLDKDEVE-RRVEEALKAVRMWDF------RDKPP-----YHLSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 633 LLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLS-TIKKCQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
498-675 |
7.65e-20 |
|
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: 89.06 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYisqdSFFFSGTIKENLE 577
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNY----SLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 578 FVGDDVTYEkMVDACKKAHIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAI 657
Cdd:TIGR01184 77 LAVDRVLPD-LSKSERRAIVEEHIALVGLTEAA--DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|
gi 336293682 658 Q-RTLEECTEN-VTTIVIAH 675
Cdd:TIGR01184 154 QeELMQIWEEHrVTVLMVTH 173
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
483-694 |
8.53e-20 |
|
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: 87.49 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSfaygmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID-KETLRSKISYI 561
Cdd:cd03215 6 EVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQD----SFFFSGTIKENLefvgddvtyekmvdackkahiheyieSLPlkyktpleekgSNLSGGQRQRLSIARALLKKP 637
Cdd:cd03215 81 PEDrkreGLVLDLSVAENI--------------------------ALS-----------SLLSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 638 EILIMDEATSNLDSITERAIQRTLEECTENVTTIVIahrLST-----IKKCQKIYVMDKGRI 694
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
482-703 |
1.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.89 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG----MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYID----DIDKET 553
Cdd:PRK13641 3 IKFENVDYIYSpgtpMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 554 LRSKISYISQ--DSFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESlplkyKTPLEekgsnLSGGQRQ 625
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFgpknfgFSEDEAKEKALKWLKKVGLSEDLIS-----KSPFE-----LSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDSIT-ERAIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEI 232
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
482-704 |
1.06e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.78 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID-KETLRSKISY 560
Cdd:PRK11614 6 LSFDKVSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDSFFFSG-TIKENLE---FVGDDVTYEKmvdackkaHIHEYIESLPLKYKTPLEEKGSnLSGGQRQRLSIARALLKK 636
Cdd:PRK11614 85 VPEGRRVFSRmTVEENLAmggFFAERDQFQE--------RIKWVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLS--TIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
497-704 |
1.07e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.04 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYID---DIDKE-----TLRSKISYISQD-SFF 567
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarSLSQQkglirQLRQHVGFVFQNfNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGTIKENLefVGDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKgsNLSGGQRQRLSIARALLKKPEILIMDEATS 647
Cdd:PRK11264 98 PHRTVLENI--IEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPR--RLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 648 NLDS--ITE-RAIQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK11264 174 ALDPelVGEvLNTIRQLAQ--EKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
10-137 |
1.12e-19 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature.
Pssm-ID: 239103 [Multi-domain] Cd Length: 129 Bit Score: 85.40 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 10 VKQHDIQDCGPACLATISKQ-YGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEeiFNNLPTPLIAH 88
Cdd:cd02423 4 VRQSYDFSCGPAALATLLRYyGGINITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLNLDK--LNALQIPVIVL 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 336293682 89 VIIDDVLlHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFL 137
Cdd:cd02423 82 VNNGGYG-HFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNALFV 129
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
191-457 |
1.27e-19 |
|
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: 89.88 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 191 LID-----DILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEII 265
Cdd:cd18573 22 LIDvaskeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 266 SRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFT--CFVPIVLYLILVFGfkNKLKKVNRRVMEDNASL 342
Cdd:cd18573 102 SRLsSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVmlLVVPPIAVGAVFYG--RYVRKLSKQVQDALADA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 343 TSYLVESLEGIETVKAFNGEGlvrlKTENKFLKFMKSYFKHGYTYNV-QGTLMDTI--SGGFGI-CLLWFGGSLVLKGEV 418
Cdd:cd18573 180 TKVAEERLSNIRTVRAFAAER----KEVERYAKKVDEVFDLAKKEALaSGLFFGSTgfSGNLSLlSVLYYGGSLVASGEL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 336293682 419 TIGELISFnaLL--AYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18573 256 TVGDLTSF--LMyaVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
482-709 |
1.46e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.78 E-value: 1.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDketlRSKISYI 561
Cdd:COG4152 2 LELKGLTKRFGDK-TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSfffsG-----TIKENLEFVGD--DVTYEkmvDAckKAHIHEYIESLPL--KYKTPLEEkgsnLSGGQRQRLSIARA 632
Cdd:COG4152 77 PEER----GlypkmKVGEQLVYLARlkGLSKA---EA--KRRADEWLERLGLgdRANKKVEE----LSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 633 LLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDKGGY 709
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSsHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
482-698 |
2.04e-19 |
|
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: 87.16 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNvlnDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyIDDIDKETLRSKISYI 561
Cdd:cd03298 1 VRLDKIRFSYGEQPM---HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG-TIKENlefVG---------DDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIAR 631
Cdd:cd03298 76 FQENNLFAHlTVEQN---VGlglspglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALAR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 632 ALLKKPEILIMDEATSNLDSITERAIQR-TLEECTEN-VTTIVIAHRLSTIKKC-QKIYVMDKGRIIEEG 698
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDlVLDLHAETkMTVLMVTHQPEDAKRLaQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
172-457 |
2.53e-19 |
|
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: 89.07 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 172 IASILVTIL--GIAGSFYyEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVV 249
Cdd:cd18577 13 AALPLMTIVfgDLFDAFT-DFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 250 KLPMNFFGTRKVGEIISRFN-DGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQN--LKLFFTCFVPIVLYLILVFGFKn 326
Cdd:cd18577 92 RQDIAWFDKNGAGELTSRLTsDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSwkLTLVLLATLPLIAIVGGIMGKL- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 327 kLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQ-GTLMDTISGGFGICl 405
Cdd:cd18577 171 -LSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGlGLLFFIIFAMYALA- 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 406 LWFGGSLVLKGEVTIGELIS--FNALLAYFIqpigrLINLQPQLQ---EAIVASDRL 457
Cdd:cd18577 249 FWYGSRLVRDGEISPGDVLTvfFAVLIGAFS-----LGQIAPNLQafaKARAAAAKI 300
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
497-709 |
3.77e-19 |
|
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: 86.04 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGF--YKIDQGKIILNNYYIDDID-KETLRSKISYISQDSFFFSG-TI 572
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPpEERARLGIFLAFQYPPEIPGvKN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 573 KENLEFVGDdvtyekmvdackkahiheyieslplkyktpleekgsNLSGGQRQRLSIARALLKKPEILIMDEATSNLD-- 650
Cdd:cd03217 95 ADFLRYVNE------------------------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDid 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 651 --SITERAIQRTLEectENVTTIVIAH--RLSTIKKCQKIYVMDKGRIIEEGShREL---LDKGGY 709
Cdd:cd03217 139 alRLVAEVINKLRE---EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELaleIEKKGY 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
482-705 |
4.16e-19 |
|
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: 91.28 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKT----TIAKLLMGFYKIDQGKIILNNYYIDDIDKETL 554
Cdd:COG4172 7 LSVEDLSVAFGQGGGtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 R----SKISYISQD---SFffsgtikeN-LEFVGDDVT-----YEKMVDACKKAHIHEYIES--LP-----LK-YktPLE 613
Cdd:COG4172 87 RrirgNRIAMIFQEpmtSL--------NpLHTIGKQIAevlrlHRGLSGAAARARALELLERvgIPdperrLDaY--PHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 614 ekgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECT--ENVTTIVIAHRLSTIKK-CQKIYVMD 690
Cdd:COG4172 157 -----LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQreLGMALLLITHDLGVVRRfADRVAVMR 231
|
250
....*....|....*
gi 336293682 691 KGRIIEEGSHRELLD 705
Cdd:COG4172 232 QGEIVEQGPTAELFA 246
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
482-694 |
4.28e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.85 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET---LRSKI 558
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 SYISQDS-FFFSGTIKENLEF-------VGDDVTyEKMVDACKKAHIHEYIESLPLKyktpleekgsnLSGGQRQRLSIA 630
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIpliiagaSGDDIR-RRVSAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEECTE-NVTTIVIAHRLSTI-KKCQKIYVMDKGRI 694
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
482-704 |
4.38e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 87.28 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKL---LMGFY---KIdQGKIILNNYYIDDIDKETLR 555
Cdd:PRK14247 4 IEIRDLKVSFG-QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYpeaRV-SGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 SKISYISQ-DSFFFSGTIKENlefVGDDVTYEKMVDACKK--AHIHEYIESLPL--KYKTPLEEKGSNLSGGQRQRLSIA 630
Cdd:PRK14247 82 RRVQMVFQiPNPIPNLSIFEN---VALGLKLNRLVKSKKElqERVRWALEKAQLwdEVKDRLDAPAGKLSGGQQQRLCIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQKiYV--MDKGRIIEEGSHRELL 704
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISD-YVafLYKGQIVEWGPTREVF 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
497-699 |
4.52e-19 |
|
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: 87.40 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDK----ETLRSKISYisqdSF-----F 567
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---RDITGlpphRIARLGIAR----TFqnprlF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGTIKENLE----------FVGDDVTYEKMVDACKKAH--IHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLK 635
Cdd:COG0411 92 PELTVLENVLvaaharlgrgLLAALLRLPRARREEREARerAEELLERVGLADR--ADEPAGNLSYGQQRRLEIARALAT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 636 KPEILIMDEATSNLdSITERA-----IQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:COG0411 170 EPKLLLLDEPAAGL-NPEETEelaelIRRLRDE--RGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
496-703 |
5.00e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.51 E-value: 5.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 496 NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyIDDIDKETLRSKISYISQD-SFFFSGTIKE 574
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG--VDLSHVPPYQRPINMMFQSyALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 575 NLEFvgdDVTYEKMVDACKKAHIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITE 654
Cdd:PRK11607 111 NIAF---GLKQDKLPKAEIASRVNEMLGLVHMQEFA--KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 336293682 655 RAIQRTLEECTENV--TTIVIAH-RLSTIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK11607 186 DRMQLEVVDILERVgvTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
486-704 |
6.59e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.02 E-value: 6.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 486 NVSFAYGMRDN--VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNN---YYIDDI---DKETLRSK 557
Cdd:PRK14246 12 NISRLYLYINDkaILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlYFGKDIfqiDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYI-SQDSFFFSGTIKENLEF------VGDDVTYEKMVDACKKAhiheyiESLPLKYKTPLEEKGSNLSGGQRQRLSIA 630
Cdd:PRK14246 92 VGMVfQQPNPFPHLSIYDNIAYplkshgIKEKREIKKIVEECLRK------VGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 631 RALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIAHRLSTIKKCQK-IYVMDKGRIIEEGSHRELL 704
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADyVAFLYNGELVEWGSSNEIF 240
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
12-137 |
8.03e-19 |
|
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in all sub-families.
Pssm-ID: 239073 [Multi-domain] Cd Length: 122 Bit Score: 82.82 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 12 QHDIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEeiFNNLPTPLIAHVII 91
Cdd:cd02259 1 GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAA--LSRLQLPALLLWKQ 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 336293682 92 DdvllHFVVVHKITKKYILIADPGR-GMIKYKPDEFFKIWSDVLIFL 137
Cdd:cd02259 79 G----HFVILYGADKGQVLIADPLEeGPVTLSESELEERWTGHWVLL 121
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
482-703 |
8.31e-19 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 88.60 E-value: 8.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDKETLRS-KISY 560
Cdd:PRK10851 3 IEIANIKKSFG-RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHARDrKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQD-SFFFSGTIKENLEFvGDDV--TYEKMVDACKKAHIHEYIESLPLKYktpLEEK-GSNLSGGQRQRLSIARALLKK 636
Cdd:PRK10851 79 VFQHyALFRHMTVFDNIAF-GLTVlpRRERPNAAAIKAKVTQLLEMVQLAH---LADRyPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 637 PEILIMDEATSNLDSITERAIQRTLEECTENV--TTIVIAH-RLSTIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
482-692 |
9.25e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 9.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID-KETLRSKISY 560
Cdd:PRK09700 6 ISMAGIGKSFGPV-HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQD-SFFFSGTIKENLeFVGDDVTYEKM----VDAcKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLK 635
Cdd:PRK09700 85 IYQElSVIDELTVLENL-YIGRHLTKKVCgvniIDW-REMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 636 KPEILIMDEATSNL-DSITER--AIQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKG 692
Cdd:PRK09700 163 DAKVIIMDEPTSSLtNKEVDYlfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
497-703 |
1.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYI-DDIDKET---------------LRSKISY 560
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgDKKNNHElitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQ--DSFFFSGTIKENLEFvGDDVTYEKMVDACKKAHIheYIESLPLKYkTPLEEKGSNLSGGQRQRLSIARALLKKPE 638
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMF-GPVALGVKKSEAKKLAKF--YLNKMGLDD-SYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 639 ILIMDEATSNLDSITERA-IQRTLEECTENVTTIVIAHRLSTI-KKCQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
500-704 |
1.06e-18 |
|
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: 88.23 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 500 DINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL----RSKISYISQDSFFFSG-TIKE 574
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlpphRRRIGYVFQEARLFPHlSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 575 NLEFVgddvtYEKMVDACKKAHIHEYIESL---PLkyktpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS 651
Cdd:COG4148 97 NLLYG-----RKRAPRAERRISFDEVVELLgigHL-----LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 336293682 652 ITERAIQRTLEE-CTE-NVTTIVIAH------RLSTikkcqKIYVMDKGRIIEEGSHRELL 704
Cdd:COG4148 167 ARKAEILPYLERlRDElDIPILYVSHsldevaRLAD-----HVVLLEQGRVVASGPLAEVL 222
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
482-703 |
1.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQ--DSFFFSGTIKENLEF----VG-DDVTYEKMVD-ACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARAL 633
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFgpinLGlDEETVAHRVSsALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 634 LKKPEILIMDEATSNLDSITERAIQRTLEECTEN--VTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
496-676 |
1.97e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 84.62 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 496 NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIIlnnyyiDDIDKETLRSKISYIsqDSFFFSGTIKEN 575
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC------VDVPDNQFGREASLI--DAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 LEFVGDdvtyEKMVDAckkahiheyieslPLkYKTPLEEkgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITER 655
Cdd:COG2401 116 VELLNA----VGLSDA-------------VL-WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180
....*....|....*....|...
gi 336293682 656 AIQRTL-EECTENVTTIVIA-HR 676
Cdd:COG2401 174 RVARNLqKLARRAGITLVVAtHH 196
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
170-457 |
2.07e-18 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 86.39 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILV---TILGIAGSFYYEFLIDD-ILPNNLKAsLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYY 245
Cdd:cd18546 1 LALALLLVvvdTAASLAGPLLVRYGIDSgVRAGDLGV-LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 246 NHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGF 324
Cdd:cd18546 80 AHLQRLSLDFHERETSGRIMTRMtSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 325 KNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGlvrlKTENKFLKFMKSYFK-HGYTYNVQGT---LMDTISGG 400
Cdd:cd18546 160 RRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRER----RNAERFAELSDDYRDaRLRAQRLVAIyfpGVELLGNL 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 401 FGICLLWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18546 236 ATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
492-693 |
2.23e-18 |
|
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: 84.79 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 492 GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYiDDID------KETL---RSKISYIS 562
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG-GWVDlaqaspREILalrRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 563 QdsfFFS-----GTIkenlefvgdDVTYEKMVD-------ACKKA-------HIHEYIESLPlkyktPleekgSNLSGGQ 623
Cdd:COG4778 100 Q---FLRviprvSAL---------DVVAEPLLErgvdreeARARArellarlNLPERLWDLP-----P-----ATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 624 RQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIV-IAHRLSTIKK-CQKIYVMDKGR 693
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
482-704 |
2.89e-18 |
|
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: 88.71 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRD----NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGK--IILNNYYIDDIDKETL- 554
Cdd:TIGR03269 280 IKVRNVSKRYISVDrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEWVDMTKPGPDg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 --RSK--ISYISQD-SFFFSGTIKENL-EFVGDDVTYE----KMVDACKKAHIHEYieslplKYKTPLEEKGSNLSGGQR 624
Cdd:TIGR03269 360 rgRAKryIGILHQEyDLYPHRTVLDNLtEAIGLELPDElarmKAVITLKMVGFDEE------KAEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 625 QRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHR 701
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPE 513
|
...
gi 336293682 702 ELL 704
Cdd:TIGR03269 514 EIV 516
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
504-675 |
3.00e-18 |
|
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: 84.77 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 504 SIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyidDIDKETLRSKISYISQDsffFSGTIkenlefvgDDV 583
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDTVSYKPQYIKAD---YEGTV--------RDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 584 TYEKMVDACkkahIHEYIES---LPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS----ITERA 656
Cdd:cd03237 82 LSSITKDFY----THPYFKTeiaKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKV 157
|
170
....*....|....*....
gi 336293682 657 IQRTLEEctENVTTIVIAH 675
Cdd:cd03237 158 IRRFAEN--NEKTAFVVEH 174
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
497-706 |
3.29e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.50 E-value: 3.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKiDQGKIILNNYYIDDID---------KETLRSKISYISQD--- 564
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRFRWNGIDllklsprerRKIIGREIAMIFQEpss 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 565 SFFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPL----KYKTPLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:COG4170 101 CLDPSAKIGDQLIEAIPSWTFKGKWWQRFKWRKKRAIELLHRvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 641 IMDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:COG4170 181 IADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
498-695 |
3.87e-18 |
|
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: 83.47 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTT----IAKLLMGFYKIDqGKIILNNYYIDDIdKETLRSKISYISQDSFFFSG-TI 572
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEF-AEKYPGEIIYVSEEDVHFPTlTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 573 KENLEFVGDdvtyekmvdaCKKahiHEYIeslplkyktpleekgSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSI 652
Cdd:cd03233 101 RETLDFALR----------CKG---NEFV---------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 336293682 653 TERAIQRTLEECT--ENVTTIVIAHRLS--TIKKCQKIYVMDKGRII 695
Cdd:cd03233 153 TALEILKCIRTMAdvLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
493-705 |
5.84e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 5.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 493 MRDNVLNDINISIHN----------GEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDK---ETLRSKIS 559
Cdd:PRK10261 325 LRSGLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFffsgTIKENLEFVGDDVTYEKMV------DACKKaHIHEYIESLPLK----YKTPLEekgsnLSGGQRQRLSI 629
Cdd:PRK10261 405 FIFQDPY----ASLDPRQTVGDSIMEPLRVhgllpgKAAAA-RVAWLLERVGLLpehaWRYPHE-----FSGGQRQRICI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 630 ARALLKKPEILIMDEATSNLD-SITERAIQRTLEECTE-NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK10261 475 ARALALNPKVIIADEAVSALDvSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
10-139 |
8.24e-18 |
|
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442502 [Multi-domain] Cd Length: 179 Bit Score: 81.58 E-value: 8.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 10 VKQHDIQDCGPACLATI-SKQYGLKLP----ISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSkkeeiFNNLPT- 83
Cdd:COG3271 46 VRQQYDYSCGAAALATLlNYHYGRPVSeaevLEGMLTHGDQRRRGFSLLDMKRYLEALGLRADGYRLT-----LDDLAQl 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 84 --PLIAHVIIDDVLlHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFLTP 139
Cdd:COG3271 121 giPAIVLINLGGYK-HFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFVVP 177
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
484-705 |
9.10e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.24 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 484 LENVSFAYGMRDNVLndiniSIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID----KETLRSKIS 559
Cdd:PRK10070 35 LEKTGLSLGVKDASL-----AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaelREVRRKKIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQD-SFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARA 632
Cdd:PRK10070 110 MVFQSfALMPHMTVLDNTAFgmelagINAEERREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 633 LLKKPEILIMDEATSNLDSITERAIQRTLE--ECTENVTTIVIAHRL-STIKKCQKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK10070 179 LAINPDILLMDEAFSALDPLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
482-706 |
9.13e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.59 E-value: 9.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTT----IAKLLmgfyKIDQGKIILNNYYIDDIDKETLRSK 557
Cdd:COG4604 2 IEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTllsmISRLL----PPDSGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKENLEFvG-----------DDvtyekmvdackKAHIHEYIESLPLkykTPLEEKG-SNLSGGQR 624
Cdd:COG4604 77 LAILRQENHINSRlTVRELVAF-GrfpyskgrltaED-----------REIIDEAIAYLDL---EDLADRYlDELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 625 QRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVI-------AHRLStikkcQKIYVMDKGRIIE 696
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADELGKTVVIvlhdinfASCYA-----DHIVAMKDGRVVA 216
|
250
....*....|
gi 336293682 697 EGSHRELLDK 706
Cdd:COG4604 217 QGTPEEIITP 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
482-711 |
9.27e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.85 E-value: 9.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDNVL-NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDI---DKETLRSK 557
Cdd:PRK11000 4 VTLRNVTKAYG--DVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-----FIGEKrmnDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKENLEFvGddvtyEKMVDAcKKAHIHEYIESLP--LKYKTPLEEKGSNLSGGQRQRLSIARALL 634
Cdd:PRK11000 77 VGMVFQSYALYPHlSVAENMSF-G-----LKLAGA-KKEEINQRVNQVAevLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 635 KKPEILIMDEATSNLDS---------ITE--RAIQRTLEECT-ENVTTIVIAHrlstikkcqKIYVMDKGRIIEEGSHRE 702
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAalrvqmrieISRlhKRLGRTMIYVThDQVEAMTLAD---------KIVVLDAGRVAQVGKPLE 220
|
....*....
gi 336293682 703 LldkggYYY 711
Cdd:PRK11000 221 L-----YHY 224
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
496-697 |
9.37e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 9.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 496 NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID---KETLRS-KISYISQDSFFFSG- 570
Cdd:PRK11629 23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRNqKLGFIYQFHHLLPDf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 TIKENlefvgddVTYEKMVDACKKAHIHEyiESLPLKYKTPLEEKG----SNLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:PRK11629 103 TALEN-------VAMPLLIGKKKPAEINS--RALEMLAAVGLEHRAnhrpSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 647 SNLDSITERAIQRTLEECTENVTT--IVIAHRLSTIKKCQKIYVMDKGRIIEE 697
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
483-703 |
9.76e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.00 E-value: 9.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSfaygmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNN--YYIDDIdKETLRSKISY 560
Cdd:COG1129 258 EVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSP-RDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQD----SFFFSGTIKENLEF-VGDDVTYEKMVDACK-KAHIHEYIESLPLKYKTPlEEKGSNLSGGQRQRLSIARALL 634
Cdd:COG1129 332 VPEDrkgeGLVLDLSIRENITLaSLDRLSRGGLLDRRReRALAEEYIKRLRIKTPSP-EQPVGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 635 KKPEILIMDEATSNLDSITERAIQRTLEECTEN-VTTIVI----------AHRlstikkcqkIYVMDKGRIIEEGSHREL 703
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEgKAVIVIsselpellglSDR---------ILVMREGRIVGELDREEA 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
498-710 |
1.08e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.75 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDiDKETLRSKISYI----SQ--------DS 565
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrSQlwwdlpaiDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 566 FFFSGTIKEnlefVgDDVTYEKmvdackkaHIHEYIESLPL--KYKTPLEekgsNLSGGQRQRLSIARALLKKPEILIMD 643
Cdd:COG4586 117 FRLLKAIYR----I-PDAEYKK--------RLDELVELLDLgeLLDTPVR----QLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 644 EATSNLDSITERAIQRTLEE--CTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDKGGYY 710
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
482-682 |
1.10e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.55 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID-----QGKIIL--NNYYIDDIDKETL 554
Cdd:PRK14258 8 IKVNNLSFYYDTQ-KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFfnQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 RSKISYISQDSFFFSGTikenlefVGDDVTYE-KMVDACKKAHIHEYIES------LPLKYKTPLEEKGSNLSGGQRQRL 627
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMS-------VYDNVAYGvKIVGWRPKLEIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEECT--ENVTTIVIAHRLSTIKK 682
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSR 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
482-706 |
1.16e-17 |
|
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: 86.78 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGF--YKIDQGKIILNNYY-------------- 545
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 546 -------------------IDDIDKETLRSKISYISQDSFFFSG--TIKENLEFVGDDVTYEKMvDACKKAHihEYIESL 604
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYEGK-EAVGRAV--DLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 605 PLKYKtpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECT--ENVTTIVIAHRLSTIKK 682
Cdd:TIGR03269 157 QLSHR--ITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIED 234
|
250 260
....*....|....*....|....*
gi 336293682 683 -CQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
504-690 |
1.33e-17 |
|
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: 86.76 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 504 SIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddidketlrSKISY----ISQDsffFSGTIKENLEFV 579
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYkpqyISPD---YDGTVEEFLRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 580 -GDDVT--YEKmvdackkahiHEYIEslPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS----I 652
Cdd:COG1245 426 nTDDFGssYYK----------TEIIK--PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlA 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 336293682 653 TERAIQRTLEEctENVTTIVIAHrlstikkcqKIYVMD 690
Cdd:COG1245 494 VAKAIRRFAEN--RGKTAMVVDH---------DIYLID 520
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
484-686 |
1.59e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 484 LENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQ 563
Cdd:PRK10247 10 LQNVGYLAGDA-KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 564 DSFFFSGTIKENLEFvgddvTYEKMVDACKKAHIHEYIESLPLKyKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMD 643
Cdd:PRK10247 89 TPTLFGDTVYDNLIF-----PWQIRNQQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 336293682 644 EATSNLDSITER----AIQRTLEEctENVTTIVIAHRLSTIKKCQKI 686
Cdd:PRK10247 163 EITSALDESNKHnvneIIHRYVRE--QNIAVLWVTHDKDEINHADKV 207
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
164-456 |
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 336293682 164 KGLLLNIFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFrktlLLYMAQNIDVplLLG 243
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFL----FIRLAGKIEM--GVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 244 Y------YNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFF--TCFVPi 314
Cdd:cd18540 75 YdlrkkaFEHLQTLSFSYFDKTPVGWIMARVtSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALivLAVVP- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 315 VLYLILVFgFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGlvrlKTENKFLKFMKSYFKHGY-TYNVQGTL 393
Cdd:cd18540 154 VLAVVSIY-FQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREE----KNLREFKELTEEMRRASVrAARLSALF 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 394 MDTIS--GGFGICL-LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18540 229 LPIVLflGSIATALvLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAER 294
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
482-704 |
2.42e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.51 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:PRK13548 3 LEARNLSVRLGGRT-LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDS---FFFS-------GTIKENLEFVGDDVTYEKMVDACKKAHIHEyieslpLKYKTpleekgsnLSGGQRQRLSIAR 631
Cdd:PRK13548 82 PQHSslsFPFTveevvamGRAPHGLSRAEDDALVAAALAQVDLAHLAG------RDYPQ--------LSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 632 ALL------KKPEILIMDEATSNLDSITERAIQRTLEECT--ENVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHRE 702
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
..
gi 336293682 703 LL 704
Cdd:PRK13548 228 VL 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
499-705 |
3.35e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.60 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 499 NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL---RSKISYISQDSFF-------F 568
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPLAslnprmtI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 569 SGTIKENLEfvgddVTYEKMvdacKKAHIHEYIESLPLKY--------KTPLEekgsnLSGGQRQRLSIARALLKKPEIL 640
Cdd:PRK15079 118 GEIIAEPLR-----TYHPKL----SRQEVKDRVKAMMLKVgllpnlinRYPHE-----FSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 641 IMDEATSNLD-SITE------RAIQRTLeecteNVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK15079 184 ICDEPVSALDvSIQAqvvnllQQLQREM-----GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYH 251
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
491-704 |
3.92e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.94 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 491 YGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDI----------DKE---TLRSK 557
Cdd:PRK10619 15 YGEHE-VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNqlrLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKEN-----LEFVG--DDVTYEKMVDACKKAHIHEYIESlplKYKtpleekgSNLSGGQRQRLSI 629
Cdd:PRK10619 94 LTMVFQHFNLWSHmTVLENvmeapIQVLGlsKQEARERAVKYLAKVGIDERAQG---KYP-------VHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEECTEN-VTTIVIAHRLSTIKKCQK-IYVMDKGRIIEEGSHRELL 704
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
497-699 |
5.19e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 85.99 E-value: 5.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddidketlRSkISYISQDSFFFSGTIKENL 576
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RS-IAYVPQQAWIMNATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 577 EFVgDDVTYEKMVDACKKAHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS-ITER 655
Cdd:PTZ00243 742 LFF-DEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGER 820
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 336293682 656 AIQRTLEECTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGS 699
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGS 864
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
498-695 |
5.25e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.60 E-value: 5.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID--QGKII-----LNNYYIddidKETLRSKISYISQDSFFFSG 570
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIfegeeLQASNI----RDTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 -TIKENLeFVGDDVT------YEKMVDACKKAhIHEyieslpLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMD 643
Cdd:PRK13549 97 lSVLENI-FLGNEITpggimdYDAMYLRAQKL-LAQ------LKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 644 EATSnldSITER------AIQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRII 695
Cdd:PRK13549 169 EPTA---SLTESetavllDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
505-690 |
5.41e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.86 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 505 IHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILnnyyiddidKETLRSKISYISQDsffFSGTIKENLEFVGDDV- 583
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---------ELKISYKPQYIKPD---YDGTVEDLLRSITDDLg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 584 -TYEKmvdackkahiHEYIEslPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD----SITERAIQ 658
Cdd:PRK13409 430 sSYYK----------SEIIK--PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIR 497
|
170 180 190
....*....|....*....|....*....|..
gi 336293682 659 RTLEEctENVTTIVIAHrlstikkcqKIYVMD 690
Cdd:PRK13409 498 RIAEE--REATALVVDH---------DIYMID 518
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
512-699 |
5.41e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 512 ALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL----RSKISYISQDSFFFSG-TIKENLEFvG----DD 582
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppeKRRIGYVFQDARLFPHyKVRGNLRY-GmaksMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 583 VTYEKMVDACKkahiheyIESLplkyktpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLE 662
Cdd:PRK11144 107 AQFDKIVALLG-------IEPL-------LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 336293682 663 ECTENVTT--IVIAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:PRK11144 173 RLAREINIpiLYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
482-703 |
8.32e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 8.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFY---KIDQGKIILNNYYID-------DIDK 551
Cdd:PRK09984 5 IRVEKLAKTFN-QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlarDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 552 EtlRSKISYISQD-SFFFSGTIKENLEF--VGDDVTYEKMVDACKKAHIHEYIESLP-LKYKTPLEEKGSNLSGGQRQRL 627
Cdd:PRK09984 84 S--RANTGYIFQQfNLVNRLSVLENVLIgaLGSTPFWRTCFSWFTREQKQRALQALTrVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTEN--VTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
167-456 |
9.82e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 81.84 E-value: 9.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 167 LLNIFIASILVTILGIA-------GSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVP 239
Cdd:cd18565 9 ILNRLFDLAPPLLIGVAidavfngEASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 240 LLLGYYNHVVKLPMNFFGTRKVGEIISRFND---------GDKIRNAISSVTLTLMIdvlmavvgGAILYLQNLKLFFTC 310
Cdd:cd18565 89 LRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNdvnqlerflDDGANSIIRVVVTVLGI--------GAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 311 FVPIVLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGL----VRLKTENKFLKFMKSYFkhgyT 386
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFererVADASEEYRDANWRAIR----L 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 387 YNVQGTLMDTISGGFGICLLWFGGSLVLKG------EVTIGELISFNALLAYFIQPI---GRLINlqpQLQEAIVASDR 456
Cdd:cd18565 237 RAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLtrlGDLID---QYQRAMASAKR 312
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
482-706 |
1.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.93 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG----MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET---- 553
Cdd:PRK13643 2 IKFEKVNYTYQpnspFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 554 LRSKISYISQ--DSFFFSGTIKENLEFVGDDVTYEKMvDACKKAHihEYIESLPLKY----KTPLEekgsnLSGGQRQRL 627
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKE-KAEKIAA--EKLEMVGLADefweKSPFE-----LSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIV-IAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVlVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
.
gi 336293682 706 K 706
Cdd:PRK13643 234 E 234
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
12-139 |
2.21e-16 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239100 [Multi-domain] Cd Length: 127 Bit Score: 76.14 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 12 QHDIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTsKKEEIfNNLPTPLIAHviI 91
Cdd:cd02419 6 QTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRL-DLEEL-GQLKLPCILH--W 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 336293682 92 DdvLLHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIFLTP 139
Cdd:cd02419 82 D--MNHFVVLKKVSRRRIVIHDPALGKRKLSLEEASRHFTGVALELWP 127
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
481-650 |
2.27e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 78.29 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 481 CISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID---QGKIILNNYYIDDIDkeTLRSK 557
Cdd:COG4136 1 MLSLENLTITLGGRP-LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALP--AEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQDSFFFSG-TIKENLEFVgddvTYEKMVDACKKAHIHEYIESLPLKY---KTPLEekgsnLSGGQRQRLSIARAL 633
Cdd:COG4136 78 IGILFQDDLLFPHlSVGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGfadRDPAT-----LSGGQRARVALLRAL 148
|
170
....*....|....*..
gi 336293682 634 LKKPEILIMDEATSNLD 650
Cdd:COG4136 149 LAEPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
482-709 |
2.92e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.82 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG----MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKE----T 553
Cdd:PRK13646 3 IRFDNVSYTYQkgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyirP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 554 LRSKISYISQ--DSFFFSGTIKENLEFVGDDVtyeKMVDACKKAHIHEYIESLPLKyKTPLEEKGSNLSGGQRQRLSIAR 631
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNF---KMNLDEVKNYAHRLLMDLGFS-RDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 632 ALLKKPEILIMDEATSNLDSITERAIQRTLEECT--ENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDKGG 708
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKDKK 238
|
.
gi 336293682 709 Y 709
Cdd:PRK13646 239 K 239
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
482-661 |
4.25e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 78.75 E-value: 4.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDN---VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtlRSKI 558
Cdd:COG4525 4 LTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--RGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 559 syISQDSFFFSGTIKENLEF------VGddvtyekmvdackKAHIHEYIESLpLKyKTPLEEKGSN----LSGGQRQRLS 628
Cdd:COG4525 82 --FQKDALLPWLNVLDNVAFglrlrgVP-------------KAERRARAEEL-LA-LVGLADFARRriwqLSGGMRQRVG 144
|
170 180 190
....*....|....*....|....*....|...
gi 336293682 629 IARALLKKPEILIMDEATSNLDSITERAIQRTL 661
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
482-704 |
4.51e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.74 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYG----MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKI--ILNN------------ 543
Cdd:PRK13651 3 IKVKNIVKIFNkklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 544 YYIDDIDKETLRSKISYISQ------------DSFFFSGTIKENLEF--VGDDVTYEkmvDACKKAHihEYIE--SLPLK 607
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEirrrvgvvfqfaEYQLFEQTIEKDIIFgpVSMGVSKE---EAKKRAA--KYIElvGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 608 YktpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRL-STIKKCQK 685
Cdd:PRK13651 158 Y---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVtHDLdNVLEWTKR 234
|
250
....*....|....*....
gi 336293682 686 IYVMDKGRIIEEGSHRELL 704
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDIL 253
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
496-697 |
5.79e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 496 NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKE---TLRSK-ISYISQdSFFFSGT 571
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAKhVGFVFQ-SFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 572 IKEnLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS 651
Cdd:PRK10584 103 LNA-LENVELPALLRGESSRQSRNGAKALLEQLGLGKR--LDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 336293682 652 ITERAIQRTLEECTEN--VTTIVIAHRLSTIKKCQKIYVMDKGRIIEE 697
Cdd:PRK10584 180 QTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
179-440 |
8.86e-16 |
|
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: 78.31 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 179 ILGIAGSFYYEFLIDDIlpNNLKASLHSISIAMLILL-LFKIVTEFF---RKTLLLYMAQNIDVPLLLGYYNHVVKLPMN 254
Cdd:cd18582 10 LLNVAVPFLLKYAVDAL--SAPASALLAVPLLLLLAYgLARILSSLFnelRDALFARVSQRAVRRLALRVFRHLHSLSLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 255 FFGTRKVGEIISRFNDGDK-IRNAISSVTLTLMIDVL-MAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVN 332
Cdd:cd18582 88 FHLSRKTGALSRAIERGTRgIEFLLRFLLFNILPTILeLLLVCGILWYLYGWSYALITLVTVALYVAFTIKVTEWRTKFR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 333 RRVMEDNASLTSYLVESLEGIETVKAFNGEGLVrlktENKFLKFMKSYFKHgyTYNVQGTLMdTISGG----FGICL--- 405
Cdd:cd18582 168 REMNEADNEANAKAVDSLLNYETVKYFNNEEYE----AERYDKALAKYEKA--AVKSQTSLA-LLNIGqaliISLGLtai 240
|
250 260 270
....*....|....*....|....*....|....*
gi 336293682 406 LWFGGSLVLKGEVTIGELISFNALLAYFIQPIGRL 440
Cdd:cd18582 241 MLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
478-695 |
8.86e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 81.31 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 478 LAGCISLENVSFAYGMRD---NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL 554
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 ----RSKISYISQDSFFFSG-TIKENLEFvgdDVTYEKMVDACKKAHIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSI 629
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHlTAAQNVEV---PAVYAGLERKQRLLRAQELLQRLGLEDRV--EYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTIKKCQKIYVMDKGRII 695
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
484-650 |
1.63e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.38 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 484 LENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKI----ILNNYYID----DIDKETlr 555
Cdd:PRK11147 322 MENVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIhcgtKLEVAYFDqhraELDPEK-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 556 skisyisqdsfffsgTIKENLEfvgdDVTYEKMVDAcKKAHIHEYIESL---PLKYKTPLEEkgsnLSGGQRQRLSIARA 632
Cdd:PRK11147 399 ---------------TVMDNLA----EGKQEVMVNG-RPRHVLGYLQDFlfhPKRAMTPVKA----LSGGERNRLLLARL 454
|
170
....*....|....*...
gi 336293682 633 LLKKPEILIMDEATSNLD 650
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLD 472
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
477-706 |
2.22e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.36 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 477 TLAGCISLENVSFAYGMRD----NVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYID-DIDK 551
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPaNLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 552 ----ETLRSKISYISQ--DSFFFSGTIKENLEF----VGDDV--TYEKMVDACKkahiheyIESLPLKY--KTPLEekgs 617
Cdd:PRK13645 82 ikevKRLRKEIGLVFQfpEYQLFQETIEKDIAFgpvnLGENKqeAYKKVPELLK-------LVQLPEDYvkRSPFE---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 618 nLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVTT--IVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:PRK13645 151 -LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKriIMVTHNMDQVLRiADEVIVMHEGKV 229
|
250
....*....|....*...
gi 336293682 695 IEEG------SHRELLDK 706
Cdd:PRK13645 230 ISIGspfeifSNQELLTK 247
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
192-456 |
2.23e-15 |
|
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: 77.20 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 192 IDDILPNNlkaSLHSISIAMLILLLFKIVT---EFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRF 268
Cdd:cd18572 23 IDAVVADG---SREAFYRAVLLLLLLSVLSglfSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 269 -NDGDKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCF--VPIVLYLILVFGfkNKLKKVNRRVMEDNASLTSY 345
Cdd:cd18572 100 tSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFitVPVIALITKVYG--RYYRKLSKEIQDALAEANQV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 346 LVESLEGIETVKAFNGEglvrlKTENK-FLKFMKSYFKH--------GYTYNVQGTLMDTISGGfgicLLWFGGSLVLKG 416
Cdd:cd18572 178 AEEALSNIRTVRSFATE-----EREARrYERALDKALKLsvrqalayAGYVAVNTLLQNGTQVL----VLFYGGHLVLSG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 336293682 417 EVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18572 249 RMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEK 288
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
497-686 |
4.81e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.53 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDIDKETLRSKISYIS-QDSFFFSGTIKEN 575
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGhRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 LEF----VGDDvtyekmvdackKAHIHEYIESLPLKyktPLEE-KGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:PRK13539 94 LEFwaafLGGE-----------ELDIAAALEAVGLA---PLAHlPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 336293682 651 SITERAIQRTLEECTENVTTIVIA-HRLSTIKKCQKI 686
Cdd:PRK13539 160 AAAVALFAELIRAHLAQGGIVIAAtHIPLGLPGAREL 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
482-698 |
5.45e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.48 E-value: 5.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIdketlRSKISYI 561
Cdd:PRK11247 13 LLLNAVSKRYGER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSGtiKENLEFVGDDVTYEKMVDAckkahiHEYIESLPLKYKTPleEKGSNLSGGQRQRLSIARALLKKPEILI 641
Cdd:PRK11247 87 FQDARLLPW--KKVIDNVGLGLKGQWRDAA------LQALAAVGLADRAN--EWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 642 MDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLStikkcQKIYVMDKGRIIEEG 698
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVS-----EAVAMADRVLLIEEG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
482-661 |
6.88e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.12 E-value: 6.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKEtlRSKIsyI 561
Cdd:PRK11248 2 LQISHLYADYGGKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE--RGVV--F 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSGTIKENLEF------VGDDVTYEKMVDACKKAHIHEYIESLPLKyktpleekgsnLSGGQRQRLSIARALLK 635
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFglqlagVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-----------LSGGQRQRVGIARALAA 145
|
170 180
....*....|....*....|....*.
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTL 661
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLL 171
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
497-699 |
7.89e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.00 E-value: 7.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTT----IAKLLMGFYKIDQGKIILNNYYIDDIDKEtLRSKISYISQ-DSFFFSGT 571
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVVYNAEtDVHFPHLT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 572 IKENLEFV---------GDDVTYEkmVDACKKAHIHEYIESLPLKYKTpleeKGSN-----LSGGQRQRLSIARALLKKP 637
Cdd:TIGR00956 155 VGETLDFAarcktpqnrPDGVSRE--EYAKHIADVYMATYGLSHTRNT----KVGNdfvrgVSGGERKRVSIAEASLGGA 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 638 EILIMDEATSNLDSITERAIQRTLEECtenvTTIVIAHRLSTIKKC-QKIY-------VMDKGRIIEEGS 699
Cdd:TIGR00956 229 KIQCWDNATRGLDSATALEFIRALKTS----ANILDTTPLVAIYQCsQDAYelfdkviVLYEGYQIYFGP 294
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
482-704 |
8.24e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.19 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:PRK09536 4 IDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQD---SFFFSG-TIKE------NLEFVGDDVTYEKMVD-ACKKAHIHEYIESlplkyktPLEEkgsnLSGGQRQRLSIA 630
Cdd:PRK09536 83 PQDtslSFEFDVrQVVEmgrtphRSRFDTWTETDRAAVErAMERTGVAQFADR-------PVTS----LSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 631 RALLKKPEILIMDEATSNLDsiTERAIqRTLE---ECTENVTTIVIA-HRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLD--INHQV-RTLElvrRLVDDGKTAVAAiHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
483-721 |
1.71e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.19 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL-------- 554
Cdd:PRK11701 8 SVRGLTKLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 -RSKISYISQD-------SFFFSGTIKENLEFVGDDvTY----EKMVDACKKAHIH-EYIESLPLKYktpleekgsnlSG 621
Cdd:PRK11701 87 lRTEWGFVHQHprdglrmQVSAGGNIGERLMAVGAR-HYgdirATAGDWLERVEIDaARIDDLPTTF-----------SG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 622 GQRQRLSIARALLKKPEILIMDEATSNLD-SITERAIQ--RTLEEcTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEE 697
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDvSVQARLLDllRGLVR-ELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVES 233
|
250 260
....*....|....*....|....
gi 336293682 698 GshrelldkggyyyrlWTEQTLDD 721
Cdd:PRK11701 234 G---------------LTDQVLDD 242
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
482-704 |
2.17e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.51 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYI 561
Cdd:PRK11231 3 LRTENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG-TIKENLEF------------VGDDvtyEKMVD-ACKKAHIHEYIESlplkyktPLEEkgsnLSGGQRQRL 627
Cdd:PRK11231 82 PQHHLTPEGiTVRELVAYgrspwlslwgrlSAED---NARVNqAMEQTRINHLADR-------RLTD----LSGGQRQRA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 628 SIARALLKKPEILIMDEATSNLDSITERAIQRTLEEC-TENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK11231 148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
498-695 |
2.40e-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: 76.40 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID--QGKIILNNYYIDDID-KETLRSKISYISQDSFFFSG-TIK 573
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNiRDTERAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 574 ENLeFVGDDVT-------YEKMVDACkkahiHEYIESLPLKyKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:TIGR02633 97 ENI-FLGNEITlpggrmaYNAMYLRA-----KNLLRELQLD-ADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 336293682 647 SnldSITERAIQRTLEECTE----NVTTIVIAHRLSTIKK-CQKIYVMDKGRII 695
Cdd:TIGR02633 170 S---SLTEKETEILLDIIRDlkahGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
500-704 |
3.42e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.29 E-value: 3.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 500 DINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQD---SFFFSGTIKENL 576
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpstSLNPRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 577 EF---VGDDVTYEKmvdacKKAHIHEYIESLPLkyktpLEEKGS----NLSGGQRQRLSIARALLKKPEILIMDEATSNL 649
Cdd:PRK15112 111 DFplrLNTDLEPEQ-----REKQIIETLRQVGL-----LPDHASyyphMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 650 D-SITERAIQRTLE-ECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK15112 181 DmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
245-457 |
4.53e-14 |
|
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: 73.33 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 245 YNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTL---MIDVLMAVVggAILYLQNLKLFFTCFVPIVLYLILV 321
Cdd:cd18583 77 FNHVMNLSMDFHDSKKSGEVLKAIEQGSSINDLLEQILFQIvpmIIDLVIAIV--YLYYLFDPYMGLIVAVVMVLYVWST 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 322 FGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTI--SG 399
Cdd:cd18583 155 IKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLIltLG 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 400 GFGICLLwfGGSLVLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18583 235 LLAGCFL--AAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
482-650 |
5.18e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 5.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddidKETLRSKISYI 561
Cdd:PRK09544 5 VSLENVSVSFGQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQDSFFFSG---TIKENLEF-----VGDDVTYEKMVDAckkAHIHEYieslplkyktPLEEkgsnLSGGQRQRLSIARAL 633
Cdd:PRK09544 73 PQKLYLDTTlplTVNRFLRLrpgtkKEDILPALKRVQA---GHLIDA----------PMQK----LSGGETQRVLLARAL 135
|
170
....*....|....*..
gi 336293682 634 LKKPEILIMDEATSNLD 650
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVD 152
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
482-698 |
5.75e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLrskISYI 561
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQdsfffSGTIKENLEFVGDDVT----YEKM-VDACKKAHIHEYIES-------LPLKYKTPLEekgsnLSGGQRQRLSI 629
Cdd:PRK15056 84 PQ-----SEEVDWSFPVLVEDVVmmgrYGHMgWLRRAKKRDRQIVTAalarvdmVEFRHRQIGE-----LSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 630 ARALLKKPEILIMDEATSNLDSITERAIQRTLEEC-TENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEG 698
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
476-703 |
6.56e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 476 ETLAGCISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETL- 554
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNR-CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 555 --RSKISYISQDSFFFSG-TIKENLEFVGDDVTyeKMVDACKKAHIHEYIESLPLKYKTPLeeKGSNLSGGQRQRLSIAR 631
Cdd:PRK11831 81 tvRKRMSMLFQSGALFTDmNVFDNVAYPLREHT--QLPAPLLHSTVMMKLEAVGLRGAAKL--MPSELSGGMARRAALAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 632 ALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRL-STIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK11831 157 AIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
481-706 |
8.35e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 73.34 E-value: 8.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 481 CISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyYIDDIDKETLRSK--- 557
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-----WIGGRVVNELEPAdrd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ISYISQD-SFFFSGTIKENLEF------VGDDVTYEKMVDAckkAHIHEyIESLplkyktpLEEKGSNLSGGQRQRLSIA 630
Cdd:PRK11650 78 IAMVFQNyALYPHMSVRENMAYglkirgMPKAEIEERVAEA---ARILE-LEPL-------LDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 631 RALLKKPEILIMDEATSNLDS-------ITERAIQRTLeecteNVTTIVIAH-RLSTIKKCQKIYVMDKGRIIEEGSHRE 702
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDAklrvqmrLEIQRLHRRL-----KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVE 221
|
....
gi 336293682 703 LLDK 706
Cdd:PRK11650 222 VYEK 225
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
12-135 |
9.22e-14 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family.
Pssm-ID: 239101 [Multi-domain] Cd Length: 125 Bit Score: 68.61 E-value: 9.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 12 QHDIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRtsKKEEIFNNLPTPLIAHVII 91
Cdd:cd02420 6 QMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYK--KDLEALREVSLPAIVFWNF 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 336293682 92 DdvllHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLI 135
Cdd:cd02420 84 N----HFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVVL 123
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
498-699 |
2.51e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 71.53 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKET---LRSKISYISQDSFF------- 567
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNPYGslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGTIKENLEFVGDDVTYEKmvdackKAHIHEYIESLPLK---YKT-PleekgSNLSGGQRQRLSIARALLKKPEILIMD 643
Cdd:PRK11308 111 VGQILEEPLLINTSLSAAER------REKALAMMAKVGLRpehYDRyP-----HMFSGGQRQRIAIARALMLDPDVVVAD 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 644 EATSNLD-SIteRA--------IQRTLeecteNVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:PRK11308 180 EPVSALDvSV--QAqvlnlmmdLQQEL-----GLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
498-697 |
2.57e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.11 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYID-DIDKETLRSKISYISQDSFFFSG-TIKEN 575
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 LeFVGDDVT-------YEKMVDACKKahiheYIESLPLKY--KTPLEEkgsnLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:PRK10762 100 I-FLGREFVnrfgridWKKMYAEADK-----LLARLNLRFssDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 647 SNLDSITERAIQRTLEECTENVTTIV-IAHRLSTI-KKCQKIYVMDKGRIIEE 697
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVyISHRLKEIfEICDDVTVFRDGQFIAE 222
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
197-464 |
3.22e-13 |
|
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: 71.33 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 197 PNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFF--GTRKVGEIISRF-NDGDK 273
Cdd:cd18578 44 DDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLsTDASD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 274 IRNAISSvTLTLMIDVLMAVVGGAIL-YLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEG 352
Cdd:cd18578 124 VRGLVGD-RLGLILQAIVTLVAGLIIaFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSN 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 353 IETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVqgtlmdtisgGFGI----------CLLWFGGSLVLKGEVTIGE 422
Cdd:cd18578 203 IRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL----------GFGLsqsltffayaLAFWYGGRLVANGEYTFEQ 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 336293682 423 -LISFNALLayF-IQPIGRLINLQPQLQEAIVASDRLGEILDLE 464
Cdd:cd18578 273 fFIVFMALI--FgAQSAGQAFSFAPDIAKAKAAAARIFRLLDRK 314
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
484-652 |
5.15e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 72.23 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 484 LENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddidKETLRSKISYISQ 563
Cdd:PRK15064 322 VENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 564 DSFFfsgtikenlEFVGDDVTYEKMVDACKKAHIHEYIESL---PLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:PRK15064 390 DHAY---------DFENDLTLFDWMSQWRQEGDDEQAVRGTlgrLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
170
....*....|....
gi 336293682 641 IMDEATSNLD--SI 652
Cdd:PRK15064 461 VMDEPTNHMDmeSI 474
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
483-717 |
5.78e-13 |
|
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: 71.89 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGfykIDQgkiilnnyyidDIDKETLRS---KIS 559
Cdd:TIGR03719 6 TMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDK-----------DFNGEARPQpgiKVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQDSFF-FSGTIKENLEF-VGD--------DVTYEKMVD--------ACKKAHIHEYIES------------------ 603
Cdd:TIGR03719 72 YLPQEPQLdPTKTVRENVEEgVAEikdaldrfNEISAKYAEpdadfdklAAEQAELQEIIDAadawdldsqleiamdalr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 604 LPlkyktPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTEnvTTIVIAH-Rlstikk 682
Cdd:TIGR03719 152 CP-----PWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG--TVVAVTHdR------ 218
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 336293682 683 cqkiYVMDK--GRIIEegshrelLDKGGYY-----YRLWTEQ 717
Cdd:TIGR03719 219 ----YFLDNvaGWILE-------LDRGRGIpwegnYSSWLEQ 249
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
501-704 |
5.86e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 70.60 E-value: 5.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 501 INISIHNGEKIALVGESGSGKTTIAKLLMGFYKiDQGKIILNNYYIDDID--KETLRSKISYISQD-SFFF--------- 568
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRMRFDDIDllRLSPRERRKLVGHNvSMIFqepqscldp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 569 SGTIKENLEFVGDDVTYE----KMVDACKKAHIhEYIESLPLK-YKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMD 643
Cdd:PRK15093 105 SERVGRQLMQNIPGWTYKgrwwQRFGWRKRRAI-ELLHRVGIKdHKDAMRSFPYELTEGECQKVMIAIALANQPRLLIAD 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 644 EATSNLDSITERAIQRTLEECTEN--VTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK15093 184 EPTNAMEPTTQAQIFRLLTRLNQNnnTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
501-703 |
6.39e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 6.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 501 INISIHNGEKIALVGESGSGKTTIAKLLMGFykID-QGKIILNNYYIDDIDKETLRSK---------ISYISQD------ 564
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDyPGRVMAEKLEFNGQDLQRISEKerrnlvgaeVAMIFQDpmtsln 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 565 -SFFFSGTIKENLEfvgddvTYEkmvDACKKAHIHEYIESLPL----KYKTPLEEKGSNLSGGQRQRLSIARALLKKPEI 639
Cdd:PRK11022 104 pCYTVGFQIMEAIK------VHQ---GGNKKTRRQRAIDLLNQvgipDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 640 LIMDEATSNLD-SITERAIQRTLE-ECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK11022 175 LIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
498-695 |
8.60e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.30 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYID-DIDKETLRSKISYISQD-SFFFSGTIKEN 575
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 L-----EFVGDDVTYEKMVDACKKAHIHEYIESLPlkyktplEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSnld 650
Cdd:PRK10982 94 MwlgryPTKGMFVDQDKMYRDTKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS--- 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 336293682 651 SITER------AIQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRII 695
Cdd:PRK10982 164 SLTEKevnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
497-709 |
8.85e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.90 E-value: 8.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGF--YKIDQGKIILNNYYIDDIDKEtLRSK----------------- 557
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHlgiflafqypieipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ------ISYISQ---------DSFFFSGTIKENLEFVGDDVTYekmvdackkahIHEYIEslplkyktpleekgSNLSGG 622
Cdd:CHL00131 101 nadflrLAYNSKrkfqglpelDPLEFLEIINEKLKLVGMDPSF-----------LSRNVN--------------EGFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 623 QRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEE-CTENVTTIVIAH--RLSTIKKCQKIYVMDKGRIIEEGS 699
Cdd:CHL00131 156 EKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
250
....*....|..
gi 336293682 700 HR--ELLDKGGY 709
Cdd:CHL00131 236 AElaKELEKKGY 247
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
497-650 |
1.08e-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: 67.52 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYiDDIDKETLRSKISYIS-QDSFFFSGTIKEN 575
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP-LDFQRDSIARGLLYLGhAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 576 LEFVGDDVTYEKMVDACKKAHIHEYiESLPLKYktpleekgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
498-650 |
1.22e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID-KETLRSKISYISQD----SFFFSGTI 572
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDrkrdGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 573 KENLEFVGDDVTYEKMVD---ACKKAHIHEYIESLPLKykTP-LEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSN 648
Cdd:PRK10762 348 KENMSLTALRYFSRAGGSlkhADEQQAVSDFIRLFNIK--TPsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
..
gi 336293682 649 LD 650
Cdd:PRK10762 426 VD 427
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
490-675 |
2.46e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.10 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 490 AYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddidKETLRSKISYISQDSfffs 569
Cdd:NF040873 1 GYGGRP-VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRS---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 570 gTIKENLEF-VGDDVT--------YEKMVDACKKAHIHEYIESLPLK--YKTPLEEkgsnLSGGQRQRLSIARALLKKPE 638
Cdd:NF040873 65 -EVPDSLPLtVRDLVAmgrwarrgLWRRLTRDDRAAVDDALERVGLAdlAGRQLGE----LSGGQRQRALLAQGLAQEAD 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 336293682 639 ILIMDEATSNLDSITERAIQRTL-EECTENVTTIVIAH 675
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTH 177
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
499-703 |
2.62e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.32 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 499 NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDI-DKETLRSKISYISQD-SFFFSGTIKENL 576
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpGHQIARMGVVRTFQHvRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 577 efvgddvtyekMVdackKAHIHEYIESLPLKYKTP----------------LEEKG---------SNLSGGQRQRLSIAR 631
Cdd:PRK11300 102 -----------LV----AQHQQLKTGLFSGLLKTPafrraesealdraatwLERVGllehanrqaGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 632 ALLKKPEILIMDEATSNLDSITERAIQRTLEECTE--NVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHREL 703
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
500-694 |
3.53e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 500 DINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID-KETLRSKISYISQD----SFFFSGTIKE 574
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDrqssGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 575 NLEfvgdDVTYEKM---VDACKKAHIHE-YIESLPLKYkTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:PRK15439 361 NVC----ALTHNRRgfwIKPARENAVLErYRRALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 336293682 651 sITERA-IQRTLEECTE-NVTTIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:PRK15439 436 -VSARNdIYQLIRSIAAqNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
498-692 |
4.33e-12 |
|
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: 65.34 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGfYKID---QGKIILNNYYIDdidkETLRSKISYISQ-DSFFFSGTIK 573
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-RKTAgviTGEILINGRPLD----KNFQRSTGYVEQqDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 574 ENLEFvgddvtyekmvDACKKAhiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLDSIT 653
Cdd:cd03232 98 EALRF-----------SALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 336293682 654 ERAIQRTLEECTENVTTIVIA-HRLS--TIKKCQKIYVMDKG 692
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTiHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
499-703 |
4.40e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 499 NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETlRSKISYISQdSFFFSG--TIKENL 576
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT-RRRVGYMSQ-AFSLYGelTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 577 EF------VGDDVTYEKMVDACKKAHIHEYIESLPlkyktpleekgSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:NF033858 361 ELharlfhLPAAEIAARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 651 SITERAIQRTLEE--CTENVTTIVIAHRLSTIKKCQKIYVMDKGRIIEEGSHREL 703
Cdd:NF033858 430 PVARDMFWRLLIElsREDGVTIFISTHFMNEAERCDRISLMHAGRVLASDTPAAL 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
508-679 |
4.64e-12 |
|
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: 69.04 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 508 GEKIALVGESGSGKTTIAKLLMGFYKIDQGKI--------ILNNY-------YIDDIDKETLRS--KISYISQDSFFFSG 570
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKRFrgtelqdYFKKLANGEIKVahKPQYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 TIKENLEFVGDdvtyEKMVDackkahihEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:COG1245 179 TVRELLEKVDE----RGKLD--------ELAEKLGLENI--LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|....
gi 336293682 651 sITER-----AIQRTLEectENVTTIVIAHRLST 679
Cdd:COG1245 245 -IYQRlnvarLIRELAE---EGKYVLVVEHDLAI 274
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
194-426 |
4.67e-12 |
|
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: 67.27 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 194 DILPNNLKAS-------LHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIIS 266
Cdd:cd18780 24 DAVTNHSGSGgeealraLNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 267 RFNDGDKIRNAISSVTLTLMIDVLMAVVGG-AILYLQNLKLFFTCF--VPIVLYLILVFGfkNKLKKVNRRVMEDNASLT 343
Cdd:cd18780 104 RLSSDTQVLQNAVTVNLSMLLRYLVQIIGGlVFMFTTSWKLTLVMLsvVPPLSIGAVIYG--KYVRKLSKKFQDALAAAS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 344 SYLVESLEGIETVKAFNGEglvrLKTENKFLKFMKSYFKHGYTYN-VQGTLMDTISGGFGICL---LWFGGSLVLKGEVT 419
Cdd:cd18780 182 TVAEESISNIRTVRSFAKE----TKEVSRYSEKINESYLLGKKLArASGGFNGFMGAAAQLAIvlvLWYGGRLVIDGELT 257
|
....*..
gi 336293682 420 IGELISF 426
Cdd:cd18780 258 TGLLTSF 264
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
470-704 |
5.32e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 5.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 470 DESIKPETlagCISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDI 549
Cdd:PRK10575 3 EYTNHSDT---TFALRNVSFRVPGR-TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 550 DKETLRSKISYISQDSFFFSG-TIKEnLEFVGDDVTYEKM--VDACKKAHIHEYIESLPLKyktPLEEK-GSNLSGGQRQ 625
Cdd:PRK10575 79 SSKAFARKVAYLPQQLPAAEGmTVRE-LVAIGRYPWHGALgrFGAADREKVEEAISLVGLK---PLAHRlVDSLSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDsITERA-----IQRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGS 699
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALD-IAHQVdvlalVHRLSQE--RGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGT 231
|
....*
gi 336293682 700 HRELL 704
Cdd:PRK10575 232 PAELM 236
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
497-704 |
9.32e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLL------MGFYKIdQGKIILNNYYIDDI-DKETLRSKISYISQDSFFFS 569
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRY-SGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 570 GTIKENL--EFVGDDVTYEKMVDACKKAHIHEYieSLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATS 647
Cdd:PRK14271 115 MSIMDNVlaGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 648 NLDSITERAIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
497-708 |
1.00e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.60 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLL-----MGFykIDQGKIILNNYYIDdidkETLRSKISYISQ-DSFFFSG 570
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGV--ITGGDRLVNGRPLD----SSFQRSIGYVQQqDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 TIKENLEFVG-----DDVT-YEKMvdackkAHIHEYIESLPL-KYKTPL-EEKGSNLSGGQRQRLSIARALLKKPEILI- 641
Cdd:TIGR00956 852 TVRESLRFSAylrqpKSVSkSEKM------EYVEEVIKLLEMeSYADAVvGVPGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 642 MDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLSTIkkcqkiyvmdkgrIIEEGSHRELLDKGG 708
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLADHGQAILCTiHQPSAI-------------LFEEFDRLLLLQKGG 980
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
174-436 |
1.18e-11 |
|
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: 66.09 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 174 SILVTILG----IAGSFYYEFLIDDiLPNNLKASLHSISIAMLILLLFKIVTEFF---RKTLLLYMAQNIDVPLLLGYYN 246
Cdd:cd18560 1 SLLLLILGkacnVLAPLFLGRAVNA-LTLAKVKDLESAVTLILLYALLRFSSKLLkelRSLLYRRVQQNAYRELSLKTFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 247 HVVKLPMNFFGTRKVGEIISRFNDG-DKIRNAISSVTLTL---MIDVLMAVVGGAILYlqNLKLFFTCFVPIVLYLILVF 322
Cdd:cd18560 80 HLHSLSLDWHLSKKTGEVVRIMDRGtESANTLLSYLVFYLvptLLELIVVSVVFAFHF--GAWLALIVFLSVLLYGVFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 323 GFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGEglvrlKTE-NKFLKFMKSYFKhgYTYNVQGTL-------M 394
Cdd:cd18560 158 KVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNE-----KYEvDRYGEAVKEYQK--SSVKVQASLsllnvgqQ 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 336293682 395 DTISGGFGIClLWFGGSLVLKGEVTIGELISFNALLAYFIQP 436
Cdd:cd18560 231 LIIQLGLTLG-LLLAGYRVVDGGLSVGDFVAVNTYIFQLFQP 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
508-677 |
1.18e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 508 GEKIALVGESGSGKTTIAKLLMGFYKIDQGKI--------ILNNY-------YIDDIDKETLRS--KISYISQDSFFFSG 570
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKRFrgtelqnYFKKLYNGEIKVvhKPQYVDLIPKVFKG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 TIKENLefvgddvtyeKMVDACKKahIHEYIESLPLKykTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:PRK13409 179 KVRELL----------KKVDERGK--LDEVVERLGLE--NILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*...
gi 336293682 651 sITER-AIQRTLEECTENVTTIVIAHRL 677
Cdd:PRK13409 245 -IRQRlNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
482-705 |
1.46e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.38 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddiDKETLRSK---- 557
Cdd:PRK15439 12 LCARSISKQYSGV-EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG-------GNPCARLTpaka 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 558 ----ISYISQDSFFFSG-TIKENLEF--VGDDVTYEKMVDACKKAHIHeyieslpLKyktpLEEKGSNLSGGQRQRLSIA 630
Cdd:PRK15439 84 hqlgIYLVPQEPLLFPNlSVKENILFglPKRQASMQKMKQLLAALGCQ-------LD----LDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 631 RALLKKPEILIMDEATSNLDSI-TERAIQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLD 705
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLST 229
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
482-650 |
1.50e-11 |
|
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: 63.92 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSkISYI 561
Cdd:TIGR01189 1 LAARNLACSRGERM-LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN-ILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 S-QDSFFFSGTIKENLEFVGDDVTYEKMV--DACKKAHIHEYiESLPLKYktpleekgsnLSGGQRQRLSIARALLKKPE 638
Cdd:TIGR01189 79 GhLPGLKPELSALENLHFWAAIHGGAQRTieDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRP 147
|
170
....*....|..
gi 336293682 639 ILIMDEATSNLD 650
Cdd:TIGR01189 148 LWILDEPTTALD 159
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
497-702 |
2.83e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID--QGKIILNNyyiDDIDKETLRsKISYISQDSFFFSG-TIK 573
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANN---RKPTKQILK-RTGFVTQDDILYPHlTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 574 ENLEF-----------------VGDDVTYEKMVDACKKAHI-HEYIESLplkyktpleekgsnlSGGQRQRLSIARALLK 635
Cdd:PLN03211 159 ETLVFcsllrlpksltkqekilVAESVISELGLTKCENTIIgNSFIRGI---------------SGGERKRVSIAHEMLI 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 636 KPEILIMDEATSNLDSITERAIQRTLEECTENVTTIVIA-HRLST--IKKCQKIYVMDKGRIIEEGSHRE 702
Cdd:PLN03211 224 NPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
452-681 |
3.52e-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: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 452 VASDRLGEILDLELEKSDDESIKPETLAGC---------ISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKT 522
Cdd:TIGR00954 413 VKSGNFKRPRVEEIESGREGGRNSNLVPGRgiveyqdngIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKS 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 523 TIAKLLMGFYKIDQGKIilnnyYIDDidketlRSKISYISQDSFFFSGTIKenlefvgDDVTYEKMVDACKK-----AHI 597
Cdd:TIGR00954 493 SLFRILGELWPVYGGRL-----TKPA------KGKLFYVPQRPYMTLGTLR-------DQIIYPDSSEDMKRrglsdKDL 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 598 HEYIESLPLKYKtpLEEKGS---------NLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEEctENV 668
Cdd:TIGR00954 555 EQILDNVQLTHI--LEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGI 630
|
250
....*....|...
gi 336293682 669 TTIVIAHRLSTIK 681
Cdd:TIGR00954 631 TLFSVSHRKSLWK 643
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
481-697 |
3.94e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 481 CISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNyyiDDID----KETLRS 556
Cdd:COG3845 257 VLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG---EDITglspRERRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 557 KISYISQD--------SFffsgTIKENLeFVG--DDVTYEK--MVDacKKAhIHEYIESLPLKY--KTP-LEEKGSNLSG 621
Cdd:COG3845 334 GVAYIPEDrlgrglvpDM----SVAENL-ILGryRRPPFSRggFLD--RKA-IRAFAEELIEEFdvRTPgPDTPARSLSG 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 622 GQRQRLSIARALLKKPEILIMDEATSNLDsitERAI----QRTLEECTENVTTIVI----------AHRlstikkcqkIY 687
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLD---VGAIefihQRLLELRDAGAAVLLIsedldeilalSDR---------IA 473
|
250
....*....|
gi 336293682 688 VMDKGRIIEE 697
Cdd:COG3845 474 VMYEGRIVGE 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
483-650 |
6.32e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 6.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 483 SLENVSFAYGMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGfykIDQgkiilnnyyidDIDKETLRS---KIS 559
Cdd:PRK11819 8 TMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG---VDK-----------EFEGEARPApgiKVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 560 YISQ----DSfffSGTIKENLEF-VGD--------DVTYEKMVD--------ACKKAHIHEYIES--------------- 603
Cdd:PRK11819 74 YLPQepqlDP---EKTVRENVEEgVAEvkaaldrfNEIYAAYAEpdadfdalAAEQGELQEIIDAadawdldsqleiamd 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 336293682 604 ---LPlkyktPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:PRK11819 151 alrCP-----PWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
482-650 |
1.99e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDN-VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIIlnnyYIDDIdketlrsKISY 560
Cdd:PRK11147 4 ISIHGAWLSFS--DApLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII----YEQDL-------IVAR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDS--------F-FFSGTIKENLEF----------VGDDVTyEKMVDACKKAH--------------IHEYIESLPLK 607
Cdd:PRK11147 71 LQQDPprnvegtvYdFVAEGIEEQAEYlkryhdishlVETDPS-EKNLNELAKLQeqldhhnlwqlenrINEVLAQLGLD 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 336293682 608 YKTPLeekgSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:PRK11147 150 PDAAL----SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
482-679 |
2.34e-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: 63.80 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDNVL-NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddidkETLrsKISY 560
Cdd:TIGR03719 323 IEAENLTKAFG--DKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG---------ETV--KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQ--DSFFFSGTIKENLEfVGDDV----TYEKMVDAckkahiheYIESLPLKyKTPLEEKGSNLSGGQRQRLSIARALL 634
Cdd:TIGR03719 390 VDQsrDALDPNKTVWEEIS-GGLDIiklgKREIPSRA--------YVGRFNFK-GSDQQKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 336293682 635 KKPEILIMDEATSNLDSITERAiqrtLEECTENV--TTIVIAH------RLST 679
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRA----LEEALLNFagCAVVISHdrwfldRIAT 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
498-696 |
3.35e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDID-KETLRSKISYISQDSFFFSG-TIKEN 575
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQELHLVPEmTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 LeFVGDDVTYEKMVDACK-KAHIHEYIESLPLKY--KTPLEEkgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLDSI 652
Cdd:PRK11288 100 L-YLGQLPHKGGIVNRRLlNYEAREQLEHLGVDIdpDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAR 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 336293682 653 -TER--AIQRTLEEctENVTTIVIAHRLSTI-KKCQKIYVMDKGRIIE 696
Cdd:PRK11288 175 eIEQlfRVIRELRA--EGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
171-435 |
4.78e-10 |
|
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: 61.26 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 171 FIASILVTILGIAGS----FYYEFLIDDILPNNLKASLHSISIAMLIL----LLFKIVTEFFRKTLLLYMAQNI--DVpl 240
Cdd:cd18548 1 AILAPLFKLLEVLLElllpTLMADIIDEGIANGDLSYILRTGLLMLLLallgLIAGILAGYFAAKASQGFGRDLrkDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 241 llgyYNHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSvTLTLMIDVLMAVVGGAIL-YLQNLKL--FFTCFVPI-- 314
Cdd:cd18548 79 ----FEKIQSFSFAEIDKFGTSSLITRLtNDVTQVQNFVMM-LLRMLVRAPIMLIGAIIMaFRINPKLalILLVAIPIla 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 315 -VLYLILVFGFK------NKLKKVNRRVMEdnasltsylveSLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTY 387
Cdd:cd18548 154 lVVFLIMKKAIPlfkkvqKKLDRLNRVVRE-----------NLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLM 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 336293682 388 NVQGTLMDTISGGFGICLLWFGGSLVLKGEVTIGELISFnalLAYFIQ 435
Cdd:cd18548 223 ALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAF---INYLMQ 267
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
508-680 |
8.09e-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: 57.77 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 508 GEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILnnyyiddIDKETLRSkisyisqdsfffsgtikenlefvgddvtyek 587
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILE------------------------------- 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 588 mvdackkahiheyiESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECT-- 665
Cdd:smart00382 44 --------------EVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
|
170 180
....*....|....*....|
gi 336293682 666 -----ENVTTIVIAHRLSTI 680
Cdd:smart00382 110 llkseKNLTVILTTNDEKDL 129
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
485-704 |
8.67e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.00 E-value: 8.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 485 ENVSFAYGmRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQD 564
Cdd:PRK10253 11 EQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 565 SFffsgtikenlefVGDDVTYEKMV-------------------DACKKAHIHEYIESLPLkyktpleEKGSNLSGGQRQ 625
Cdd:PRK10253 90 AT------------TPGDITVQELVargryphqplftrwrkedeEAVTKAMQATGITHLAD-------QSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEEC--TENVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHRE 702
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKE 230
|
..
gi 336293682 703 LL 704
Cdd:PRK10253 231 IV 232
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
202-457 |
9.24e-10 |
|
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: 60.56 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 202 ASLHSIsIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISS 280
Cdd:cd18589 34 AFTAAI-TVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTtDTEDMSESLSE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 281 vTLTLMIDVLMAVVGgAILYLQNLKLFFTCFVPIVLYLILVFG-FKNKLKK-VNRRVMEDNASLTSYLVESLEGIETVKA 358
Cdd:cd18589 113 -NLSLLMWYLARGLF-LFIFMLWLSPKLALLTALGLPLLLLVPkFVGKFQQsLAVQVQKSLARANQVAVETFSAMKTVRS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 359 F-NGEGlvrlKTENKFLKFMKSYF---KHGYTYNVQgTLMDTISG-GFGICLLWFGGSLVLKGEVTIGELISFNALLAYF 433
Cdd:cd18589 191 FaNEEG----EAQRYRQRLQKTYRlnkKEAAAYAVS-MWTSSFSGlALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQF 265
|
250 260
....*....|....*....|....
gi 336293682 434 IQPIGRLINLQPQLQEAIVASDRL 457
Cdd:cd18589 266 TSAVEVLLSYYPSVMKAVGSSEKI 289
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
10-136 |
1.02e-09 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family, which contains Colicin V perocessing peptidase.
Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 56.96 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 10 VKQHDIQDCGPACLATISKQ-YGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEEIFNNLPTPLIah 88
Cdd:cd02424 4 IKQTDLNDCGIAVIQMLYNHyYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFLELKNKFIIL-- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 336293682 89 vIIDDVLLHFVVVHKITKKYILIADPGRGMIKYKPDEFFKIWSDVLIF 136
Cdd:cd02424 82 -LKSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIIT 128
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
508-704 |
1.41e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 508 GEKIALVGESGSGKTT----IAKLLMGfykidQGKIILNNYYIDDIDKETLRSKISYISQ-DSFFFSGTIKENLEFVGDD 582
Cdd:PRK03695 22 GEILHLVGPNGAGKSTllarMAGLLPG-----SGSIQFAGQPLEAWSAAELARHRAYLSQqQTPPFAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 583 vtyeKMVDACKKAHIHEYIESLPLKYKtpLEEKGSNLSGGQRQRLSIARALLK-KPEI------LIMDEATSNLDSITER 655
Cdd:PRK03695 97 ----KTRTEAVASALNEVAEALGLDDK--LGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 336293682 656 AIQRTLEE-CTENVTTIVIAHRLS-TIKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK03695 171 ALDRLLSElCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
508-678 |
1.42e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 508 GEKIALVGESGSGKTTIAKLLMGFYKIDQGKI--------ILNNY-------YIDDIDKETLRS--KISYISQDSFFFSG 570
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFrgselqnYFTKLLEGDVKVivKPQYVDLIPKAVKG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 571 TIKENLEFVGDDVTYEKMVDACKKAHIheyieslplkyktpLEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:cd03236 106 KVGELLKKKDERGKLDELVDQLELRHV--------------LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|.
gi 336293682 651 ---SITERAIQRTLEECTENVttIVIAHRLS 678
Cdd:cd03236 172 ikqRLNAARLIRELAEDDNYV--LVVEHDLA 200
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
174-455 |
1.46e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 59.60 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 174 SILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPM 253
Cdd:cd18561 5 GLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 254 NFFGTRKVGEIISRFNDG-DKIRNAISSVTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVN 332
Cdd:cd18561 85 GYLEGERTGELQTTVVDGvEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 333 RRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGICLLWFGGSL 412
Cdd:cd18561 165 RRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 336293682 413 VLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASD 455
Cdd:cd18561 245 VLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAAD 287
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
497-694 |
2.59e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.33 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYK-IDQGKIILNNYYIdDIDK--ETLRSKISYISQD----SFFFS 569
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPV-KIRNpqQAIAQGIAMVPEDrkrdGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 570 GTIKENLEF-VGDDVTYEKMVDACKK-AHIHEYIESLPLKYKTPlEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATS 647
Cdd:PRK13549 356 MGVGKNITLaALDRFTGGSRIDDAAElKTILESIQRLKVKTASP-ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 336293682 648 NLDSITERAIQRTLEE-CTENVTTIVIAHRLSTI-KKCQKIYVMDKGRI 694
Cdd:PRK13549 435 GIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
482-703 |
2.73e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAY---GMRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYK-----IDQGKIIL---NNYYID--- 547
Cdd:PRK10261 13 LAVENLNIAFmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglVQCDKMLLrrrSRQVIElse 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 548 --DIDKETLR-SKISYISQDS-------FFFSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESlplkyKTPLEEKGS 617
Cdd:PRK10261 93 qsAAQMRHVRgADMAMIFQEPmtslnpvFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA-----QTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 618 NLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEECTENVT--TIVIAHRLSTIKK-CQKIYVMDKGRI 694
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEA 247
|
....*....
gi 336293682 695 IEEGSHREL 703
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
498-699 |
2.74e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 60.80 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDdIDKETLRSKISYISQDSFFFSG-TIKENL 576
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHlTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 577 EFVGD--DVTYEKmvdacKKAHIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITE 654
Cdd:TIGR01257 1025 LFYAQlkGRSWEE-----AQLEMEAMLEDTGLHHKR--NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 336293682 655 RAIQRTLEECTENVTTIVIAHRLSTIKKC-QKIYVMDKGRIIEEGS 699
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSGT 1143
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
498-694 |
3.01e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID-QGKIILNNYYIDDID-KETLRSKISYISQDSFFfSGTIKEn 575
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKR-HGIVPI- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 lEFVGDDVTYEKMVDACKKAHIHEY---------IESLPLKYKTPLEEKGSnLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:TIGR02633 354 -LGVGKNITLSVLKSFCFKMRIDAAaelqiigsaIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 336293682 647 SNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTI-KKCQKIYVMDKGRI 694
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVlGLSDRVLVIGEGKL 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
491-698 |
1.03e-08 |
|
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: 55.41 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 491 YGMRDNVLNDINISIHNGEKIALVGESGSGKTTIakLLMGFYKIDQGKII--LNNYYiddidketlRSKISYISQDSFFf 568
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKARLIsfLPKFS---------RNKLIFIDQLQFL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 569 sgtIKENLEFVgddvtyekmvdackkahiheyieslplkyktPLEEKGSNLSGGQRQRLSIARALLKKPE--ILIMDEAT 646
Cdd:cd03238 72 ---IDVGLGYL-------------------------------TLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPS 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 647 SNLDSITERAIQRTLEEC-TENVTTIVIAHRLSTIKKCQKIYVMDK------GRIIEEG 698
Cdd:cd03238 118 TGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
499-702 |
1.16e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.26 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 499 NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDK-ETLRSKISYISQ----DSFFFSGTIK 573
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrdNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 574 ENLEF------------VG--DDVTYEKMVDACKkahiheyiESLPLKYKTpLEEKGSNLSGGQRQRLSIARALLKKPEI 639
Cdd:PRK09700 360 QNMAIsrslkdggykgaMGlfHEVDEQRTAENQR--------ELLALKCHS-VNQNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 336293682 640 LIMDEATSNLDSITERAI---QRTLEEctENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRE 702
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIykvMRQLAD--DGKVILMVSSELPEIITvCDRIAVFCEGRLTQILTNRD 495
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
203-426 |
1.38e-08 |
|
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: 56.78 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 203 SLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRFNdGD--------K- 273
Cdd:cd18574 40 DLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLT-ADvqefkssfKq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 274 -IRNAISSVTLTlmidvlmavVGGAI-LYL--QNLKLFFTCFVPIVlYLILVFgFKNKLKKVNRRVMEDNASLTSYLVES 349
Cdd:cd18574 119 cVSQGLRSVTQT---------VGCVVsLYLisPKLTLLLLVIVPVV-VLVGTL-YGSFLRKLSRRAQAQVAKATGVADEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 350 LEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNV-QGtLMDTISGGFGICLLWFGGSLVLKGEVTIGELISF 426
Cdd:cd18574 188 LGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIfQG-LSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSF 264
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
474-650 |
1.55e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.87 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 474 KPETLAG-CISLENVSFAYGMRdNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYiddidke 552
Cdd:PRK10636 304 APESLPNpLLKMEKVSAGYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGI------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 553 tlrsKISYISQdsfffsgtikENLEFV-GDDVTYEKMVDACKKA---HIHEYIESLPLKYKTPLEEKGsNLSGGQRQRLS 628
Cdd:PRK10636 376 ----KLGYFAQ----------HQLEFLrADESPLQHLARLAPQEleqKLRDYLGGFGFQGDKVTEETR-RFSGGEKARLV 440
|
170 180
....*....|....*....|..
gi 336293682 629 IARALLKKPEILIMDEATSNLD 650
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLD 462
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
498-708 |
1.90e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID--QGKIILnnyyiddiDKETLRSK---------ISYISQD-- 564
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILF--------DGEVCRFKdirdsealgIVIIHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 565 -SFFFSgtIKENLeFVGD----------DVTYEKMVDACKKAHIHEyieslplkyktPLEEKGSNLSGGQRQRLSIARAL 633
Cdd:NF040905 89 lIPYLS--IAENI-FLGNerakrgvidwNETNRRARELLAKVGLDE-----------SPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 336293682 634 LKKPEILIMDEATSNL-DSITERAIQRTLEECTENVTTIVIAHRLSTIKKcqkiyVMDKGRIIEEGSHRELLDKGG 708
Cdd:NF040905 155 SKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRR-----VADSITVLRDGRTIETLDCRA 225
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
170-435 |
1.98e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 56.36 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 170 IFIASILVTILGIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLYMAQNIDVPLLLGYYNHVV 249
Cdd:cd18580 4 LLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 250 KLPMNFFGTRKVGEIISRF-NDGDKIRNAISSvTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFknkL 328
Cdd:cd18580 84 RAPMSFFDTTPSGRILNRFsKDIGLIDEELPL-ALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRY---Y 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 329 KKVNRRV----MEDNASLTSYLVESLEGIETVKAFNGEGlvRLKTENKFL--KFMKSYFkhgYTYNVQ---GTLMDTISG 399
Cdd:cd18580 160 LRTSRQLrrleSESRSPLYSHFSETLSGLSTIRAFGWQE--RFIEENLRLldASQRAFY---LLLAVQrwlGLRLDLLGA 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 336293682 400 GFGICLLWFggSLVLKGEVTIGEL-------ISFNALLAYFIQ 435
Cdd:cd18580 235 LLALVVALL--AVLLRSSISAGLVglaltyaLSLTGSLQWLVR 275
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
596-709 |
3.84e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 57.15 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 596 HIHEYIE---SLPLKYkTPLEEKGSNLSGGQRQRLSIARALL---KKPEILIMDEATSNLDSITERAIQRTLEECT-ENV 668
Cdd:PRK00635 785 SIHEKIHalcSLGLDY-LPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGH 863
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 336293682 669 TTIVIAHRLSTIKKCQkiYVMDKGriiEEGShrellDKGGY 709
Cdd:PRK00635 864 TVVIIEHNMHVVKVAD--YVLELG---PEGG-----NLGGY 894
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
187-426 |
4.09e-08 |
|
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: 55.39 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 187 YYEFL-IDDILpnnLKASLHSISIAMLILLLFKIVTEFF---RKTLL-LYMAQ-NIDVPLLLgyYNHVVKLPMNFFGTRK 260
Cdd:cd18784 17 YYTGQvIDGIV---IEKSQDKFSRAIIIMGLLAIASSVAagiRGGLFtLAMARlNIRIRNLL--FRSIVSQEIGFFDTVK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 261 VGEIISRFN-DGDKIrnaisSVTLTLMIDVL---MAVVGGAILYLQNL--KLFFTCFV--PIVLYLILVFGfkNKLKKVN 332
Cdd:cd18784 92 TGDITSRLTsDTTTM-----SDTVSLNLNIFlrsLVKAIGVIVFMFKLswQLSLVTLIglPLIAIVSKVYG--DYYKKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 333 RRVMEDNASLTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHG--YTYNVQGTLMdtISGGFGICLLWFGG 410
Cdd:cd18784 165 KAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEAlaYGGYVWSNEL--TELALTVSTLYYGG 242
|
250
....*....|....*.
gi 336293682 411 SLVLKGEVTIGELISF 426
Cdd:cd18784 243 HLVITGQISGGNLISF 258
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
500-703 |
4.73e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 4.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 500 DINISIHNGEKIALVGESGSGKT-TIAKLL----MGFYKIdQGKIILNNyyiDDIDKETLRSK-ISYISQD--SFF---- 567
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpAGVRQT-AGRVLLDG---KPVAPCALRGRkIATIMQNprSAFnplh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 -FSGTIKENLEFVGDDVTYEKMVDACKKAHIHEYIESLPLKyktPLEekgsnLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:PRK10418 97 tMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLY---PFE-----MSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 647 SNLDSITERAIQRTLEEC--TENVTTIVIAHRLSTIKKC-QKIYVMDKGRIIEEGSHREL 703
Cdd:PRK10418 169 TDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGDVETL 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
447-650 |
5.05e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 447 LQEAIVASDRLGEI--------LDLELEKSDDESIKPetlagCISLENVSFAYGMRDNVLNDINISIHNGEKIALVGESG 518
Cdd:PLN03073 471 VQSRIKALDRLGHVdavvndpdYKFEFPTPDDRPGPP-----IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNG 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 519 SGKTTIAKLLMGFYKIDQGKI---------ILNNYYIDDIDKETlrSKISYISQdsfFFSGTIKENLefvgddvtyekmv 589
Cdd:PLN03073 546 IGKSTILKLISGELQPSSGTVfrsakvrmaVFSQHHVDGLDLSS--NPLLYMMR---CFPGVPEQKL------------- 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 590 dackKAHIHEY--IESLPLKyktPLeekgSNLSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:PLN03073 608 ----RAHLGSFgvTGNLALQ---PM----YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
482-650 |
6.42e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.02 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRDnVLNDINISIHNGEKIALVGESGSGKTTIAKLlMGFYKIDQgkiILNNYYIDDIDKETLRSKISYI 561
Cdd:PLN03073 178 IHMENFSISVGGRD-LIVDASVTLAFGRHYGLVGRNGTGKTTFLRY-MAMHAIDG---IPKNCQILHVEQEVVGDDTTAL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 S-----------------------QDSFFFSGTIKENLEFVGDDvtyEKMVDACKKAHIHEYIESLP------------- 605
Cdd:PLN03073 253 QcvlntdiertqlleeeaqlvaqqRELEFETETGKGKGANKDGV---DKDAVSQRLEEIYKRLELIDaytaearaasila 329
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 336293682 606 -LKYKTPLEEKGSN-LSGGQRQRLSIARALLKKPEILIMDEATSNLD 650
Cdd:PLN03073 330 gLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
433-662 |
1.36e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 433 FIQPIGRLINL--------QPQLQEAIVASDRLGEIL-DLELEKSDDESIKPETLAGC--ISLENVSFAYGMRDnVLNDI 501
Cdd:PRK10938 201 FVQFAGVLADCtlaetgerEEILQQALVAQLAHSEQLeGVQLPEPDEPSARHALPANEprIVLNNGVVSYNDRP-ILHNL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 502 NISIHNGEKIALVGESGSGKTTIAKLLMGFYKidQGkiilnnyYIDDI--------DKETL---RSKISYISQD---SFF 567
Cdd:PRK10938 280 SWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QG-------YSNDLtlfgrrrgSGETIwdiKKHIGYVSSSlhlDYR 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGTIKeNLEFVG--DDV-TYEKMVDACKKAhIHEYIESLPL---KYKTPLEekgsNLSGGQrQRLS-IARALLKKPEIL 640
Cdd:PRK10938 351 VSTSVR-NVILSGffDSIgIYQAVSDRQQKL-AQQWLDILGIdkrTADAPFH----SLSWGQ-QRLAlIVRALVKHPTLL 423
|
250 260
....*....|....*....|..
gi 336293682 641 IMDEATSNLDSITERAIQRTLE 662
Cdd:PRK10938 424 ILDEPLQGLDPLNRQLVRRFVD 445
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
482-675 |
2.60e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGmrDNVL-NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNnyyiddidkETLrsKISY 560
Cdd:PRK11819 325 IEAENLSKSFG--DRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG---------ETV--KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 561 ISQDsfffsgtiKENLEfvGDDVTYEKMVDAckkahiHEYIEslpL-KYKTPLEE-------KGS-------NLSGGQRQ 625
Cdd:PRK11819 392 VDQS--------RDALD--PNKTVWEEISGG------LDIIK---VgNREIPSRAyvgrfnfKGGdqqkkvgVLSGGERN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 336293682 626 RLSIARALLKKPEILIMDEATSNLDSITERAiqrtLEECTENV--TTIVIAH 675
Cdd:PRK11819 453 RLHLAKTLKQGGNVLLLDEPTNDLDVETLRA----LEEALLEFpgCAVVISH 500
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-676 |
2.95e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.49 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDiDKETLRSKISYISQDSFFFSG-TIKEN 575
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGINPYlTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 ----LEFVGDDVTYEKMVDACKKAHIHEYIESLplkyktpleekgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLDs 651
Cdd:PRK13540 95 clydIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALD- 159
|
170 180
....*....|....*....|....*
gi 336293682 652 itERAIqrtleectENVTTIVIAHR 676
Cdd:PRK13540 160 --ELSL--------LTIITKIQEHR 174
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
568-708 |
3.33e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGtiKENLEFVGDDVTYEKMvDAckKAHIHEYIESLPLKYKTplEEKGSNLSGGQRQRLSIARALLKKPEILIMDEATS 647
Cdd:NF000106 101 FSG--RENLYMIGR*LDLSRK-DA--RARADELLERFSLTEAA--GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 648 NLDSITERAIQRTLEECTENVTTIVIAHRL--STIKKCQKIYVMDKGRIIEEGSHRELLDKGG 708
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
497-650 |
4.02e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIIL-NNYYIDDIDKETL---RSKISY-ISQDSFFFSGT 571
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpGNWQLAWVNQETPalpQPALEYvIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 572 IKENLEFVGDD----VTYEKMVDACKKAHIHEYIESL--PLKYKTP-LEEKGSNLSGGQRQRLSIARALLKKPEILIMDE 644
Cdd:PRK10636 96 AQLHDANERNDghaiATIHGKLDAIDAWTIRSRAASLlhGLGFSNEqLERPVSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
....*.
gi 336293682 645 ATSNLD 650
Cdd:PRK10636 176 PTNHLD 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
494-671 |
5.87e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.31 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 494 RDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFykiDQGKIILNNYYIDDIDK--ETLrSKIS-YISQ-DSFFFS 569
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGR---KTGGYIEGDIRISGFPKkqETF-ARISgYCEQnDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 570 GTIKENLEF-----VGDDVT-YEKM--VDackkaHIHEYIESLPLKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEILI 641
Cdd:PLN03140 968 VTVRESLIYsaflrLPKEVSkEEKMmfVD-----EVMELVELDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIF 1042
|
170 180 190
....*....|....*....|....*....|....
gi 336293682 642 MDEATSNLD----SITERAIQRTLEECTENVTTI 671
Cdd:PLN03140 1043 MDEPTSGLDaraaAIVMRTVRNTVDTGRTVVCTI 1076
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
498-706 |
6.45e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.36 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGkiilnnyyidDIDKETLRSKISYISQDSFFFSGTikENLE 577
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVG----------KVDRNGEVSVIAISAGLSGQLTGI--ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 578 FVGDDVTYEKMVDACKKAHIHEYIESLPLKYKtPLEekgsNLSGGQRQRLSIARALLKKPEILIMDEATSNLD-SITERA 656
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQ-PVK----KYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQKC 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 336293682 657 IQRTLEECTENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDK 706
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
498-724 |
7.80e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 7.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 498 LNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIilnnyyiddiDKETLRSKISYISQDSFFFSGTikENLE 577
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------DIKGSAALIAISSGLNGQLTGI--ENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 578 FVG--DDVTYEKMVDACKK----AHIHEYIESlPLKyktpleekgsNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS 651
Cdd:PRK13545 108 LKGlmMGLTKEKIKEIIPEiiefADIGKFIYQ-PVK----------TYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 652 ITERAIQRTLEECTENVTTI-VIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDKGGYYYRLWTEQTLDDEEQ 724
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQGKTIfFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEERKD 251
|
|
| Peptidase_C39A |
cd02549 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
18-132 |
1.13e-06 |
|
A sub-family of peptidase family C39. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is conserved in this sub-family of proteins with a single peptidase domain, which are lacking the nucleotide-binding transporter signature or have different domain architectures.
Pssm-ID: 239109 [Multi-domain] Cd Length: 141 Bit Score: 48.56 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 18 CGPACLATISKQYGLKLPISKIREAAGT-----DLEGTSVYGIVQ-AAQKLGFSTK------AVRTSKKEEIfnnlptPL 85
Cdd:cd02549 7 CGPTSLAMVLSYLGVKVTKPQLAAEGNTydfakDGYGTYPKPIVSaAARKYGLVVRpltgllALLRQLAAGH------PV 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 336293682 86 IAHVIIDDVLL---HFVVVHKIT-KKYILIADPGRGMIKYKP-DEFFKIWSD 132
Cdd:cd02549 81 IVSVNLGVSITpsgHAMVVIGYDrKGNVYVNDPGGGRRLVVSfDEFEKAWKR 132
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
497-704 |
2.15e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKID--------QGKIILNNYYIDDIDKETL---RSKISYISQDS 565
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 566 FFFSGtikENLEFVGddvTYEKMVDACKKAHIHEYI--ESLPLKYKTPLEEKG-SNLSGGQRQRLSIARALLK------- 635
Cdd:PRK13547 96 FAFSA---REIVLLG---RYPHARRAGALTHRDGEIawQALALAGATALVGRDvTTLSGGELARVQFARVLAQlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 336293682 636 --KPEILIMDEATSNLDSI-------TERAIQRtleECTENVTTIVIAHRLSTiKKCQKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK13547 170 aqPPRYLLLDEPTAALDLAhqhrlldTVRRLAR---DWNLGVLAIVHDPNLAA-RHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
493-694 |
2.54e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 493 MRDNVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDK-ETLRSKISYISQDSFffSGT 571
Cdd:PRK10982 259 LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAnEAINHGFALVTEERR--STG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 572 IKENLefvgdDVTYEKMVdackkAHIHEYIESLPL-----------------KYKTPLEEK--GSnLSGGQRQRLSIARA 632
Cdd:PRK10982 337 IYAYL-----DIGFNSLI-----SNIRNYKNKVGLldnsrmksdtqwvidsmRVKTPGHRTqiGS-LSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 633 LLKKPEILIMDEATSNLDSITERAI-QRTLEECTENVTTIVIAHRL-STIKKCQKIYVMDKGRI 694
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
497-697 |
2.86e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 497 VLNDINISIHNGEKIALVGESGSGKTTIAKLLMGF---YKIdQGKIILNNYYID--DIDkETLRSKISYISQD----SFF 567
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRsygRNI-SGTVFKDGKEVDvsTVS-DAIDAGLAYVTEDrkgyGLN 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGTIKENLEFVG-DDVTYEKMVDACKKAHIHE-YIESlpLKYKTP-LEEKGSNLSGGQRQRLSIARALLKKPEILIMDE 644
Cdd:NF040905 353 LIDDIKRNITLANlGKVSRRGVIDENEEIKVAEeYRKK--MNIKTPsVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 645 ATSNLD--------SIteraIQRTLEectENVTTIVIAHRL-STIKKCQKIYVMDKGRIIEE 697
Cdd:NF040905 431 PTRGIDvgakyeiyTI----INELAA---EGKGVIVISSELpELLGMCDRIYVMNEGRITGE 485
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
499-702 |
3.00e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 499 NDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDdidketLRSKISYIS-----------QDSFF 567
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIRagimlcpedrkAEGII 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 568 FSGTIKENLEFvgddvtyekmvdACKKAHIH---------------EYIESLplKYKTP-LEEKGSNLSGGQRQRLSIAR 631
Cdd:PRK11288 344 PVHSVADNINI------------SARRHHLRagclinnrweaenadRFIRSL--NIKTPsREQLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 336293682 632 ALLKKPEILIMDEATSNLDSITERAIQRTLEECTEN-VTTIVIAHRL-STIKKCQKIYVMDKGRIIEEGSHRE 702
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
503-711 |
3.30e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.70 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 503 ISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQG------KIILNNyyIDDIDKetlrsKISYISQ-DSFFFSGTIKEN 575
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagKSILTN--ISDVHQ-----NMGYCPQfDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 LEFvgddvtYEKM--VDACKKAHIHEY-IESLPLK-YKTPLeekGSNLSGGQRQRLSIARALLKKPEILIMDEATSNLDS 651
Cdd:TIGR01257 2033 LYL------YARLrgVPAEEIEKVANWsIQSLGLSlYADRL---AGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 652 ITERAIQRTLEECT-ENVTTIVIAHRLSTIKK-CQKIYVMDKGRIIEEGSHRELLDKGGYYY 711
Cdd:TIGR01257 2104 QARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGDGY 2165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
505-696 |
3.71e-05 |
|
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: 44.87 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 505 IHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKiilnnyyiDDIDKETLRSKISYISqdsfffsgtikenlefvgddvt 584
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN--------DEWDGITPVYKPQYID---------------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 585 yekmvdackkahiheyieslplkyktpleekgsnLSGGQRQRLSIARALLKKPEILIMDEATSNLDS----ITERAIQRT 660
Cdd:cd03222 72 ----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRL 117
|
170 180 190
....*....|....*....|....*....|....*.
gi 336293682 661 LEECTEnvTTIVIAHRLSTIKkcqkiYVMDKGRIIE 696
Cdd:cd03222 118 SEEGKK--TALVVEHDLAVLD-----YLSDRIHVFE 146
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
209-378 |
4.46e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 46.02 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 209 IAMLILLLFKIVteFFRKTLL-----LYMAqnidvplllgYYNHVVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISSVT 282
Cdd:cd18599 69 LVILLLSLIRGF--VFVKVTLrassrLHNK----------LFQKILRSPMSFFDTTPTGRILNRFSkDLDEVDVRLPFTL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 283 LTLMIDVLMAVvggaiLYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVME--DNASLT---SYLVESLEGIETVK 357
Cdd:cd18599 137 ENFLQNVLLVV-----FSLIIIAIVFPWFLIALIPLAIIFVFLSKIFRRAIRELKrlENISRSplfSHLTATIQGLSTIH 211
|
170 180
....*....|....*....|.
gi 336293682 358 AFNgeglvrlKTENKFLKFMK 378
Cdd:cd18599 212 AFN-------KEKEFLSKFKK 225
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
14-137 |
5.01e-05 |
|
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in this sub-family.
Pssm-ID: 239098 [Multi-domain] Cd Length: 121 Bit Score: 43.39 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 14 DIQDCGPACLATISKQYGLKLPISKIREAAGTDLEGTSVYGIVQAAQKLGFSTKAVRTSKKEeiFNNLPTPLIAhviIDD 93
Cdd:cd02417 3 TKPDSGLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVER--LARLPLPALA---WDD 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 336293682 94 VLLHFVVVhKITKKYILIADPGRGM-IKYKPDEFFKIWSDVLIFL 137
Cdd:cd02417 78 DGGHFILA-KLDGQKYLIQDPISQRpEVLSREEFEARWSGELILV 121
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
482-684 |
6.23e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 482 ISLENVSFAYGMRdnVLNDINISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLrskiSYI 561
Cdd:PRK13541 2 LSLHQLQFNIEQK--NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC----TYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 562 SQD-SFFFSGTIKENLEFVGDDVTYEKMVDACkkahIHEYieslplKYKTPLEEKGSNLSGGQRQRLSIARALLKKPEIL 640
Cdd:PRK13541 76 GHNlGLKLEMTVFENLKFWSEIYNSAETLYAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 336293682 641 IMDEATSNLDSiTERAIQRTLEECTENVTTIVI--AHRLSTIKKCQ 684
Cdd:PRK13541 146 LLDEVETNLSK-ENRDLLNNLIVMKANSGGIVLlsSHLESSIKSAQ 190
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
502-704 |
1.79e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.62 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 502 NISIHNGEKIALVGESGSGKTTIAKLLMGFYKIDQGKIILNNYYIDDIDKETLRSKISYISQDSfffsgtikeNLEFVGD 581
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRN---------NTDMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 582 D------VTYEKMVDACKK-AHIHEY-----IESL---PLKYktpleekgsnLSGGQRQRLSIARALLKKPEILIMDEAT 646
Cdd:PRK10938 94 GeddtgrTTAEIIQDEVKDpARCEQLaqqfgITALldrRFKY----------LSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 647 SNLDSITERAIQRTLEE-CTENVTTIVIAHRLSTIKKC-QKIYVMDKGRIIEEGSHRELL 704
Cdd:PRK10938 164 DGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDFvQFAGVLADCTLAETGEREEIL 223
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
245-435 |
2.62e-04 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350025 [Multi-domain] Cd Length: 300 Bit Score: 43.77 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 245 YNHVVKLPMNFFGTRKVGEIISRFNDG-DKIRNAISSVTLTLM---IDVLMAVvggaILYLQNLKLFF--TCFVPIVLYL 318
Cdd:cd18581 86 FAHLHSLSLRWHLSRKTGEVLRVMDRGtSSINSLLSYVLFNIGptiADIIIAI----IYFAIAFNPWFglIVFVTMALYL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 319 ILVFG---FKNKLkkvnRRVM--EDNASlTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTL 393
Cdd:cd18581 162 ILTIIiteWRTKF----RREMnkLDNEK-RAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTA 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 336293682 394 MDTI--SGGFGICLLwfGGSLVLKGEVTIGELISFnalLAYFIQ 435
Cdd:cd18581 237 QNLIitIGLLAGSLL--CAYFVVEGKLTVGDFVLF---LTYIIQ 275
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
617-675 |
3.23e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 3.23e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 617 SNLSGGQRQRLSIARALLKKPEILIMDEATSNLDSITERAIQRTLEEctENVTTIVIAH 675
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE--RNSTMIIISH 210
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
595-709 |
3.83e-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: 42.99 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 595 AHIHEYIESLP---LKYkTPLEEKGSNLSGGQRQRLSIARALLKK---PEILIMDEATSNLDSITERAIQRTLEECTEN- 667
Cdd:cd03271 144 PKIARKLQTLCdvgLGY-IKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKg 222
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 336293682 668 VTTIVIAHRLSTIKKCQkiYVMDKGriiEEGShrellDKGGY 709
Cdd:cd03271 223 NTVVVIEHNLDVIKCAD--WIIDLG---PEGG-----DGGGQ 254
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
246-360 |
6.28e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 42.46 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 246 NHVVKLPMNFFGTRKVGEIISRF-NDGDKIRNAISSvTLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGF 324
Cdd:cd18606 76 KRVLRAPMSFFDTTPLGRILNRFsKDTDVLDNELPD-SLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANY 154
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 336293682 325 --------KnKLKKVNRrvmednASLTSYLVESLEGIETVKAFN 360
Cdd:cd18606 155 yrassrelK-RLESILR------SFVYANFSESLSGLSTIRAYG 191
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
187-426 |
7.98e-04 |
|
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: 41.94 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 187 YYEFLIDDILPNnlKASLHSISIAMLILLLFKIVTEFF---RKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGE 263
Cdd:cd18590 17 YYTGRVIDILGG--EYQHNAFTSAIGLMCLFSLGSSLSaglRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 264 IISRFN-DGDKIRNAISsVTLTLMIDVLMAVVGGAILYLQ-NLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVMEDNAS 341
Cdd:cd18590 95 LTSRLStDTTLMSRSVA-LNANVLLRSLVKTLGMLGFMLSlSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 342 LTSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYFKHGYTYNVQGTLMDTISGGFGICLLWFGGSLVLKGEVTIG 421
Cdd:cd18590 174 AGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTG 253
|
....*
gi 336293682 422 ELISF 426
Cdd:cd18590 254 SLVSF 258
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
597-709 |
8.32e-04 |
|
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: 42.69 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 597 IHEYIESL---PLKYkTPLEEKGSNLSGGQRQRLSIARALLKK---PEILIMDEATSNL--DSITE--RAIQRTLEECTe 666
Cdd:TIGR00630 806 ISRKLQTLcdvGLGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfDDIKKllEVLQRLVDKGN- 883
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 336293682 667 nvTTIVIAHRLSTIKkcQKIYVMDKGriiEEGShrellDKGGY 709
Cdd:TIGR00630 884 --TVVVIEHNLDVIK--TADYIIDLG---PEGG-----DGGGT 914
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
210-362 |
2.04e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 40.77 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 210 AMLILLLFkiVTEFFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDV 289
Cdd:cd18601 66 AGLTAATF--VFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQL 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 336293682 290 LMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGFKNKLKKVNRRVMEDNAS-LTSYLVESLEGIETVKAFNGE 362
Cdd:cd18601 144 LLQVVGVVLLAVVVNPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSpVFSHLSSTLQGLWTIRAYSAQ 217
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
223-359 |
2.15e-03 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; 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: 350044 [Multi-domain] Cd Length: 324 Bit Score: 40.94 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 223 FFRKTLLLYMAQNIDVPLLLGYYNHVVKLPMNFFGTRKVGEIISRFNDGDKIRNAISSVTLTLMIDVLMAVVgGAILYLQ 302
Cdd:cd18600 88 FFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVI-GAITVVS 166
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 336293682 303 NLKLF-FTCFVP-IVLYLILVFGFKNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAF 359
Cdd:cd18600 167 ILQPYiFLATVPvIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAF 225
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
504-712 |
2.16e-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: 39.90 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 504 SIHNGEKI-------ALVGESGSGKTTIAK-LLMGFYKidqgkiilnnyyiddidkETLRSKISYISQDSFFFSGTIKEN 575
Cdd:cd03240 11 SFHERSEIeffspltLIVGQNGAGKTTIIEaLKYALTG------------------ELPPNSKGGAHDPKLIREGEVRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 576 LEFVGDDVTYEKMVdACKKAHIHEYI------ESlplkyKTPLEEKGSNLSGGQRQ------RLSIARALLKKPEILIMD 643
Cdd:cd03240 73 VKLAFENANGKKYT-ITRSLAILENVifchqgES-----NWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALD 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 336293682 644 EATSNLDSitERaIQRTLEECTE------NVTTIVIAHrlstikkcqkiyvmdkgriieegsHRELLDKGGYYYR 712
Cdd:cd03240 147 EPTTNLDE--EN-IEESLAEIIEerksqkNFQLIVITH------------------------DEELVDAADHIYR 194
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
511-558 |
3.70e-03 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 38.18 E-value: 3.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 336293682 511 IALVGESGSGKTTIAKLL--MGFYKIDQGKIILNNYYIDDIDKETLRSKI 558
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELskRLGFGDNVRDLALENGLVLGDDPETRESKR 50
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
194-381 |
5.66e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 39.44 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 194 DILPNNLKASLHSISIAMLILLLFKIVTEFFRKTLLLY----MAQNIDVPLLlgyyNHVVKLPMNFFGTRKVGEIISRFN 269
Cdd:cd18605 31 NSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYgglrAARRLHNKLL----SSILFAKMSFFDKTPVGRILNRFS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 270 DgDkirnaISSV--TLTLMIDVLMAVVGGAILYLQNLKLFFTCFVPIVLYLILVFGF-KNKLKKVNR---RVMEDNAS-L 342
Cdd:cd18605 107 S-D-----VYTIddSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRiQRYYRATSRelkRLNSVNLSpL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 336293682 343 TSYLVESLEGIETVKAFNGEGLVRLKTENKFLKFMKSYF 381
Cdd:cd18605 181 YTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQL 219
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
240-362 |
7.03e-03 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain 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.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 39.12 E-value: 7.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 240 LLLGYYNHVVKLPMNFFGTRKVGEIISRFN-DGDKIRNAISSVTLTLMIDVLMAVvgGAILYLQNLKLFFTCFVPIVLYL 318
Cdd:cd18559 73 VHLDLYHKALRSPISFFERTPSGELVNLFSkDLDRVDSMAPQVIKMWMGPLQNVI--GLYLLILLAGPMAAVGIPLGLLY 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 336293682 319 ILVFGF-KNKLKKVNRRVMEDNASLTSYLVESLEGIETVKAFNGE 362
Cdd:cd18559 151 VPVNRVyAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWE 195
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
164-456 |
7.47e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 39.16 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 164 KGLLLNIFIASILVTILgIAGSFYYEFLIDDILPNNLKASLHSISIAMLILLLFKIVTEFFrKTLLLYMAQ----NIDVP 239
Cdd:cd18556 1 KLLFFSILFISLLSSIL-ISISPVILAKITDLLTSSSSDSYNYIVVLAALYVITISATKLL-GFLSLYLQSslrvELIIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 240 LLLGYYNHVVKLPMNFFGTRKVGEIISRFNDGDK-----IRNAISSVtLTLMIDVLMAVVggaiLYLQNLKLFFTC--FV 312
Cdd:cd18556 79 ISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNdlytlVRNLSTNI-LPPLLQLIIAIV----VILSSGDYFVAAlfLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 336293682 313 PIVLYLILVFGFKNKLKKVNRRVMedNASLTSY--LVESLEGIETVKAFNGEGLVrLKTENKFLK----FMKSYFKHGYT 386
Cdd:cd18556 154 YAVLFVINNTIFTKKIVSLRNDLM--DAGRKSYslLTDSVKNIVAAKQNNAFDFL-FKRYEATLTndrnSQKRYWKLTFK 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 336293682 387 YNVQGTLMDTISggFGICLLWfggSL--VLKGEVTIGELISFNALLAYFIQPIGRLINLQPQLQEAIVASDR 456
Cdd:cd18556 231 MLILNSLLNVIL--FGLSFFY---SLygVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSVHSLAG 297
|
|
| |
