|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-709 |
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: 646.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 5 KKRVKFVEQMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPC 84
Cdd:COG2274 1 RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 85 IIQWGNNHFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFALQFQFIGNTKNIIPKEKQENIILKYFKQHKGRFFG 164
Cdd:COG2274 81 ILHWDGNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKRGEKPFGLRWFLRLLRRYRRLLLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 165 LVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKMF 244
Cdd:COG2274 161 VLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 245 HLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNANVIR 324
Cdd:COG2274 241 RLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 325 KMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLLVLWVG 404
Cdd:COG2274 321 RLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 405 GHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQE--KSNVQAHSIKGDIKFENVN 482
Cdd:COG2274 401 AYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREegRSKLSLPRLKGDIELENVS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 483 FKYNQFSKYILKDLNFTIKQGEKVAIVGPSgsgkssiskLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKL 562
Cdd:COG2274 481 FRYPGDSPPVLDNISLTIKPGERVAIVGRSgsgkstllkLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFL 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 563 FSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATS 642
Cdd:COG2274 561 FSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 643 HLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLYSQ 709
Cdd:COG2274 641 ALDAETEAIILENLRRLlkGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQ 709
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
151-707 |
2.54e-142 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 428.43 E-value: 2.54e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 151 ILKYFKQHKGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKS 230
Cdd:COG1132 12 LLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 231 LDLSIMNDFMKKMFHLPYSFFDNRSSGDLLFRANSAVF-IRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLS 309
Cdd:COG1132 92 VVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDaVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 310 MLLAVILFVNANVIRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTI 388
Cdd:COG1132 172 PLLLLVLRLFGRRLRKLFRR-VQEALaELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 389 TGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDE-QEKSNV 467
Cdd:COG1132 251 MELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEiPDPPGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 468 QAHS-IKGDIKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSgsgkssiskLLLALYKVSEGQILINNKNINDYDY 546
Cdd:COG1132 331 VPLPpVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSgsgkstlvnLLLRFYDPTSGRILIDGVDIRDLTL 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 547 HSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVAR 626
Cdd:COG1132 410 ESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIAR 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 627 ALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYY 704
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYA 569
|
...
gi 446631050 705 NLY 707
Cdd:COG1132 570 RLY 572
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
7-706 |
1.11e-126 |
|
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: 392.38 E-value: 1.11e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 7 RVKFVEQMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCII 86
Cdd:TIGR03796 1 RTPTVLQMEAVECGAASLAMILAYYGRYVPLEELREECGVSRDGSKASNLLKAARSYGLEAKGFRKELDALAELPLPYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 87 QWGNNHFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFAL------QFQFIGNTKNIIPkekqenIILKYFKQHKG 160
Cdd:TIGR03796 81 FWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVVLtfepgpEFQKGGRKPSLLR------ALWRRLRGSRG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 161 RFFGLVF--LSIIIQGLmtVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMND 238
Cdd:TIGR03796 155 ALLYLLLagLLLVLPGL--VIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:TIGR03796 233 FLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:TIGR03796 313 VSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSA 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLR------TKDEQEKSNVQAHSI 472
Cdd:TIGR03796 393 LILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvdplLEEPEGSAATSEPPR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 473 K--GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLR 550
Cdd:TIGR03796 473 RlsGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLA 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQ 630
Cdd:TIGR03796 553 NSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVR 632
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 631 EPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNL 706
Cdd:TIGR03796 633 NPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
20-709 |
2.14e-104 |
|
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: 334.02 E-value: 2.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 20 GLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCIIQWGNNHFVVLeRI 99
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKVSIGRLNKLPLPALIDGEGGWFVLG-KL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 100 KKQSYIIVDPNRGKIEV-PQDEFKQKYSGFALqfqfIGNTKNIIPKEKQENI------ILKYFKQhkgrFFGLVFLSIII 172
Cdd:TIGR01846 80 TANGVTIYDPPGDAPEVlSREVLEALWSGTVI----LLATRSVAGKALKFGFswfipaIIRYRKQ----FREVLLISLAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 173 QGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKMFHLPYSFFD 252
Cdd:TIGR01846 152 QLFALVTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 253 NRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNANVIRKMTKKNIQ 332
Cdd:TIGR01846 232 SRRVGDTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 333 DKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLLVLWVGGHALINGE 412
Cdd:TIGR01846 312 RSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 413 ITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAH-SIKGDIKFENVNFKYNQFSKY 491
Cdd:TIGR01846 392 LSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAALpELRGAITFENIRFRYAPDSPE 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSISDNI 571
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNI 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 572 SMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERH 651
Cdd:TIGR01846 552 ALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEAL 631
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 652 IENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLYSQ 709
Cdd:TIGR01846 632 IMRNMREIcrGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQ 691
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
94-706 |
1.47e-97 |
|
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: 315.74 E-value: 1.47e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 94 VVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFALQFQFIGNTKNIIPKEkqeniILKY-FKQHKGRFFGLVFLSIII 172
Cdd:TIGR03797 74 VALLPVSRGGYEIFDPATGTRRRVDAAMAATLAPEAYMFYRPLPDKALGLRD-----LLRFaLRGARRDLLAILAMGLLG 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 173 QGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKMFHLPYSFFD 252
Cdd:TIGR03797 149 TLLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 253 NRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLD-LSLLLLSLSMLLAVILFVNANVIRKMTKK-N 330
Cdd:TIGR03797 229 QYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLNLGLMFYYSWKlALVAVALALVAIAVTLVLGLLQVRKERRLlE 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 331 IQDKVNTQAVLTENmyNIVDIKSLGLEKKRLSLWSGNYSKELE---SSQRLNIFQAVIHTItgfFQVSVPLLVLWVGGHA 407
Cdd:TIGR03797 309 LSGKISGLTVQLIN--GISKLRVAGAENRAFARWAKLFSRQRKlelSAQRIENLLTVFNAV---LPVLTSAALFAAAISL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 408 LINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHSIKGDIKFENVNFKYNQ 487
Cdd:TIGR03797 384 LGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKTDPGKLSGAIEVDRVTFRYRP 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 488 FSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSI 567
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSI 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNI----SMSkdnHDDlkVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSH 643
Cdd:TIGR03797 544 FENIaggaPLT---LDE--AWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSA 618
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 644 LDLFTERHIENTLKELNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNL 706
Cdd:TIGR03797 619 LDNRTQAIVSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
159-452 |
4.92e-97 |
|
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: 301.35 E-value: 4.92e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMND 238
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:cd18555 81 FFEHLLKLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:cd18555 161 TRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18555 241 LILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-707 |
3.87e-92 |
|
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: 302.04 E-value: 3.87e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 13 QMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLP------CII 86
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADMSLFEDKNLPlpfiahVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 87 QWGNNHFVVLERIKKQSYIIVDPNR--GKIEVPQDEFKQKYSGFALqfqFIGNTKNIIPKEKQENIILKYF----KQHKg 160
Cdd:TIGR01193 81 NGKLPHYYVVYGVTKNHLIIADPDPtvGITKISKEDFYEEWTGIAI---FISPTPEYKPIKEKENSLLKFIplitRQKK- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 161 rffgLVFLSIIIQGLMTVIPLSTKW----VTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIM 236
Cdd:TIGR01193 157 ----LIVNIVIAAIIVTLISIAGSYylqkIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDII 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 237 NDFMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVIL 316
Cdd:TIGR01193 233 LSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVII 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 317 FVNANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSV 396
Cdd:TIGR01193 313 ILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLIL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 397 PLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHSIK--G 474
Cdd:TIGR01193 393 NVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNlnG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 475 DIKFENVNFKYNqFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIG 554
Cdd:TIGR01193 473 DIVINDVSYSYG-YGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQESKLFSGSISDNISM-SKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 634 AIVFDEATSHLDLFTERHI-ENTLKELNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLY 707
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIvNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
476-707 |
1.15e-77 |
|
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: 248.30 E-value: 1.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 636 VFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLY 707
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLmkNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
474-700 |
2.88e-76 |
|
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: 244.44 E-value: 2.88e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSI 553
Cdd:cd03254 1 GEIEFENVNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNR 700
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
150-706 |
7.68e-76 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 255.01 E-value: 7.68e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 150 IILKYFKQHKGRFFG-LVFLSIIIQGLMTViPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQ 228
Cdd:TIGR02204 8 ALWPFVRPYRGRVLAaLVALLITAAATLSL-PYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 229 KSLDLSIMNDFMKKMFHLPYSFFDNRSSGDLLFR-ANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLS 307
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRlTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 308 LSMLLAVILFVNANVIRKMTKKNiQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELE-SSQRLNIfQAVI 385
Cdd:TIGR02204 167 AVPLVLLPILLFGRRVRKLSRES-QDRIaDAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEaARQRIRT-RALL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 386 HTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAF---SSIAGSYITPIVSVSNnytQLISLGSYFSRIKDVLRTKDEQ 462
Cdd:TIGR02204 245 TAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFvfyAVMVAGSIGTLSEVWG---ELQRAAGAAERLIELLQAEPDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 463 EKSNVQ---AHSIKGDIKFENVNFKYNQFSKY-ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINN 538
Cdd:TIGR02204 322 KAPAHPktlPVPLRGEIEFEQVNFAYPARPDQpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 539 KNINDYDYHSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQ 618
Cdd:TIGR02204 402 VDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:TIGR02204 482 RQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLmkGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAEL 561
|
570
....*....|
gi 446631050 697 LKNRSYYYNL 706
Cdd:TIGR02204 562 IAKGGLYARL 571
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
476-709 |
1.68e-75 |
|
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: 242.91 E-value: 1.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 636 VFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLYSQ 709
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVskGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
151-708 |
1.57e-74 |
|
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: 251.17 E-value: 1.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 151 ILKYFKQHKGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLnsfgWLIIIFsisFVLMSLLRGIS------- 223
Cdd:TIGR02203 5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVL----WWVPLV---VIGLAVLRGICsfvstyl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 224 IALLQKSLDLSIMNDFMKKMFHLPYSFFDNRSSGDLLFR-ANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLS 302
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRiTFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 303 LLLlslsmllAVILFVNANVIRKMTK------KNIQDKVNTQA-VLTENMYNIVDIKSLG---LEKKRLS-LWSGNYSKE 371
Cdd:TIGR02203 158 LIV-------VVMLPVLSILMRRVSKrlrrisKEIQNSMGQVTtVAEETLQGYRVVKLFGgqaYETRRFDaVSNRNRRLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 372 LESSQRLNIFQAVIHTItgffqVSVPL-LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFS 450
Cdd:TIGR02203 231 MKMTSAGSISSPITQLI-----ASLALaVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 451 RIKDVLRTKDEQEKSNVQAHSIKGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVS 530
Cdd:TIGR02203 306 SLFTLLDSPPEKDTGTRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 531 EGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSISDNISMSK-DNHDDLKVIDAAKKSGILEDILNSPMGFETIISE 609
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 610 SGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMI 687
Cdd:TIGR02203 466 NGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
570 580
....*....|....*....|.
gi 446631050 688 KEIGTHEQLLKNRSYYYNLYS 708
Cdd:TIGR02203 546 VERGTHNELLARNGLYAQLHN 566
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
151-706 |
6.81e-74 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 253.11 E-value: 6.81e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 151 ILKYFKQHKGRFF-GLVFLSIIIQGLMtVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQK 229
Cdd:TIGR00958 152 LLGLSGRDWPWLIsAFVFLTLSSLGEM-FIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 230 SLDLSIMNDFMKKMFHLPYSFFDNRSSGDLLFRA-------------NSAVFIRDII--------------STTMITiFI 282
Cdd:TIGR00958 231 RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLssdtqtmsrslslNVNVLLRNLVmllgllgfmlwlspRLTMVT-LI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 283 DLLLIITYTAVMinfsldlsllllslsmllavilfvnaNVIRKMTKKNIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRL 361
Cdd:TIGR00958 310 NLPLVFLAEKVF--------------------------GKRYQLLSEELQEAVaKANQVAEEALSGMRTVRSFAAEEGEA 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 362 SLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAF---SSIAGSYITPIVSVsnn 438
Cdd:TIGR00958 364 SRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFllyQEQLGEAVRVLSYV--- 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 439 YTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHS-IKGDIKFENVNFKY-NQFSKYILKDLNFTIKQGEKVAIVGPSGSGK 516
Cdd:TIGR00958 441 YSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLnLEGLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGEVVALVGPSGSGK 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 517 SSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDI 596
Cdd:TIGR00958 521 STVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFI 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 597 LNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAHRLRTIQNA 676
Cdd:TIGR00958 601 MEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERA 680
|
570 580 590
....*....|....*....|....*....|
gi 446631050 677 DKIIYLEDGMIKEIGTHEQLLKNRSYYYNL 706
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
476-709 |
8.28e-68 |
|
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: 222.41 E-value: 8.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKY-----NQfskyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLR 550
Cdd:cd03249 1 IEFKNVSFRYpsrpdVP----ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQ 630
Cdd:cd03249 77 SQIGLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 631 EPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLYS 708
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVK 236
|
.
gi 446631050 709 Q 709
Cdd:cd03249 237 A 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
391-699 |
7.71e-67 |
|
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: 230.41 E-value: 7.71e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 391 FFQVSVPLLVLWVGgHALINGEITLGTLIAFSSIAGSYITPivsvsnnytqLISLGSYF----------SRIKDVLRTKD 460
Cdd:COG4988 251 FASLSIALVAVYIG-FRLLGGSLTLFAALFVLLLAPEFFLP----------LRDLGSFYharangiaaaEKIFALLDAPE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 461 EQEKSNVQAHSIKG--DIKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINN 538
Cdd:COG4988 320 PAAPAGTAPLPAAGppSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 539 KNINDYDYHSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQ 618
Cdd:COG4988 399 VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558
|
...
gi 446631050 697 LKN 699
Cdd:COG4988 559 LAK 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
476-707 |
9.81e-67 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 219.67 E-value: 9.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 636 VFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLY 707
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
188-708 |
8.71e-63 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 219.89 E-value: 8.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 188 DNAFSNSDinklNSFgwlIIIFSISFVLMSLLRGIS-------IALLQKSLDLSIMNDFMKKMFHLPYSFFDNRSSGDLL 260
Cdd:PRK11176 53 DDGFGKAD----RSV---LKWMPLVVIGLMILRGITsfissycISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 261 FR--------ANSAvfirdiiSTTMITIFIDLLLIITYTAVMInfsldlsllllSLSMLLAVILFVNANV----IRKMTK 328
Cdd:PRK11176 126 SRitydseqvASSS-------SGALITVVREGASIIGLFIMMF-----------YYSWQLSLILIVIAPIvsiaIRVVSK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 329 ------KNIQDKVNTQAVLTENMynivdIK------SLG---LEKKRLSLWSGN---YSKELESSQrlNIFQAVIHTITG 390
Cdd:PRK11176 188 rfrnisKNMQNTMGQVTTSAEQM-----LKghkevlIFGgqeVETKRFDKVSNRmrqQGMKMVSAS--SISDPIIQLIAS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 391 FFQVsvplLVLWVGGHALINGEITLGTL-IAFSSIAGsYITPIVSVSNNYTQlislgsyFSR-------IKDVLRTKDEQ 462
Cdd:PRK11176 261 LALA----FVLYAASFPSVMDTLTAGTItVVFSSMIA-LMRPLKSLTNVNAQ-------FQRgmaacqtLFAILDLEQEK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 463 EKSNVQAHSIKGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN 542
Cdd:PRK11176 329 DEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 543 DYDYHSLRTSIGTVLQESKLFSGSISDNIS-MSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQR 621
Cdd:PRK11176 409 DYTLASLRNQVALVSQNVHLFNDTIANNIAyARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQR 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
....*....
gi 446631050 700 RSYYYNLYS 708
Cdd:PRK11176 569 NGVYAQLHK 577
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
157-698 |
3.22e-62 |
|
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: 217.22 E-value: 3.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 157 QHKGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLnsFGWLIIIFSISFVLMSL--LRGISIALLQKSLDLS 234
Cdd:TIGR01842 3 KVKRTFIIVGLFSFVINILMLAPPLYMLQVYDRVLTSGSVPTL--LMLTVLALGLYLFLGLLdaLRSFVLVRIGEKLDGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 235 IMNDFMKKMFHLPYsffdNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAV 314
Cdd:TIGR01842 81 LNQPIFAASFSATL----RRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 315 ILFVNANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQV 394
Cdd:TIGR01842 157 LALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 395 SVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRtkdeQEKSNVQAHSI-- 472
Cdd:TIGR01842 237 VLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLA----NYPSRDPAMPLpe 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 473 -KGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRT 551
Cdd:TIGR01842 313 pEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 552 SIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQE 631
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 632 PSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
339-709 |
1.28e-61 |
|
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: 216.17 E-value: 1.28e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 339 AVLTENMYNIVDIKSLGLE---KKRLSLWSGNYSKELESSQRLNIF-QAVIHTITGFfqvSVpLLVLWVGGHALINGEI- 413
Cdd:COG4987 196 ARLTDLLQGAAELAAYGALdraLARLDAAEARLAAAQRRLARLSALaQALLQLAAGL---AV-VAVLWLAAPLVAAGALs 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 414 -------TLGTLIAFSSIAgsyitPIVSVSNNYTQLISLGSyfsRIKDVLRTKDE-QEKSNVQAHSIKGDIKFENVNFKY 485
Cdd:COG4987 272 gpllallVLAALALFEALA-----PLPAAAQHLGRVRAAAR---RLNELLDAPPAvTEPAEPAPAPGGPSLELEDVSFRY 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 486 NQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSG 565
Cdd:COG4987 344 PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDT 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 566 SISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLD 645
Cdd:COG4987 424 TLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLD 503
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 646 LFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLYSQ 709
Cdd:COG4987 504 AATEQALLADLLEAlaGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
378-706 |
3.09e-61 |
|
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: 215.84 E-value: 3.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 378 LNIFQAVIhtitgfFQVSVpLLVLWVGGHALINGEITLGTLIAfssiAGSYITPIvsvsnnYTQLISLGSYFSRIK---- 453
Cdd:COG5265 265 LNFGQALI------IALGL-TAMMLMAAQGVVAGTMTVGDFVL----VNAYLIQL------YIPLNFLGFVYREIRqala 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 454 ------DVLRTKDE-QEKSNVQAHSIK-GDIKFENVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLA 525
Cdd:COG5265 328 dmermfDLLDQPPEvADAPDAPPLVVGgGEVRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 526 LYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFET 605
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDT 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 606 IISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLE 683
Cdd:COG5265 487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVarGRTTLVIAHRLSTIVDADEILVLE 566
|
330 340
....*....|....*....|...
gi 446631050 684 DGMIKEIGTHEQLLKNRSYYYNL 706
Cdd:COG5265 567 AGRIVERGTHAELLAQGGLYAQM 589
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
151-706 |
3.15e-61 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 215.60 E-value: 3.15e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 151 ILKYFKQHKGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDInklnsfgWLIIIFSISFVLMSLLRGISIAL---- 226
Cdd:PRK13657 10 VLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDI-------FPLLAAWAGFGLFNIIAGVLVARhadr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 227 LQKSLDLSIMNDFMKKMFHLPYSFFDNRSSGDLL---FRANSAV------FIRDIISTTM-------ITIFIDLLLIITY 290
Cdd:PRK13657 83 LAHRRRLAVLTEYFERIIQLPLAWHSQRGSGRALhtlLRGTDALfglwleFMREHLATLValvvllpLALFMNWRLSLVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 291 TAVMINFSldlsllllslsmllavilFVNANVIRKMtkKNIQDKV-----NTQAVLTENMYNIVDIKS---LGLEKKRLS 362
Cdd:PRK13657 163 VVLGIVYT------------------LITTLVMRKT--KDGQAAVeehyhDLFAHVSDAIGNVSVVQSynrIEAETQALR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 363 lwsgNYSKELESSQR--------LNIFQAVIHTITgffqvsvpLLVLWVGGHALI-NGEITLGTLIAFSSIAGSYITPIV 433
Cdd:PRK13657 223 ----DIADNLLAAQMpvlswwalASVLNRAASTIT--------MLAILVLGAALVqKGQLRVGEVVAFVGFATLLIGRLD 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 434 SVSNNYTQLIS----LGSYFSRIKDVLRTKDEQekSNVQAHSIKGDIKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIV 509
Cdd:PRK13657 291 QVVAFINQVFMaapkLEEFFEVEDAVPDVRDPP--GAIDLGRVKGAVEFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 510 GPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKK 589
Cdd:PRK13657 368 GPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAER 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 590 SGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIA 667
Cdd:PRK13657 448 AQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELmkGRTTFIIA 527
|
570 580 590
....*....|....*....|....*....|....*....
gi 446631050 668 HRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNL 706
Cdd:PRK13657 528 HRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
313-698 |
1.11e-58 |
|
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: 208.06 E-value: 1.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 313 AVILFV----NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTI 388
Cdd:COG4618 165 ALVLVAlallNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSAL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 389 TGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSnVQ 468
Cdd:COG4618 245 SKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPER-MP 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 469 AHSIKGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNINDYDYHS 548
Cdd:COG4618 324 LPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPsgsgkstlarLLVGVWPPTAGSVRLDGADLSQWDREE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQESKLFSGSISDNISMSKDnHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARAL 628
Cdd:COG4618 404 LGRHIGYLPQDVELFDGTIAENIARFGD-ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 629 YQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
474-692 |
1.38e-58 |
|
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: 197.33 E-value: 1.38e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSI 553
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSISDNISmSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGT 692
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
476-685 |
6.36e-57 |
|
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: 191.06 E-value: 6.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNIsmskdnhddlkvidaakksgiledilnspmgfetiisesgnnFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446631050 636 VFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDG 685
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
474-687 |
4.40e-56 |
|
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: 190.49 E-value: 4.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSI 553
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMI 687
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
472-687 |
7.95e-49 |
|
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: 171.11 E-value: 7.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 472 IKGDIKFENVNFKY-NQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLR 550
Cdd:cd03248 8 LKGIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQ 630
Cdd:cd03248 88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 631 EPSAIVFDEATSHLDLFTERHIENTLKE--LNITQIIIAHRLRTIQNADKIIYLEDGMI 687
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
159-452 |
1.50e-48 |
|
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: 172.73 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMND 238
Cdd:cd18779 1 PGLLGQILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:cd18779 81 FLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:cd18779 161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18779 241 VLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
476-687 |
3.42e-48 |
|
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: 167.39 E-value: 3.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNIsmskdnhddlkvidaakksgiledilnspmgfetiisesgnnFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 636 VFDEATSHLDLFTERHIENTLKELNI---TQIIIAHRLRTIQNADKIIYLEDGMI 687
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAagaTRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
365-707 |
1.69e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 176.94 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 365 SGNYSKELESS-QRLNIFQAVIHTITGFFQVSVPL-------LVLW-----VGGH----ALInGEITLGTLIAFSSIAgs 427
Cdd:PRK11160 219 EDRYRQQLEQTeQQWLAAQRRQANLTGLSQALMILangltvvLMLWlaaggVGGNaqpgALI-ALFVFAALAAFEALM-- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 428 yitPIVSVSNNYTQLISLGSyfsRIKDVLR-TKDEQEKSNVQAHSIKGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKV 506
Cdd:PRK11160 296 ---PVAGAFQHLGQVIASAR---RINEITEqKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKV 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 507 AIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDLKVIDA 586
Cdd:PRK11160 370 ALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEV 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 587 AKKSGiLEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQI 664
Cdd:PRK11160 450 LQQVG-LEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVL 528
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446631050 665 IIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLY 707
Cdd:PRK11160 529 MITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
159-437 |
1.15e-44 |
|
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: 161.84 E-value: 1.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMND 238
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:cd18570 161 FNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSN 437
Cdd:cd18570 241 LILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLIN 279
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
336-707 |
1.71e-41 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 159.49 E-value: 1.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 336 NTQAvlTENMYNIVDIKSLGLEKKRlslwSGNYSKELESSQRLNI--------FQAVIHTITGFFQvsvpLLVLWVGGHA 407
Cdd:PRK10789 176 NDRT--QESLTSIRMIKAFGLEDRQ----SALFAADAEDTGKKNMrvaridarFDPTIYIAIGMAN----LLAIGGGSWM 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 408 LINGEITLGTLIAFSSIAGSYITPIVSVSNNYtQLISLGSY-FSRIKDVLR----TKDEQEKSNVQAHSIKGDIKfenvN 482
Cdd:PRK10789 246 VVNGSLTLGQLTSFVMYLGLMIWPMLALAWMF-NIVERGSAaYSRIRAMLAeapvVKDGSEPVPEGRGELDVNIR----Q 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 483 FKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKL 562
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 563 FSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATS 642
Cdd:PRK10789 401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 643 HLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLY 707
Cdd:PRK10789 481 AVDGRTEHQILHNLRQWgeGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMY 547
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
474-692 |
1.36e-40 |
|
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: 147.56 E-value: 1.36e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSI 553
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSISDNISMSkDNHDDLKVIDAAKksgiledilnspmgfetiISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPF-DEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGT 692
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEftNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
476-682 |
1.84e-40 |
|
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: 155.91 E-value: 1.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446631050 636 VFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYL 682
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
165-452 |
2.24e-39 |
|
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: 146.94 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 165 LVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKMF 244
Cdd:cd18568 7 ILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 245 HLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNANVIR 324
Cdd:cd18568 87 SLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 325 KMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLLVLWVG 404
Cdd:cd18568 167 RNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446631050 405 GHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18568 247 AYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
8-132 |
2.89e-39 |
|
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: 140.86 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 8 VKFVEQMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEID-MAELTAISLPCII 86
Cdd:cd02425 1 VKPILQNNQTECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISfKKNLYPLKLPVII 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446631050 87 QWGNNHFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFALQF 132
Cdd:cd02425 81 FWNNNHFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYILTF 126
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
411-707 |
5.53e-39 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 152.56 E-value: 5.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 411 GEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHSiKGDIKFENVNFKYNQfSK 490
Cdd:PRK10790 277 GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQ-SGRIDIDNVSFAYRD-DN 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 491 YILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSISDN 570
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLAN 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 ISMSKDNHDDlKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTER 650
Cdd:PRK10790 435 VTLGRDISEE-QVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQ 513
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 651 HIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLY 707
Cdd:PRK10790 514 AIQQALAAVreHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
7-130 |
1.50e-38 |
|
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: 139.28 E-value: 1.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 7 RVKFVEQMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCII 86
Cdd:pfam03412 1 KYKIVLQVDENDCGLACLAMILKYYGSNVSLEELRELAGTPAEGTSLLGLKKAAEKLGFKAKAIKADLSELKELPLPFIA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446631050 87 QWGNN--HFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFAL 130
Cdd:pfam03412 81 HWDGNggHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVAL 126
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
165-436 |
4.29e-37 |
|
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: 140.81 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 165 LVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKMF 244
Cdd:cd18782 7 VLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 245 HLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNANVIR 324
Cdd:cd18782 87 RLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 325 KMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLLVLWVG 404
Cdd:cd18782 167 RQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVG 246
|
250 260 270
....*....|....*....|....*....|..
gi 446631050 405 GHALINGEITLGTLIAFSSIAGSYITPIVSVS 436
Cdd:cd18782 247 AYLVLRGELTLGQLIAFRILSGYVTGPILRLS 278
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
159-452 |
2.49e-36 |
|
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: 138.36 E-value: 2.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMND 238
Cdd:cd18567 1 KRALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:cd18567 81 LFRHLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:cd18567 161 LYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18567 241 LVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELRMLRLHLERL 294
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
162-442 |
6.89e-36 |
|
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: 137.30 E-value: 6.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMK 241
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 242 KMFHLPYSFFDNRSSGDLLFRANSAVF-IRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNA 320
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDaVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 321 NVIRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLL 399
Cdd:cd07346 161 RRIRKASRE-VRESLaELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 446631050 400 VLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQL 282
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
8-132 |
4.25e-35 |
|
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: 129.30 E-value: 4.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 8 VKFVEQMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCIIQ 87
Cdd:cd02419 1 LPVILQTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRLDLEELGQLKLPCILH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 446631050 88 WGNNHFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFALQF 132
Cdd:cd02419 81 WDMNHFVVLKKVSRRRIVIHDPALGKRKLSLEEASRHFTGVALEL 125
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
490-709 |
1.49e-34 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 139.21 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLAL--YkvsEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGSI 567
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLF 647
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 648 TERHIENTLKELNITQ--IIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLYSQ 709
Cdd:PRK11174 520 SEQLVMQALNAASRRQttLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAH 583
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
476-700 |
1.04e-33 |
|
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: 128.99 E-value: 1.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPngsgkstllrLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQ--ESKLFSGSISDNIS-------MSKDNHDDlKVIDAAKKSGiLEDILNSPMgfetiisesgNNFSGGQRQRLLVAR 626
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAfgpenlgLPREEIRE-RVEEALELVG-LEHLADRPP----------HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 627 ALYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTI-QNADKIIYLEDGMIKEIGTHEQLLKNR 700
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
473-699 |
1.37e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 138.96 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 473 KGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTS 552
Cdd:PLN03232 1232 RGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSGSISDNISMSKDnHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEP 632
Cdd:PLN03232 1312 LSIIPQSPVLFSGTVRFNIDPFSE-HNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 633 SAIVFDEATSHLDLFTERHIENTLKE--LNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
476-691 |
1.52e-33 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 126.66 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDyHSLRTSIGT 555
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNIsmskdnhddlkvidaakksgiledilnspmgfetiisesGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 636 VFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIG 691
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
474-699 |
4.47e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 137.18 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGpsgSGKSSISKLLLALYKVSE---GQILINNKNINDYDYHSLR 550
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVG---RTGAGKSSMLNALFRIVElerGRILIDGCDISKFGLMDLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQESKLFSGSISDNISmSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQ 630
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 631 EPSAIVFDEATSHLDLFTERHIENTLKE--LNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREefKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
476-685 |
2.04e-32 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 124.50 E-value: 2.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYN---QFSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLAL---YKVSEGQILINNknindydyhsl 549
Cdd:cd03250 1 ISVEDASFTWDsgeQETSFTLKDINLEVPKGELVAIVGPvgsg---kssLLSALlgeLEKLSGSVSVPG----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 rtSIGTVLQESKLFSGSISDNISMSKD-NHDDL-KVIDAAkksGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARA 627
Cdd:cd03250 67 --SIAYVSQEPWIQNGTIRENILFGKPfDEERYeKVIKAC---ALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 628 LYQEPSAIVFDEATSHLDLFTERHI-ENTLKEL---NITQIIIAHRLRTIQNADKIIYLEDG 685
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfENCILGLllnNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
161-437 |
2.11e-32 |
|
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: 127.23 E-value: 2.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 161 RFFGLVFL-SIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDF 239
Cdd:cd18588 2 KLLGEVLLaSLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 240 MKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVN 319
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 320 ANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLL 399
Cdd:cd18588 162 TPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLA 241
|
250 260 270
....*....|....*....|....*....|....*...
gi 446631050 400 VLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSN 437
Cdd:cd18588 242 ILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQ 279
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
187-706 |
2.42e-32 |
|
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: 135.07 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 187 TDNAFSNSDIN----KLNSFGWLIIIFSISFVLMSLlrGISIALLQKSLDLSImnDFMKKMFHLPYSFFDNRSSGDLLFR 262
Cdd:TIGR00957 992 TDDPMVNGTQNntslRLSVYGALGILQGFAVFGYSM--AVSIGGIQASRVLHQ--DLLHNKLRSPMSFFERTPSGNLVNR 1067
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 263 ANSAVFIRDIISTTMITIFIDLLLIITYTAVMInfSLDLSLLLLSLSMLLAVILFVN---ANVIRKMTKKNIQDKVNTQA 339
Cdd:TIGR00957 1068 FSKELDTVDSMIPPVIKMFMGSLFNVIGALIVI--LLATPIAAVIIPPLGLLYFFVQrfyVASSRQLKRLESVSRSPVYS 1145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 340 VLTENMYNIVDIKSLGlEKKRLSLWSgnySKELESSQRL-------NIFQAVIHTITGFFQVSVPLLVLWVGGHALINGE 412
Cdd:TIGR00957 1146 HFNETLLGVSVIRAFE-EQERFIHQS---DLKVDENQKAyypsivaNRWLAVRLECVGNCIVLFAALFAVISRHSLSAGL 1221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 413 ITLGtlIAFSSIAGSYITPIVSVSNNY-TQLISLgsyfSRIKDVLRTKDE-----QEKSNVQAHSIKGDIKFENVNFKYN 486
Cdd:TIGR00957 1222 VGLS--VSYSLQVTFYLNWLVRMSSEMeTNIVAV----ERLKEYSETEKEapwqiQETAPPSGWPPRGRVEFRNYCLRYR 1295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 487 QFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGS 566
Cdd:TIGR00957 1296 EDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGS 1375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNISmSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDL 646
Cdd:TIGR00957 1376 LRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 647 FTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNL 706
Cdd:TIGR00957 1455 ETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
477-685 |
5.02e-32 |
|
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: 123.35 E-value: 5.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 477 KFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTV 556
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 557 LQ--ESKLFSGSISDNIS-----MSKDNHDDLKVIDAAKKSGILEDILNSPMgfetiisesgNNFSGGQRQRLLVARALY 629
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAfglenLGLPEEEIEERVEEALELVGLEGLRDRSP----------FTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 630 QEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDG 685
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
476-696 |
8.53e-32 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 123.44 E-value: 8.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPS---GSGKSSISKLLLALYKV--SEGQILINNKNINDYDYH--S 548
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSgcgKSTLLRLLNRLNDLIPGapDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQESKLFSGSISDNIS-------MSKDNHDDLKVIDAAKKSGILEDILNSPMGFEtiisesgnnFSGGQRQR 621
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgIKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN--ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQL 696
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKkeYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
476-687 |
5.38e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 120.69 E-value: 5.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNI----SMSKDNHDDLKVIDAAKKSGILEDILNSPMgfetiisesgNNFSGGQRQRLLVARALYQE 631
Cdd:COG4619 79 VPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPV----------ERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 632 PSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
474-697 |
9.35e-31 |
|
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: 121.55 E-value: 9.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSI 553
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSISDNISMSKDNHDDlKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECKCTDD-RLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 634 AIVFDEATSHLDLFTerhiENTLKELNITQ------IIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLL 697
Cdd:cd03288 177 ILIMDEATASIDMAT----ENILQKVVMTAfadrtvVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
398-670 |
3.65e-30 |
|
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: 125.55 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 398 LLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHSIKG--- 474
Cdd:TIGR02868 253 LGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGlgk 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 475 -DIKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSI 553
Cdd:TIGR02868 333 pTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:TIGR02868 412 SVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
250 260 270
....*....|....*....|....*....|....*....
gi 446631050 634 AIVFDEATSHLDLFTERHIENTL--KELNITQIIIAHRL 670
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLlaALSGRTVVLITHHL 530
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
476-699 |
1.01e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQ--ESKLFSGSISDNISMSKDNhddlKVIDAAKKSGILEDiLNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGLEN----KKVPPKKMKDIIDD-LAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
165-707 |
1.18e-28 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 123.22 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 165 LVFLSIIIQG-LMTVIPL-STKWV-TDNAFSNSDINKlNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMK 241
Cdd:PTZ00265 829 IIALSILVAGgLYPVFALlYAKYVsTLFDFANLEANS-NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 242 KMFHLPYSFFDNRSSGDLLFRA--NSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLsmllavILFVN 319
Cdd:PTZ00265 908 NILYQEISFFDQDKHAPGLLSAhiNRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTG------TYFIF 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 320 ANVI----RKMTKKNIQDKVNTQA------------------VLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQR 377
Cdd:PTZ00265 982 MRVFairaRLTANKDVEKKEINQPgtvfaynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKR 1061
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 378 LNIFQAVIHTITGFFQVSVPLLVLWVGGHALINGEIT----LGTLIAFSsIAGSYITPIVSVSNNYTQL-ISLGSYFSRI 452
Cdd:PTZ00265 1062 KTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILvddfMKSLFTFL-FTGSYAGKLMSLKGDSENAkLSFEKYYPLI 1140
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 453 --KDVLRTKDEQEKSNVQAHSIKGDIKFENVNFKY-NQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKV 529
Cdd:PTZ00265 1141 irKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDL 1220
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 530 ------------------------------------------------------SEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:PTZ00265 1221 kndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSI 1300
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:PTZ00265 1301 VSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKIL 1380
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 636 VFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQNADKIIYLED-----GMIKEIGTHEQLLKNRSYYYNL 706
Cdd:PTZ00265 1381 LLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSVQDGVYKK 1460
|
.
gi 446631050 707 Y 707
Cdd:PTZ00265 1461 Y 1461
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
476-685 |
1.42e-28 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 112.67 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHS--LRTSI 553
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSG-SISDNISMSkdnhddlkvidaakksgiledilnspmgfetiisesgnnFSGGQRQRLLVARALYQEP 632
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 633 SAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDG 685
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQaqlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
9-130 |
5.99e-28 |
|
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: 109.22 E-value: 5.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 9 KFVEQMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDM--AELTAISLPCII 86
Cdd:cd02418 2 PYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVKADMdlFELKDIPLPFIA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 446631050 87 ----QWGNNHFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFAL 130
Cdd:cd02418 82 hvikEWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVAL 129
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
476-687 |
1.24e-27 |
|
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: 111.04 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQ--FSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL---- 549
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 RTSIGTVLQESKLFSG-SISDNISM------SKDNHDDLKVIDAAKKSGiLEDILNSPmgfetiISEsgnnFSGGQRQRL 622
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllagVPKKERRERAEELLERVG-LGDRLNHY------PSE----LSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQNADKIIYLEDGMI 687
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeagTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
476-699 |
1.26e-27 |
|
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: 117.31 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVS---EGQILINNKNINDYDYHSLRTS 552
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQE--SKLFSGSISDNI-------SMSKDNHDDlKVIDAAKKSGIledilnspmgfETIISESGNNFSGGQRQRLL 623
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIaealenlGLSRAEARA-RVLELLEAVGL-----------ERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 624 VARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTI-QNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqrerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 446631050 699 N 699
Cdd:COG1123 233 A 233
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
165-447 |
1.62e-27 |
|
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: 112.95 E-value: 1.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 165 LVFLSIIIQGLmtVIPLSTKWVTDNAFsnsdINKLNS-FGWLIIIFSISFVL---MSLLRGISIALLQKSLDLSIMNDFM 240
Cdd:cd18569 9 LAGLLLVIPGL--VIPVFSRIFIDDIL----VGGLPDwLRPLLLGMALTALLqglLTWLQQYYLLRLETKLALSSSSRFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 241 KKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNA 320
Cdd:cd18569 83 WHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 321 NVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLLV 400
Cdd:cd18569 163 RKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446631050 401 LWVGGHALINGEITLGTLIAFSSIAGSYITPIvsvsnnyTQLISLGS 447
Cdd:cd18569 243 LGLGGLLVMDGALTIGMLVAFQSLMASFLAPV-------NSLVGLGG 282
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
476-691 |
2.53e-27 |
|
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: 110.67 E-value: 2.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVN--FKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL---R 550
Cdd:cd03257 2 LEVKNLSvsFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQES-----------KLFSGSISDNISMSKDNHDDLKVIDAAKKSGILEDILNS-PmgfetiisesgNNFSGGQ 618
Cdd:cd03257 82 KEIQMVFQDPmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRyP-----------HELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIG 691
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
159-452 |
3.68e-27 |
|
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: 111.91 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMND 238
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:cd18566 81 AFEHLLSLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:cd18566 161 LGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
207-684 |
6.88e-27 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 117.44 E-value: 6.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 207 IIFSISFV-----LMSLLRGISIALLQKSLDLSIMNDFMKKMFHLPYSFFDNRSSGDLlfRANSAVFIRDI---ISTTMI 278
Cdd:PTZ00265 99 IIFSLVLIgifqfILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKL--TSDLDFYLEQVnagIGTKFI 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 279 TIFidllliiTYTAVMINFSLDLSLLLLSLSMLLAVI---LFVNANVIRKMTKKNIQDKV----NTQAVLTENMYNIVDI 351
Cdd:PTZ00265 177 TIF-------TYASAFLGLYIWSLFKNARLTLCITCVfplIYICGVICNKKVKINKKTSLlynnNTMSIIEEALVGIRTV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 352 KSLGLEKKRLSLWsgNYSKELESSQRL--NIFQAV-IHTITGFFQVSVPLlVLWVGGHALING----------------E 412
Cdd:PTZ00265 250 VSYCGEKTILKKF--NLSEKLYSKYILkaNFMESLhIGMINGFILASYAF-GFWYGTRIIISDlsnqqpnndfhggsviS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 413 ITLGTLIAFSSIagSYITP-IVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQahsikgDIKFENVNFKYNQFSKY 491
Cdd:PTZ00265 327 ILLGVLISMFML--TIILPnITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK------KIQFKNVRFHYDTRKDV 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 -ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNK-NINDYDYHSLRTSIGTVLQESKLFSGSISD 569
Cdd:PTZ00265 399 eIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDINLKWWRSKIGVVSQDPLLFSNSIKN 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 570 NISMSKDNHDDLKVID--------------------AAKKSGILEDILNS------------------------------ 599
Cdd:PTZ00265 479 NIKYSLYSLKDLEALSnyynedgndsqenknkrnscRAKCAGDLNDMSNTtdsneliemrknyqtikdsevvdvskkvli 558
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 600 -------PMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAH 668
Cdd:PTZ00265 559 hdfvsalPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgneNRITIIIAH 638
|
570
....*....|....*.
gi 446631050 669 RLRTIQNADKIIYLED 684
Cdd:PTZ00265 639 RLSTIRYANTIFVLSN 654
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
476-687 |
2.05e-26 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 107.62 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFskYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIND--YDYHSLRTSI 553
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSG-SISDNIS--------MSKDNHDDlKVIDAAKKSGILEDILNSPmgfetiisesgNNFSGGQRQRLLV 624
Cdd:cd03262 79 GMVFQQFNLFPHlTVLENITlapikvkgMSKAEAEE-RALELLEKVGLADKADAYP-----------AQLSGGQQQRVAI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
476-698 |
2.21e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 108.25 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNIndydyHSLRTSIGT 555
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPngagkstllkAILGLLPPTSGTVRLFGKPP-----RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKL---FSGSISDNISMSKDNH----------DDLKVIDAAKKSGiLEDILNSPMGfetiisesgnNFSGGQRQRL 622
Cdd:COG1121 80 VPQRAEVdwdFPITVRDVVLMGRYGRrglfrrpsraDREAVDEALERVG-LEDLADRPIG----------ELSGGQQQRV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTI-QNADKIIYLEDGMI-----KEIGTH 693
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGAVrEYFDRVLLLNRGLVahgppEEVLTP 228
|
....*
gi 446631050 694 EQLLK 698
Cdd:COG1121 229 ENLSR 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
466-701 |
4.58e-26 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 114.88 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 466 NVQAhsikGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYD 545
Cdd:PTZ00243 1303 PVQA----GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 546 YHSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDlKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVA 625
Cdd:PTZ00243 1379 LRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSA-EVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 626 RALYQEPSA-IVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRS 701
Cdd:PTZ00243 1458 RALLKKGSGfILMDEATANIDPALDRQIQATVMSAfsAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
476-697 |
1.06e-25 |
|
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: 106.67 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALY---KVSEGQILINNKNINDYDYHSLRTS 552
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPngsg---kstLLRALAgllKPSSGEVLLDGRDLASLSRRELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKL-FSGSISDNISM---------SKDNHDDLKVIDAA-KKSGIlEDILNSPMgfetiisesgNNFSGGQRQR 621
Cdd:COG1120 77 IAYVPQEPPApFGLTVRELVALgryphlglfGRPSAEDREAVEEAlERTGL-EHLADRPV----------DELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLfteRH-IE--NTLKELNITQ---IIIA-HRLR-TIQNADKIIYLEDGMIKEIGTH 693
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDL---AHqLEvlELLRRLARERgrtVVMVlHDLNlAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 446631050 694 EQLL 697
Cdd:COG1120 223 EEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
479-691 |
1.71e-25 |
|
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: 103.67 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQ 558
Cdd:cd03214 3 ENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 esklfsgsisdnismskdnhddlkvidAAKKSGIlEDILNSPMgfetiisesgNNFSGGQRQRLLVARALYQEPSAIVFD 638
Cdd:cd03214 81 ---------------------------ALELLGL-AHLADRPF----------NELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 639 EATSHLDLFTERHIENTLKEL----NITQIIIAHRL-RTIQNADKIIYLEDGMIKEIG 691
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLarerGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
13-132 |
2.78e-25 |
|
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: 101.35 E-value: 2.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 13 QMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCIIQWGNNH 92
Cdd:cd02420 6 QMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYKKDLEALREVSLPAIVFWNFNH 85
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446631050 93 FVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFALQF 132
Cdd:cd02420 86 FLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVVLTM 125
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
493-642 |
3.63e-25 |
|
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: 101.96 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSG-SISDNI 571
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 572 SMS------KDNHDDLKVIDAAKKSGILEDIlnspmgfETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATS 642
Cdd:pfam00005 81 RLGlllkglSKREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
476-699 |
4.42e-25 |
|
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: 109.61 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSK---YILKDLNFTIKQGEKVAIVGPSgsgkssiskLLLALYKVSEGQILINNKNINDYDYHS---L 549
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESgsgkstlarLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 RTSIGTVLQ--ESKLFSG-SISDNISMSKDNHDDL-------KVIDAAKKSGILEDILN-SPmgFEtiisesgnnFSGGQ 618
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRmTVGDIIAEPLRLHGLLsraerreRVAELLERVGLPPDLADrYP--HE---------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTH 693
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....*.
gi 446631050 694 EQLLKN 699
Cdd:COG1123 490 EEVFAN 495
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
13-127 |
5.72e-25 |
|
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: 100.15 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 13 QMESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCIIQWGNNH 92
Cdd:cd02259 1 GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLPALLLWKQGH 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 446631050 93 FVVLERIKKQSYIIVDPNR-GKIEVPQDEFKQKYSG 127
Cdd:cd02259 81 FVILYGADKGQVLIADPLEeGPVTLSESELEERWTG 116
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
477-687 |
7.81e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 103.00 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 477 KFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDydyhsLRTSIGTV 556
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 557 LQESKL---FSGSISDNISMSKDNH---------DDLKVIDAAKKSGILEDILNSPMGfetiisesgnNFSGGQRQRLLV 624
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYGHkglfrrlskADKAKVDEALERVGLSELADRQIG----------ELSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
476-698 |
2.48e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.56 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQE-SKLFSGS-ISDNISMSKDNH----DDL--KVIDAAKKSGILEDILNSPmgfetiisesgNNFSGGQRQRLLVARA 627
Cdd:PRK13635 86 VFQNpDNQFVGAtVQDDVAFGLENIgvprEEMveRVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 628 LYQEPSAIVFDEATSHLD-------LFTERHIENtlkELNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:PRK13635 155 LALQPDIIILDEATSMLDprgrrevLETVRQLKE---QKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
476-699 |
3.05e-24 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 101.99 E-value: 3.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:cd03295 1 IEFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNISM-SKDNHDDLKVIDaAKKSGILEDILNSPMGF-ETIISEsgnnFSGGQRQRLLVARALYQEP 632
Cdd:cd03295 80 VIQQIGLFPHmTVEENIALvPKLLKWPKEKIR-ERADELLALVGLDPAEFaDRYPHE----LSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 633 SAIVFDEATSHLDLFTERHIENTL----KELNITQIIIAHRL-RTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
476-698 |
4.81e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.14 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQE-SKLFSGSISD-NISMSKDNH----DDL--KVIDAAKKSGILEDILNSPmgfetiisesgNNFSGGQRQRLLVARA 627
Cdd:PRK13648 88 VFQNpDNQFVGSIVKyDVAFGLENHavpyDEMhrRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 628 LYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVksehNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
477-685 |
5.06e-24 |
|
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: 98.86 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 477 KFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTV 556
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 557 LQesklfsgsisdnismskdnhddlkvidaakksgiledilnspmgfetiisesgnnFSGGQRQRLLVARALYQEPSAIV 636
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446631050 637 FDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQNA-DKIIYLEDG 685
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
479-688 |
5.47e-24 |
|
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: 100.41 E-value: 5.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDyhsLRTSIGTVLQ 558
Cdd:cd03226 3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 ES--KLFSGSISDNISMSKDNHDDlkviDAAKKSGILEDilnspMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIV 636
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDA----GNEQAETVLKD-----LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 637 FDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDGMIK 688
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAaqgKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
476-701 |
6.38e-24 |
|
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: 101.09 E-value: 6.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHsLRTSIGT 555
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNISMSKDNHDdLKVIDAAKKsgiLEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSA 634
Cdd:COG4555 79 LPDERGLYDRlTVRENIRYFAELYG-LFDEELKKR---IEELIEL-LGLEEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 635 IVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKNRS 701
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
162-442 |
1.43e-23 |
|
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: 101.36 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNsdinklNSFGWLIIIFSISFVLMSLLRGISIALLQK---SLDLSIMND 238
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAG------GSSGGLLALLVALFLLQAVLSALSSYLLGRtgeRVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANS-AVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILF 317
Cdd:cd18551 75 LWRRLLRLPVSFFDRRRSGDLVSRVTNdTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 318 VNANVIRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSV 396
Cdd:cd18551 155 PLGRRIRKASKR-AQDALgELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLA 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446631050 397 PLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18551 234 LLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQL 279
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
476-689 |
2.16e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 99.35 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQ--FSKYILKDLNFTIKQGEKVAIVGPSgsgkssiskLLLALYKVSEGQILINNKNINDYDYHSL---- 549
Cdd:COG1136 5 LELRNLTKSYGTgeGEVTALRGVSLSIEAGEFVAIVGPSgsgkstllnILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 RTSIGTVLQESKLFSG-SISDNISM------SKDNHDDLKVIDAAKKSGiLEDILNS-PmgfetiisesgNNFSGGQRQR 621
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllagVSRKERRERARELLERVG-LGDRLDHrP-----------SQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQNADKIIYLEDGMIKE 689
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrelgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
321-706 |
3.50e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 105.83 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 321 NVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKEL---ESSQRLNIFQAvihtitgFFQVSVP 397
Cdd:PLN03232 462 RKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELswfRKAQLLSAFNS-------FILNSIP 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 398 LLVLWV--GGHALINGEITLGTliAFSSIAGSYI--TPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHSIK 473
Cdd:PLN03232 535 VVVTLVsfGVFVLLGGDLTPAR--AFTSLSLFAVlrSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGA 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYN-QFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILInnknindydyhsLRTS 552
Cdd:PLN03232 613 PAISIKNGYFSWDsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGS 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSGSISDNISMSKDNHDDL--KVIDAakkSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQ 630
Cdd:PLN03232 681 VAYVPQVSWIFNATVRENILFGSDFESERywRAIDV---TALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYS 757
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 631 EPSAIVFDEATSHLDLFTERHIENTLKELNI---TQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNL 706
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVAHQVFDSCMKDELkgkTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
476-687 |
4.35e-23 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 97.86 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHS---LRTS 552
Cdd:cd03292 1 IEFINVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSG-SISDNISMSkdnhddLKVI-----DAAKKSGILEDILnspmGFETIISESGNNFSGGQRQRLLVAR 626
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFA------LEVTgvpprEIRKRVPAALELV----GLSHKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 627 ALYQEPSAIVFDEATSHLDLFTERHIENTLKELNI--TQIIIAHRLRTIQNADK--IIYLEDGMI 687
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
161-452 |
7.23e-23 |
|
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: 99.46 E-value: 7.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 161 RFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFM 240
Cdd:cd18545 1 KLLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 241 KKMFHLPYSFFDNRSSGDLLFRA----NSavfIRDIISTTMITIFIDLLLIITYTAVM--INFSLDLSLLllslsmllAV 314
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVindvNS---LSDLLSNGLINLIPDLLTLVGIVIIMfsLNVRLALVTL--------AV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 315 --ILFVNANVIRKMTKKNIQDKVNTQAVLT----ENMYNIVDIKSLGLEKKRLSLW---SGNYSKELESSQRLN-IFQAV 384
Cdd:cd18545 150 lpLLVLVVFLLRRRARKAWQRVRKKISNLNaylhESISGIRVIQSFAREDENEEIFdelNRENRKANMRAVRLNaLFWPL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 385 IHTITGFFQVsvplLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18545 230 VELISALGTA----LVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
476-699 |
1.23e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 97.80 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLAL---------YKVsEGQILINNKNIND--Y 544
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPsgcg---kstLLRCLnrmndlipgARV-EGEILLDGEDIYDpdV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 545 DYHSLRTSIGTVLQESKLFSGSISDNISM--------SKDNHDDLkVIDAAKKSGILE---DILNspmgfetiisESGNN 613
Cdd:COG1117 86 DVVELRRRVGMVFQKPNPFPKSIYDNVAYglrlhgikSKSELDEI-VEESLRKAALWDevkDRLK----------KSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 614 FSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLrtiQNA----DKIIYLEDGMI 687
Cdd:COG1117 155 LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELkkDYTIVIVTHNM---QQAarvsDYTAFFYLGEL 231
|
250
....*....|..
gi 446631050 688 KEIGTHEQLLKN 699
Cdd:COG1117 232 VEFGPTEQIFTN 243
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
162-432 |
1.74e-22 |
|
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: 97.71 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDIN--KLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDF 239
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 240 MKKMFHLPYSFFDNRSSGDLLFR-ANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRlTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPI 432
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
476-698 |
3.07e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 96.29 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNINDyDYHSLRTSIGT 555
Cdd:COG1131 1 IEVRGLTKRYG--DKTALDGVSLTVEPGEIFGLLGPngagktttirMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNISMS------KDNHDDLKVIDAAKKSGiLEDILNSPMGfetiisesgnNFSGGQRQRLLVARAL 628
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFarlyglPRKEARERIDELLELFG-LTDAADRKVG----------TLSGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 629 YQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITqIIIA-HRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAaegKT-VLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
456-700 |
3.18e-22 |
|
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: 97.23 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 456 LRTKDEQEKSNVQAHSIKGDIKFENVNFKYNQfskyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQIl 535
Cdd:cd03291 20 LLEKAKQENNDRKHSSDDNNLFFSNLCLVGAP----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 536 innknindydYHSLRTSIGTvlQESKLFSGSISDNI--SMSKDNHDDLKVIDAAKksgILEDILNSPMGFETIISESGNN 613
Cdd:cd03291 95 ----------KHSGRISFSS--QFSWIMPGTIKENIifGVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGIT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 614 FSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHI-ENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEI 690
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLmaNKTRILVTSKMEHLKKADKILILHEGSSYFY 239
|
250
....*....|
gi 446631050 691 GTHEQLLKNR 700
Cdd:cd03291 240 GTFSELQSLR 249
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
476-698 |
5.14e-22 |
|
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: 95.64 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVN--FKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSI 553
Cdd:COG1124 2 LEVRNLSvsYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESklfSGS------ISDNIS-----MSKDNHDDlKVIDAAKKSGILEDILNS-PmgfetiisesgNNFSGGQRQR 621
Cdd:COG1124 82 QMVFQDP---YASlhprhtVDRILAeplriHGLPDREE-RIAELLEQVGLPPSFLDRyP-----------HQLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQL 696
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLreerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
..
gi 446631050 697 LK 698
Cdd:COG1124 227 LA 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
476-699 |
5.33e-22 |
|
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: 95.34 E-value: 5.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVN--FKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRT-- 551
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 552 -SIGTVLQESKLFSG-SISDNISMSkdnhddLKvIDAAKKSGILEDI--LNSPMGFETIISESGNNFSGGQRQRLLVARA 627
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALP------LE-IAGVPKAEIEERVleLLELVGLEDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 628 LYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINrelgLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
475-700 |
6.22e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.63 E-value: 6.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 475 DIKFENVNFKYNQ---FSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNI----NDYDYH 547
Cdd:PRK13634 2 DITFQKVEHRYQYktpFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 548 SLRTSIGTVLQ--ESKLFSGSISDNISMSKDNHdDLKVIDAAKKS-------GILEDILN-SPmgFEtiisesgnnFSGG 617
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNF-GVSEEDAKQKAremielvGLPEELLArSP--FE---------LSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 618 QRQRLLVARALYQEPSAIVFDEATSHLD---------LFTERHientlKELNITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemmeMFYKLH-----KEKGLTTVLVTHSMEDAARyADQIVVMHKGTV 224
|
250
....*....|...
gi 446631050 688 KEIGTHEQLLKNR 700
Cdd:PRK13634 225 FLQGTPREIFADP 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
476-698 |
7.00e-22 |
|
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: 95.05 E-value: 7.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNINDYDYH---SLRTS 552
Cdd:COG1127 6 IEVRNLTKSFG--DRVVLDGVSLDVPRGEILAIIGGsgsgksvllkLIIGLLRPDSGEILVDGQDITGLSEKelyELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSG-SISDNI--------SMSKDNHDDLkVIDAAKKSGiLEDILN-SPmgfetiiSEsgnnFSGGQRQRL 622
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVafplrehtDLSEAEIREL-VLEKLELVG-LPGAADkMP-------SE----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLL 697
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRdelgLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230
|
.
gi 446631050 698 K 698
Cdd:COG1127 231 A 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
314-697 |
8.31e-22 |
|
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: 101.18 E-value: 8.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 314 VILFVNANVIRKMTKKNIQDKvntQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELES--SQRLNIFQ--AVIHTIT 389
Cdd:TIGR00957 467 MVLMVPLNAVMAMKTKTYQVA---HMKSKDNRIKLMNEILNGIKVLKLYAWELAFLDKVEGirQEELKVLKksAYLHAVG 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 390 GFFQVSVPLLV----LWVggHALINGEITLGTLIAFSSIAGSYIT--PIVSVSNNYTQLISLGSYFSRIKDVLrTKDEQE 463
Cdd:TIGR00957 544 TFTWVCTPFLValitFAV--YVTVDENNILDAEKAFVSLALFNILrfPLNILPMVISSIVQASVSLKRLRIFL-SHEELE 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 464 KSNVQAHSIK----GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQIlinnk 539
Cdd:TIGR00957 621 PDSIERRTIKpgegNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV----- 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 540 nindydyhSLRTSIGTVLQESKLFSGSISDNISMSKDNHDDL--KVIDAAkksGILEDILNSPMGFETIISESGNNFSGG 617
Cdd:TIGR00957 696 --------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYyqQVLEAC---ALLPDLEILPSGDRTEIGEKGVNLSGG 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 618 QRQRLLVARALYQEPSAIVFDEATSHLDLFTERHI-------ENTLKelNITQIIIAHRLRTIQNADKIIYLEDGMIKEI 690
Cdd:TIGR00957 765 QKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehvigpEGVLK--NKTRILVTHGISYLPQVDVIIVMSGGKISEM 842
|
....*..
gi 446631050 691 GTHEQLL 697
Cdd:TIGR00957 843 GSYQELL 849
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
476-687 |
1.19e-21 |
|
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: 92.46 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNINDyDYHSLRTSIGT 555
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPngagkttlikIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFsgsisdnismskdnhDDLKVIDAAKksgiledilnspmgfetiisesgnnFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03230 78 LPEEPSLY---------------ENLTVRENLK-------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 636 VFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
476-689 |
2.52e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.19 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNINDYDYHS---LRTS 552
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPsgagkstllkLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSG-SISDNISMSkdnhddLKVIDAAKKSgILEDILnspmgfETI----ISESGNNF----SGGQRQRLL 623
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALP------LRVTGKSRKE-IRRRVR------EVLdlvgLSDKAKALphelSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 624 VARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITqIIIA-HRLRTIQNADK-IIYLEDGMIKE 689
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINrrgTT-VLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
476-698 |
2.92e-21 |
|
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: 93.34 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNI---NDYDYHSLRTS 552
Cdd:cd03261 1 IELRGLTKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSG-SISDNISMSKDNHDDL--KVIDAakksgILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALY 629
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIRE-----IVLEKLEA-VGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 630 QEPSAIVFDEATSHLDLFTERHIENTL----KELNITQIIIAHRLRTI-QNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
476-699 |
6.29e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 92.36 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFskYILKDLNFTIKQGEKVAIVGPsgsgkssisklLL----ALYKVSEGQILINNKNIND--YDYHSL 549
Cdd:COG1126 2 IEIENLHKSFGDL--EVLKGISLDVEKGEVVVIIGPsgsg----kstLLrcinLLEEPDSGTITVDGEDLTDskKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 RTSIGTVLQESKLFSG-SISDNIS--------MSKDnhddlkviDAAKKSgilEDILNSpMGfetiISESGNNF----SG 616
Cdd:COG1126 76 RRKVGMVFQQFNLFPHlTVLENVTlapikvkkMSKA--------EAEERA---MELLER-VG----LADKADAYpaqlSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 617 GQRQRLLVARALYQEPSAIVFDEATSHLD--LFTErhIENTLKEL---NITQIIIAHRL---RTIqnADKIIYLEDGMIK 688
Cdd:COG1126 140 GQQQRVAIARALAMEPKVMLFDEPTSALDpeLVGE--VLDVMRDLakeGMTMVVVTHEMgfaREV--ADRVVFMDGGRIV 215
|
250
....*....|.
gi 446631050 689 EIGTHEQLLKN 699
Cdd:COG1126 216 EEGPPEEFFEN 226
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
162-432 |
7.95e-21 |
|
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: 93.26 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMK 241
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 242 KMFHLPYSFFDNRSSGDLLFRANSAV-FIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNA 320
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVdTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 321 NVIRKMTKKnIQD---KVNTqaVLTENMYNIVDIKSLGLEK----KRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQ 393
Cdd:cd18542 161 KKVRPAFEE-IREqegELNT--VLQENLTGVRVVKAFAREDyeieKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQI 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 446631050 394 VsvplLVLWVGGHALINGEITLGTLIAFSSIAGSYITPI 432
Cdd:cd18542 238 V----LVLWVGGYLVINGEITLGELVAFISYLWMLIWPV 272
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
493-686 |
1.36e-20 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 90.85 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL----RTSIGTVLQESKLFSGSIS 568
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 569 DNISM-SKDNHDDLK-VIDAAKksgILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDL 646
Cdd:cd03290 97 ENITFgSPFNKQRYKaVTDACS---LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446631050 647 FTERHI--ENTLKELN---ITQIIIAHRLRTIQNADKIIYLEDGM 686
Cdd:cd03290 174 HLSDHLmqEGILKFLQddkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
476-691 |
1.66e-20 |
|
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: 90.27 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHslRTSIGT 555
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNIS-------MSKDNHDDlKVIDAAKKSGILEDILNSPmgfETIisesgnnfSGGQRQRLLVARA 627
Cdd:cd03259 77 VFQDYALFPHlTVAENIAfglklrgVPKAEIRA-RVRELLELVGLEGLLNRYP---HEL--------SGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 628 LYQEPSAIVFDEATSHLD----LFTERHIENTLKELNITQIIIAHRLR-TIQNADKIIYLEDGMIKEIG 691
Cdd:cd03259 145 LAREPSLLLLDEPLSALDaklrEELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
161-445 |
2.89e-20 |
|
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: 91.81 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 161 RFFGLVFL-SIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGwLIIIFSISF-VLMSLLRGISIALLQKSLDLSIMND 238
Cdd:cd18783 2 RLFRDVAIaSLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLT-IGVVIALLFeGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:cd18783 81 TFDRLLSLPIDFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPL 398
Cdd:cd18783 161 FLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446631050 399 LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVsvsnnytQLISL 445
Cdd:cd18783 241 GVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLV-------QLAGL 280
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
162-442 |
1.04e-19 |
|
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: 90.17 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLnsfgWLIIIFsisFVLMSLLRGISI---ALLQKSLDLSIMND 238
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEAL----LLVPLA---IIGLFLLRGLASylqTYLMAYVGQRVVRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMF----HLPYSFFDNRSSGDLLFRANSAV-FIRDIISTTMITIFIDLLLIITYTAVM--INFSLdlsllllslsml 311
Cdd:cd18552 74 LRNDLFdkllRLPLSFFDRNSSGDLISRITNDVnQVQNALTSALTVLVRDPLTVIGLLGVLfyLDWKL------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 312 lAVILFV----NANVIRKMTKK------NIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRlslwSGNYSKELESSQRLNI 380
Cdd:cd18552 142 -TLIALVvlplAALPIRRIGKRlrkisrRSQESMgDLTSVLQETLSGIRVVKAFGAEDYE----IKRFRKANERLRRLSM 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 381 ----FQAVIHTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18552 217 kiarARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANL 282
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
476-691 |
1.62e-19 |
|
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: 87.70 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYD-YHSlrtSIG 554
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPpKDR---DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQESKLFSG-SISDNIS-------MSKDNHDDlKVIDAAKKSGIledilnspmgfETIISESGNNFSGGQRQRLLVAR 626
Cdd:cd03301 76 MVFQNYALYPHmTVYDNIAfglklrkVPKDEIDE-RVREVAELLQI-----------EHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 627 ALYQEPSAIVFDEATSHLD------LFTErhIENTLKELNITQIIIAH-RLRTIQNADKIIYLEDGMIKEIG 691
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDaklrvqMRAE--LKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
476-699 |
2.31e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKY----NQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDY-DYHSLR 550
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQ--ESKLFSGSISDNISMSKDN------HDDLKVIDAAKKSGILEDILNSPmgfetiisesgNNFSGGQRQRL 622
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGPENlgippeEIRERVDESLKKVGMYEYRRHAP-----------HLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkygITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
gi 446631050 699 N 699
Cdd:PRK13633 234 E 234
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
476-696 |
2.31e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 88.64 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFS-KYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIG 554
Cdd:PRK13650 5 IEVKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQ--ESKLFSGSISDNISMSKDN----HDDLK--VIDAAKKSGILEDILNSPmgfetiisesgNNFSGGQRQRLLVAR 626
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGLENkgipHEEMKerVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 627 ALYQEPSAIVFDEATSHLD----LFTERHIENTLKELNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
476-699 |
2.83e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.57 E-value: 2.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQ---FSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIND--YDYHSLR 550
Cdd:PRK13637 3 IKIENLTHIYMEgtpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQ--ESKLFSGSISDNISMSKDN----HDDLK--VIDAAKKSGIledilnspmGFETIISESGNNFSGGQRQRL 622
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINlglsEEEIEnrVKRAMNIVGL---------DYEDYKDKSPFELSGGQKRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLL 697
Cdd:PRK13637 154 AIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREVF 233
|
..
gi 446631050 698 KN 699
Cdd:PRK13637 234 KE 235
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
314-696 |
2.93e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 93.05 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 314 VILFVNANVIRKMTKKNIQ--DKVNTQAVLTENMY-NIVDIKSLGLEKKRLSLWSGNYSKELESSQR---LNIFQAVIHT 387
Cdd:TIGR01271 233 LLALFQACLGQKMMPYRDKraGKISERLAITSEIIeNIQSVKAYCWEEAMEKIIKNIRQDELKLTRKiayLRYFYSSAFF 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 388 ITGFFQVsvpllVLWVGGHALINGeITLGTLiaFSSIagSY-ITPIVSVSNNYTQLI-----SLGSyFSRIKDVLR---- 457
Cdd:TIGR01271 313 FSGFFVV-----FLSVVPYALIKG-IILRRI--FTTI--SYcIVLRMTVTRQFPGAIqtwydSLGA-ITKIQDFLCkeey 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 458 -------TKDEQEKSNVQAHSIKG------DIKFENVNFK---------YNQFSKY---ILKDLNFTIKQGEKVAIVGPS 512
Cdd:TIGR01271 382 ktleynlTTTEVEMVNVTASWDEGigelfeKIKQNNKARKqpngddglfFSNFSLYvtpVLKNISFKLEKGQLLAVAGST 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 513 GSGKSSISKLLLALYKVSEGQIlinnknindydYHSLRTSIGTvlQESKLFSGSISDNI--SMSKDNHDDLKVIDAAKks 590
Cdd:TIGR01271 462 GSGKSSLLMMIMGELEPSEGKI-----------KHSGRISFSP--QTSWIMPGTIKDNIifGLSYDEYRYTSVIKACQ-- 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 591 gILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHI-ENTLKEL--NITQIIIA 667
Cdd:TIGR01271 527 -LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLmsNKTRILVT 605
|
410 420
....*....|....*....|....*....
gi 446631050 668 HRLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:TIGR01271 606 SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
476-696 |
3.22e-19 |
|
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: 87.29 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHslRTSIGT 555
Cdd:cd03300 1 IELENVSKFYGGFV--ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNIS----MSKDNHDDLK--VIDAAKKSGILEDILNSPmgfetiisesgNNFSGGQRQRLLVARAL 628
Cdd:cd03300 77 VFQNYALFPHlTVFENIAfglrLKKLPKAEIKerVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 629 YQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAH-RLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKrlqkELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
164-442 |
9.20e-19 |
|
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: 87.15 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 164 GLVFLsIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFsisFVLMSLLRGISIALLQKSLDlSIMNDFMKKM 243
Cdd:cd18576 1 GLILL-LLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGL---FLLQAVFSFFRIYLFARVGE-RVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 244 F----HLPYSFFDNRSSGDLLFR-ANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFV 318
Cdd:cd18576 76 YrhlqRLPLSFFHERRVGELTSRlSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 319 NANVIRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSL---GLEKKRlslwsgnYSKELESSQRLNIFQAVIHT------I 388
Cdd:cd18576 156 FGRRIRKLSKK-VQDELaEANTIVEETLQGIRVVKAFtreDYEIER-------YRKALERVVKLALKRARIRAlfssfiI 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 389 TGFFQVSVplLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18576 228 FLLFGAIV--AVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQL 279
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
388-699 |
9.67e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 91.34 E-value: 9.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 388 ITGFFQVSVPLLVLWV--GGHALINGEITLGTliAFSSIAGSYIT--PIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQE 463
Cdd:PLN03130 525 FNSFILNSIPVLVTVVsfGVFTLLGGDLTPAR--AFTSLSLFAVLrfPLFMLPNLITQAVNANVSLKRLEELLLAEERVL 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 464 KSNVQAHSIKGDIKFENVNFKYN-QFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLA-LYKVSEGQILInnkni 541
Cdd:PLN03130 603 LPNPPLEPGLPAISIKNGYFSWDsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI----- 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 542 ndydyhslRTSIGTVLQESKLFSGSISDNISMSKDNHDDL--KVIDAakkSGILEDILNSPMGFETIISESGNNFSGGQR 619
Cdd:PLN03130 678 --------RGTVAYVPQVSWIFNATVRDNILFGSPFDPERyeRAIDV---TALQHDLDLLPGGDLTEIGERGVNISGGQK 746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 620 QRLLVARALYQEPSAIVFDEATSHLDLFTERHI-ENTLK-EL-NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:PLN03130 747 QRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKdELrGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEEL 826
|
...
gi 446631050 697 LKN 699
Cdd:PLN03130 827 SNN 829
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
476-687 |
1.49e-18 |
|
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: 85.70 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTS--- 552
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSG-SISDNISMSK--------------DNHDDLKVIDAAKKSGILEDILNspmgfetiiseSGNNFSGG 617
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRlgrrstwrslfglfPKEEKQRALAALERVGLLDKAYQ-----------RADQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 618 QRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTI-QNADKIIYLEDGMI 687
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreegITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
476-703 |
1.57e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 85.29 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYD-YHSLRTSIG 554
Cdd:cd03218 1 LRAENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQESKLFSG-SISDNISMSKDNHDDLKVIDAAKKSGILEDilnspMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03218 79 YLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELLEE-----FHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 634 AIVFDEATSHLDLFTERHIENT---LKELNITQIIIAHRLR-TIQNADKIIYLEDGMIKEIGTHEQLLKN---RSYY 703
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIikiLKDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANelvRKVY 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
474-696 |
1.79e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.44 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQFskYILKDLNFTIKQGEKVAIVGPsgsgkssiskLL--LA-LYKVSEGQILINNKNINDydyhsLR 550
Cdd:COG3839 2 ASLELENVSKSYGGV--EALKDIDLDIEDGEFLVLLGPsgcg---kstLLrmIAgLEDPTSGEILIGGRDVTD-----LP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TS---IGTVLQESKLF-SGSISDNIS-------MSKDNHDDlKVIDAAKKSGIlEDILNS-PmgfetiisesgNNFSGGQ 618
Cdd:COG3839 72 PKdrnIAMVFQSYALYpHMTVYENIAfplklrkVPKAEIDR-RVREAAELLGL-EDLLDRkP-----------KQLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLD--LFTE--RHIENTLKELNITQIIIAH------RLrtiqnADKIIYLEDGMIK 688
Cdd:COG3839 139 RQRVALGRALVREPKVFLLDEPLSNLDakLRVEmrAEIKRLHRRLGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQ 213
|
....*...
gi 446631050 689 EIGTHEQL 696
Cdd:COG3839 214 QVGTPEEL 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
476-696 |
1.83e-18 |
|
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: 85.08 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyiLKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINdyDYHSLRTSIGT 555
Cdd:cd03296 3 IEVRNVSKRFGDFVA--LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNISMSKDNHDDLKVIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSA 634
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKL-VQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 635 IVFDEATSHLDLFTERHIENTLKEL----NITQIIIAH-RLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLhdelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
377-685 |
2.98e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.71 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 377 RLNIFQavihtiTGFFQVS--VPLLVLwvgGHALINGEITLGTLI----AFSSIAGSYITPIvsvsNNYTQLISLGSYFS 450
Cdd:COG4178 267 NLTFFT------TGYGQLAviFPILVA---APRYFAGEITLGGLMqaasAFGQVQGALSWFV----DNYQSLAEWRATVD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 451 RI---KDVLRTKDEQEKSNVQAHSIKGD-IKFENVNFkYNQFSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLL--L 524
Cdd:COG4178 334 RLagfEEALEAADALPEAASRIETSEDGaLALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPsgsg---kstLLraI 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 525 A-LYKVSEGQILinnknindydyhslRTSIGTVL---QESKLFSGSISDNIS--MSKDNHDDLKVIDAAKKSGiLEDILN 598
Cdd:COG4178 410 AgLWPYGSGRIA--------------RPAGARVLflpQRPYLPLGTLREALLypATAEAFSDAELREALEAVG-LGHLAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 599 SpmgfetiISES---GNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTI 673
Cdd:COG4178 475 R-------LDEEadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLA 547
|
330
....*....|..
gi 446631050 674 QNADKIIYLEDG 685
Cdd:COG4178 548 AFHDRVLELTGD 559
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
476-699 |
7.91e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.22 E-value: 7.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIND--YDYHSLRTSI 553
Cdd:PRK09493 2 IEFKNVSKHFGPTQ--VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSIS-DNIS--------MSKDNHDDLkVIDAAKKSGILEDILNSPmgfetiiSEsgnnFSGGQRQRLLV 624
Cdd:PRK09493 80 GMVFQQFYLFPHLTAlENVMfgplrvrgASKEEAEKQ-ARELLAKVGLAERAHHYP-------SE----LSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 625 ARALYQEPSAIVFDEATSHLDlfTE-RH----IENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALD--PElRHevlkVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
.
gi 446631050 699 N 699
Cdd:PRK09493 226 N 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
476-694 |
8.06e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 83.52 E-value: 8.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINN------KNINDYDYHSL 549
Cdd:COG4161 3 IQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 RTSIGTVLQESKLFSG-SISDNISMSKdnhddLKVIDAAKKSGI-----------LEDILNS-PMgfetiisesgnNFSG 616
Cdd:COG4161 81 RQKVGMVFQQYNLWPHlTVMENLIEAP-----CKVLGLSKEQARekamkllarlrLTDKADRfPL-----------HLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 617 GQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRL---RTIqnADKIIYLEDGMIKEI 690
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSqtgITQVIVTHEVefaRKV--ASQVVYMEKGRIIEQ 222
|
....
gi 446631050 691 GTHE 694
Cdd:COG4161 223 GDAS 226
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
159-452 |
1.46e-17 |
|
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: 83.81 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSfgwLIIIFSISFVLMSLLRGISIALLQKS---LDLSI 235
Cdd:cd18586 1 RRVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLG---LTLGMVVLLAFDGLLRQVRSRILQRVglrLDVEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 236 MNDFMKKMFHLPYsffDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVI 315
Cdd:cd18586 78 GRRVFRAVLELPL---ESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 316 LFVNANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVS 395
Cdd:cd18586 155 AWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 396 VPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18586 235 LQSLILGVGAYLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQAYERL 291
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
476-704 |
2.79e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 82.73 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYD-YHSLRTSIG 554
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQ--ESKLFSGSISDNISMSKDNHdDLKVIDAAKKSgileDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEP 632
Cdd:PRK13644 81 IVFQnpETQFVGRTVEEDLAFGPENL-CLPPIEIRKRV----DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 633 SAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYY 704
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
476-694 |
3.00e-17 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.60 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINN------KNINDYDYHSL 549
Cdd:PRK11124 3 IQLNGINCFYG--AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 RTSIGTVLQESKLFSG-SISDNI--------SMSKDnhddlKVIDAAKKsgILEDI-LNS-----PMgfetiisesgnNF 614
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHlTVQQNLieapcrvlGLSKD-----QALARAEK--LLERLrLKPyadrfPL-----------HL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRL---RTIqnADKIIYLEDGMIK 688
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELaetGITQVIVTHEVevaRKT--ASRVVYMENGHIV 220
|
....*.
gi 446631050 689 EIGTHE 694
Cdd:PRK11124 221 EQGDAS 226
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
6-132 |
3.46e-17 |
|
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: 80.04 E-value: 3.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 6 KRVKFVEQMESVECGLACFAMIANYH-NIKLS----LNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAI 80
Cdd:COG3271 41 RFRNVVRQQYDYSCGAAALATLLNYHyGRPVSeaevLEGMLTHGDQRRRGFSLLDMKRYLEALGLRADGYRLTLDDLAQL 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 81 SLPCII---QWGNNHFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFALQF 132
Cdd:COG3271 121 GIPAIVlinLGGYKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVLFV 175
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
478-685 |
6.18e-17 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 79.52 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 478 FENVNF----KYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSiskLL--LALYKVSE---GQILINNKNIndyDYHS 548
Cdd:cd03213 6 FRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKST---LLnaLAGRRTGLgvsGEVLINGRPL---DKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQESKLfsgsisdnismskdnHDDLKVID----AAKKSGIledilnspmgfetiisesgnnfSGGQRQRLLV 624
Cdd:cd03213 80 FRKIIGYVPQDDIL---------------HPTLTVREtlmfAAKLRGL----------------------SGGERKRVSI 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRT--IQNADKIIYLEDG 685
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLadtGRTIICSIHQPSSeiFELFDKLLLLSQG 188
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
476-699 |
6.58e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 6.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKL---LLALYKVSEGQILINNKNINDYDYHSLRTS 552
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQ--ESKLFSGSISDNISMSKDNhddlKVIDAAKKSGILEDILNSPMGFETIISESGnNFSGGQRQRLLVARALYQ 630
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGLEN----RAVPRPEMIKIVRDVLADVGMLDYIDSEPA-NLSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 631 EPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLkkknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
480-699 |
1.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.89 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 480 NVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNInDYDYHSL---RTSIGTV 556
Cdd:PRK13639 6 DLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 557 LQ--ESKLFSGSISD-------NISMSKDNHDDlKVIDAAKKSGILedilnspmGFEtiiSESGNNFSGGQRQRLLVARA 627
Cdd:PRK13639 84 FQnpDDQLFAPTVEEdvafgplNLGLSKEEVEK-RVKEALKAVGME--------GFE---NKPPHHLSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 628 LYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQ-NADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkegITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
8-132 |
1.31e-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, which contains Colicin V perocessing peptidase.
Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 76.61 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 8 VKFVEQMESVECGLACFAMIAN-YHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLP--- 83
Cdd:cd02424 1 MKIIKQTDLNDCGIAVIQMLYNhYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFLELKNKfii 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446631050 84 CIIQWGNNHFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFALQF 132
Cdd:cd02424 81 LLKSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIITV 129
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
167-452 |
4.58e-16 |
|
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: 79.14 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 167 FLSIIIQGLMT-VIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKMFH 245
Cdd:cd18557 2 LLFLLISSAAQlLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 246 LPYSFFDNRSSGDLLFRANSAV-FIRDIISTTMITIF---------IDLLLIITY--TAVMINFSldlsllllslsmlla 313
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTsVLQSAVTDNLSQLLrnilqviggLIILFILSWklTLVLLLVI--------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 314 VILFVNANV----IRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTI 388
Cdd:cd18557 147 PLLLIASKIygryIRKLSKE-VQDALaKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 389 TGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18557 226 TSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
476-699 |
4.68e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.12 E-value: 4.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSK--YILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNKNINDYDYHSLRT-- 551
Cdd:COG1135 2 IELENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYsgagkstlirCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 552 -SIGTVLQESKLFSG-SISDNISMSkdnhddLKVIDAAKKS------------GiLEDILNS-PmgfetiisesgNNFSG 616
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENVALP------LEIAGVPKAEirkrvaellelvG-LSDKADAyP-----------SQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 617 GQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIG 691
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKdinrELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223
|
....*...
gi 446631050 692 THEQLLKN 699
Cdd:COG1135 224 PVLDVFAN 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
476-699 |
5.45e-16 |
|
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: 77.76 E-value: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyiLKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDyhSLRTSIGT 555
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP--PEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNIS------MSKDNHDDLKVIDAAKKSGIlEDILN-SPmgfETIisesgnnfSGGQRQRLLVARA 627
Cdd:cd03299 76 VPQNYALFPHmTVYKNIAyglkkrKVDKKEIERKVLEIAEMLGI-DHLLNrKP---ETL--------SGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 628 LYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
159-432 |
6.09e-16 |
|
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: 79.02 E-value: 6.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMND 238
Cdd:cd18571 1 KKLILQLLLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANSAVFIRDIISTTMITIFIDLLLIITYTAVMI--NFSLDLSLLLLSLSMLLAVIL 316
Cdd:cd18571 81 FLIKLMRLPISFFDTKMTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAyyNLTIFLIFLIGSVLYILWILL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 317 FVnaNVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELE-SSQRLNIFQaVIHTITGFFQVS 395
Cdd:cd18571 161 FL--KKRKKLDYKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKiNIKSLKLDQ-YQQIGALFINQL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 446631050 396 VPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPI 432
Cdd:cd18571 238 KNILITFLAAKLVIDGEITLGMMLAIQYIIGQLNSPI 274
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
159-444 |
6.19e-16 |
|
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: 79.06 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLlrgISIALLQKsLDLSIMND 238
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVF---LFIRLAGK-IEMGVSYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFH----LPYSFFDNRSSGDLLFRANSAVF-IRDIIS----------TTMITIFIDLLLI------ITYTAVminf 297
Cdd:cd18540 77 LRKKAFEhlqtLSFSYFDKTPVGWIMARVTSDTQrLGEIISwglvdlvwgiTYMIGILIVMLILnwklalIVLAVV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 298 sldlsllllslsmllAVILFVNANVIRKMTKKNIQ-DKVNTQ--AVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELES 374
Cdd:cd18540 153 ---------------PVLAVVSIYFQKKILKAYRKvRKINSRitGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRA 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 375 SQRLNIFQAVIHTITGFFqVSVPL-LVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLIS 444
Cdd:cd18540 218 SVRAARLSALFLPIVLFL-GSIATaLVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQS 287
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
165-452 |
8.05e-16 |
|
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: 78.68 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 165 LVFLSIIIQGLMTVI-PLSTKWVTDNAFSNSDINKLNsfgWLIIIFSISFVLMSLLrgisiALLQKSLD----LSIMNDF 239
Cdd:cd18550 3 LVLLLILLSALLGLLpPLLLREIIDDALPQGDLGLLV---LLALGMVAVAVASALL-----GVVQTYLSarigQGVMYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 240 MKKMF----HLPYSFFDNRSSGDLLFRANSAVF-IRDIISTTMITIFIDLLLIITYTAVMInfsldlsllllSLSMLLAV 314
Cdd:cd18550 75 RVQLYahlqRMSLAFFTRTRTGEIQSRLNNDVGgAQSVVTGTLTSVVSNVVTLVATLVAML-----------ALDWRLAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 315 I------LFV-----NANVIRKMTKKNIQ--DKVNTQAVLTENMYNIVDIKSLGLEKKRLSlwsgNYSKELESSQRLNIF 381
Cdd:cd18550 144 LslvllpLFVlptrrVGRRRRKLTREQQEklAELNSIMQETLSVSGALLVKLFGREDDEAA----RFARRSRELRDLGVR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 382 QAVIH-----TITGFFQVsVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18550 220 QALAGrwffaALGLFTAI-GPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
476-700 |
8.52e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 78.35 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNInDYDYH---SLRTS 552
Cdd:PRK13636 6 LKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQ--ESKLFSGSISDNISMSKDN----HDDL--KVIDAAKKSGIlEDILNSPMgfetiisesgNNFSGGQRQRLLV 624
Cdd:PRK13636 84 VGMVFQdpDNQLFSASVYQDVSFGAVNlklpEDEVrkRVDNALKRTGI-EHLKDKPT----------HCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLFTERHI----ENTLKELNITQIIIAHRLRTIQ-NADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEImkllVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
|
.
gi 446631050 700 R 700
Cdd:PRK13636 233 K 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
141-708 |
9.17e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 81.88 E-value: 9.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 141 IIPKEKQENIILKYFKQHKGRFFGLVFL----------SIIIQGLMTVIPLSTKWVTDNafSNSDINKLNSFGWLII--- 207
Cdd:TIGR01271 846 NVFETTTWNTYLRYITTNRNLVFVLIFClviflaevaaSLLGLWLITDNPSAPNYVDQQ--HANASSPDVQKPVIITpts 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 208 ---IFSI------SFVLMSLLRGISialLQKSLdLSIMNDFMKKMFH----LPYSFFDNRSSGDLLFRANSAVFIRDIIS 274
Cdd:TIGR01271 924 ayyIFYIyvgtadSVLALGFFRGLP---LVHTL-LTVSKRLHEQMLHsvlqAPMAVLNTMKAGRILNRFTKDMAIIDDML 999
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 275 TTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVIL---FVNANVIRKMTKKNIQDKVNTQAVLTenMYNIVDI 351
Cdd:TIGR01271 1000 PLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLrayFLRTSQQLKQLESEARSPIFSHLITS--LKGLWTI 1077
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 352 KSLG-------LEKKRLSLWSGNYSKELESsqrLNIFQAVIHTITGFFQVSVPLLVlwVGGHALINGEI----TLGTLIa 420
Cdd:TIGR01271 1078 RAFGrqsyfetLFHKALNLHTANWFLYLST---LRWFQMRIDIIFVFFFIAVTFIA--IGTNQDGEGEVgiilTLAMNI- 1151
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 421 FSSIAGSYITPIV------SVSNNYtQLISLGSYFSRIKDvlRTKDEQEKSNV---QAHSIK-----GDIKFENVNFKYN 486
Cdd:TIGR01271 1152 LSTLQWAVNSSIDvdglmrSVSRVF-KFIDLPQEEPRPSG--GGGKYQLSTVLvieNPHAQKcwpsgGQMDVQGLTAKYT 1228
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 487 QFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKvSEGQILINNKNINDYDYHSLRTSIGTVLQESKLFSGS 566
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGT 1307
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNISmSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDL 646
Cdd:TIGR01271 1308 FRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 647 FTERHIENTLKEL--NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYYNLYS 708
Cdd:TIGR01271 1387 VTLQIIRKTLKQSfsNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMS 1450
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
492-698 |
1.13e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.99 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDydyHSLRT-SIGTVLQESKLFSG-SISD 569
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQrDICMVFQSYALFPHmSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 570 NIS----MSKDNHDDLK--VIDAAKksgiLEDIlnspMGFEtiiSESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSH 643
Cdd:PRK11432 98 NVGyglkMLGVPKEERKqrVKEALE----LVDL----AGFE---DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 644 LDLFTERHIENTLKEL----NITQIIIAH-RLRTIQNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:PRK11432 167 LDANLRRSMREKIRELqqqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
162-442 |
1.43e-15 |
|
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: 77.81 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINkLNSFGWLIIIFSISFVLMSLLRGISIALLQKsLDLSIM----N 237
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIVPGQGD-LQGLLLLALLYLGLLLLSFLLQYLQTYLLQK-LGQRIIydlrR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 238 DFMKKMFHLPYSFFDNRSSGDLLFRANSAV-FIRDIISTTMITIFIDLLLIITYTAVM--INFSLDLSLLLLslsmllAV 314
Cdd:cd18544 79 DLFSHIQRLPLSFFDRTPVGRLVTRVTNDTeALNELFTSGLVTLIGDLLLLIGILIAMflLNWRLALISLLV------LP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 315 ILFVNANVIRKMTKKNIQD------KVNTQavLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTI 388
Cdd:cd18544 153 LLLLATYLFRKKSRKAYREvreklsRLNAF--LQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 389 TGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18544 231 VELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNIL 284
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
474-703 |
2.18e-15 |
|
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: 76.82 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 474 GDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKvSEGQILINNKNINDYDYHSLRTSI 553
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFSGSISDNISmSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKE--LNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYY 703
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQafADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
476-671 |
3.53e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.97 E-value: 3.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFskYILKDLNFTIKQGEKVAIVGPSGSGKSSISKL------LLALYKVsEGQILINNKNIND--YDYH 547
Cdd:PRK14243 11 LRTENLNVYYGSF--LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRV-EGKVTFHGKNLYApdVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 548 SLRTSIGTVLQESKLFSGSISDNISMS------KDNHDDLkvIDAAKKSGILEDILNSPMgfetiiSESGNNFSGGQRQR 621
Cdd:PRK14243 88 EVRRRIGMVFQKPNPFPKSIYDNIAYGaringyKGDMDEL--VERSLRQAALWDEVKDKL------KQSGLSLSGGQQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLR 671
Cdd:PRK14243 160 LCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELkeQYTIIIVTHNMQ 211
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
166-437 |
3.92e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 76.42 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 166 VFLSIIIQGLMTVIPLSTKWVTDNAFSNSdiNKLNSFGWLIIIFSISFVLMSLLRGISIAL---LQKSLDLSIMNDFMKK 242
Cdd:cd18778 5 LLCALLSTLLGLVPPWLIRELVDLVTIGS--KSLGLLLGLALLLLGAYLLRALLNFLRIYLnhvAEQKVVADLRSDLYDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 243 MFHLPYSFFDNRSSGDLLFR-ANSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVILFVNAN 321
Cdd:cd18778 83 LQRLSLRYFDDRQTGDLMSRvINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 322 VIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGL---EKKRLSLWSGNYSKE-LESSQRLNIFQAVIHTITGFFQVsvp 397
Cdd:cd18778 163 KVRPRYRKVREALGELNALLQDNLSGIREIQAFGReeeEAKRFEALSRRYRKAqLRAMKLWAIFHPLMEFLTSLGTV--- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446631050 398 lLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSN 437
Cdd:cd18778 240 -LVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHG 278
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
490-697 |
4.28e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKV------SEGQILINNKNINDYDYHSLRTSIGTVLQESKLF 563
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIydskikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 564 SG-SISDNISMS------KDNHDDLKVIDAA-KKSGILEDI---LNSPmgfetiisesGNNFSGGQRQRLLVARALYQEP 632
Cdd:PRK14246 103 PHlSIYDNIAYPlkshgiKEKREIKKIVEEClRKVGLWKEVydrLNSP----------ASQLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 633 SAIVFDEATSHLDLFTERHIENTLKELN--ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLL 697
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKneIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
476-707 |
4.46e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 76.36 E-value: 4.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQ---FSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN----DYDYHS 548
Cdd:PRK13646 3 IRFDNVSYTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQ--ESKLFSGSISDNISMSKDNHD-DLKVIDAAKKSGILEdilnspMGFE-TIISESGNNFSGGQRQRLLV 624
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKmNLDEVKNYAHRLLMD------LGFSrDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQ----IIIAHRLRTI-QNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnktiILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
....*...
gi 446631050 700 RSYYYNLY 707
Cdd:PRK13646 237 KKKLADWH 244
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
163-432 |
6.32e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 76.01 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 163 FGLVFLSIIIqGLMTVIPLstKWVTDNAFSNSDINKLNSFGW--------LIIIFSISFVLMSLLRGIsIALLQKSLDLS 234
Cdd:cd18564 5 LLALLLETAL-RLLEPWPL--KVVIDDVLGDKPLPGLLGLAPllgpdplaLLLLAAAALVGIALLRGL-ASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 235 IMNDFM----KKMFH----LPYSFFDNRSSGDLLFRANSAV-FIRDIISTTMITIFIDLLLIITYTAVM--INFsldlsl 303
Cdd:cd18564 81 VGQRVVldlrRDLFAhlqrLSLSFHDRRRTGDLLSRLTGDVgAIQDLLVSGVLPLLTNLLTLVGMLGVMfwLDW------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 304 lllslsmLLAVI-------LFVnanVIRKMTKKnIQDKVNTQ--------AVLTENMYNIVDIKSLGLEKKRLSLWSGNY 368
Cdd:cd18564 155 -------QLALIalavaplLLL---AARRFSRR-IKEASREQrrregalaSVAQESLSAIRVVQAFGREEHEERRFAREN 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 369 SKELESSQRLNIFQAVIHTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPI 432
Cdd:cd18564 224 RKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPV 287
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
493-699 |
7.11e-15 |
|
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: 77.80 E-value: 7.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGpsgsgkssiskLLLALYKV--SEGQILINNKNINDYD------------------YHSL--R 550
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGesgs---gkstLGLALLRLipSEGEIRFDGQDLDGLSrralrplrrrmqvvfqdpFGSLspR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQEsklfsGSISDNISMSKDNHDDlKVIDAAKKSGILEDILNS-PmgfetiisesgNNFSGGQRQRLLVARALY 629
Cdd:COG4172 379 MTVGQIIAE-----GLRVHGPGLSAAERRA-RVAEALEEVGLDPAARHRyP-----------HEFSGGQRQRIAIARALI 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 630 QEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
495-699 |
7.96e-15 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 75.86 E-value: 7.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 495 DLNFTIKQGEKVAIVGpsgsgkssiskLLLALYK---VSEGQILINNKNINDYD-------------------YHSL--R 550
Cdd:COG0444 23 GVSFDVRRGETLGLVGesgsgkstlarAILGLLPppgITSGEILFDGEDLLKLSekelrkirgreiqmifqdpMTSLnpV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQES-KLFSGsisdnisMSKDNHDDlKVIDAAKKSGIL--EDILNS-PmgFEtiisesgnnFSGGQRQRLLVAR 626
Cdd:COG0444 103 MTVGDQIAEPlRIHGG-------LSKAEARE-RAIELLERVGLPdpERRLDRyP--HE---------LSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 627 ALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTI-QNADKII--YLedGMIKEIGTHEQLLKN 699
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLqrelGLAILFITHDLGVVaEIADRVAvmYA--GRIVEEGPVEELFEN 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
476-700 |
8.57e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFskyiLKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIgt 555
Cdd:COG3840 2 LRLDDLTYRYGDF----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSM-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNISMSKdnHDDLK--------VIDAAKKSGiLEDILNS-PmgfetiisesgNNFSGGQRQRLLVA 625
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGL--RPGLKltaeqraqVEQALERVG-LAGLLDRlP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 626 RALYQEPSAIVFDEATSHLD---------LFTERHientlKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQ 695
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDpalrqemldLVDELC-----RERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*
gi 446631050 696 LLKNR 700
Cdd:COG3840 217 LLDGE 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
493-699 |
9.45e-15 |
|
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: 74.99 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL----RTSIGTVLQESKLFSG-SI 567
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNISMSKDnhddLKVIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLF 647
Cdd:cd03294 120 LENVAFGLE----VQGVPRAEREERAAEALEL-VGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 648 TERHIENTL----KELNITQIIIAHRL-RTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:cd03294 195 IRREMQDELlrlqAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
463-692 |
1.33e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 463 EKSNVQAHSIKGDIKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN 542
Cdd:PRK09452 2 KKLNKQPSSLSPLVELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 543 DYDyhSLRTSIGTVLQESKLFSG-SISDNIS----MSKDNHDDLK--VIDAAKKSGiLEDILNS-PmgfetiisesgNNF 614
Cdd:PRK09452 80 HVP--AENRHVNTVFQSYALFPHmTVFENVAfglrMQKTPAAEITprVMEALRMVQ-LEEFAQRkP-----------HQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAH-RLRTIQNADKIIYLEDGMIKE 689
Cdd:PRK09452 146 SGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKalqrKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQ 225
|
...
gi 446631050 690 IGT 692
Cdd:PRK09452 226 DGT 228
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
162-437 |
2.11e-14 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 74.47 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINK-LNSFGWLIIIF---SISFVLMSLLRGISIALLQKSLDLSIMN 237
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGnTSLLLLLVLGLagaYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 238 DFMKKMFHLPYSFFDNRSSGDLLFRANS-AVFIRDIISTTMITIFIDLLLIITYTAVM--INFSLdlsllllslsmllAV 314
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSdTDRLQDFLSDGLPDFLTNILMIIGIGVVLfsLNWKL-------------AL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 315 ILFVNANVIRKMTKKnIQDKVNT------------QAVLTENMYNIVDIKSLGLEK---KRLSLWSGNYskeLESSQRLN 379
Cdd:cd18563 148 LVLIPVPLVVWGSYF-FWKKIRRlfhrqwrrwsrlNSVLNDTLPGIRVVKAFGQEKreiKRFDEANQEL---LDANIRAE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 380 IFQAVIHTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSN 437
Cdd:cd18563 224 KLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSR 281
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
495-697 |
2.21e-14 |
|
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: 75.15 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 495 DLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIND----YDYHSLRTSIGTVLQESKLFSG-SISD 569
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 570 NI--SMSKDNHDDLKVIDAAkksgiLEDILnspmGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLF 647
Cdd:TIGR02142 95 NLryGMKRARPSERRISFER-----VIELL----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 648 TERHI----ENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLL 697
Cdd:TIGR02142 166 RKYEIlpylERLHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
476-685 |
2.60e-14 |
|
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: 70.56 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPsgsgkssisklllalykvsegqilinN---KNindydyhslrTS 552
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGR--------------------------NgagKS----------TL 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSGSISdnismskdnhddlkvIDAAKKSGILEdilnspmgfetiisesgnNFSGGQRQRLLVARALYQEP 632
Cdd:cd03221 43 LKLIAGELEPDEGIVT---------------WGSTVKIGYFE------------------QLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 633 SAIVFDEATSHLDLFTERHIENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDG 685
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
479-699 |
2.81e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPS---GSGKSSISKLLLALYKVS--EGQILINNKNI--NDYDYHSLRT 551
Cdd:PRK14267 6 ETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSgcgKSTLLRTFNRLLELNEEArvEGEVRLFGRNIysPDVDPIEVRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 552 SIGTVLQESKLFSG-SISDNISM---------SKDNHDDlKVIDAAKKSGILEDILNSpmgfetiISESGNNFSGGQRQR 621
Cdd:PRK14267 86 EVGMVFQYPNPFPHlTIYDNVAIgvklnglvkSKKELDE-RVEWALKKAALWDEVKDR-------LNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHR-LRTIQNADKIIYLEDGMIKEIGTHEQLLK 698
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELkkEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
.
gi 446631050 699 N 699
Cdd:PRK14267 238 N 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
492-691 |
3.33e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 3.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDyhSLRTSIGTVLQESKLFSG-SISDN 570
Cdd:PRK11000 18 ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP--PAERGVGMVFQSYALYPHlSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 ISMSkdnhddLKvIDAAKKSGI------LEDILNspmgFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHL 644
Cdd:PRK11000 96 MSFG------LK-LAGAKKEEInqrvnqVAEVLQ----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446631050 645 D--LFTERHIENTL--KELNITQIIIAH-RLRTIQNADKIIYLEDGMIKEIG 691
Cdd:PRK11000 165 DaaLRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
162-435 |
5.38e-14 |
|
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: 73.21 E-value: 5.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLsIIIQGLMTVIPLSTKWVTDnafsnsDINKLNSFGWLIIIFSISFVLMSLLRGI-----SIALLQKSLDLS-- 234
Cdd:cd18541 2 LLGILFL-ILVDLLQLLIPRIIGRAID------ALTAGTLTASQLLRYALLILLLALLIGIfrflwRYLIFGASRRIEyd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 235 IMNDFMKKMFHLPYSFFDNRSSGDLLFRANSAV-FIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLA 313
Cdd:cd18541 75 LRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLnAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 314 VILFVNANVIRKMTKKnIQD---KVNTQAVltENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITG 390
Cdd:cd18541 155 LLVYRLGKKIHKRFRK-VQEafsDLSDRVQ--ESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446631050 391 FFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSV 435
Cdd:cd18541 232 LLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMAL 276
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
476-668 |
7.30e-14 |
|
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: 71.35 E-value: 7.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKY--NQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHslrtsI 553
Cdd:cd03293 1 LEVRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQESKLFS-GSISDNISMSkdnhDDLKVIDAAKKSGILEDILNSpMGfetiISESGNNF----SGGQRQRLLVARAL 628
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG----LELQGVPKAEARERAEELLEL-VG----LSGFENAYphqlSGGMRQRVALARAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446631050 629 YQEPSAIVFDEATSHLDLFTERHIENTL----KELNITQIIIAH 668
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTH 190
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
476-699 |
8.67e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 71.73 E-value: 8.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSiskLLLALYKVSE--------GQILINNKNIND--YD 545
Cdd:PRK14239 6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRMNDlnpevtitGSIVYNGHNIYSprTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 546 YHSLRTSIGTVLQESKLFSGSISDNI--SMSKDNHDDLKVIDAA-----KKSGILEDIlnspmgfETIISESGNNFSGGQ 618
Cdd:PRK14239 81 TVDLRKEIGMVFQQPNPFPMSIYENVvyGLRLKGIKDKQVLDEAvekslKGASIWDEV-------KDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQ 695
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQ 233
|
....
gi 446631050 696 LLKN 699
Cdd:PRK14239 234 MFMN 237
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
476-694 |
8.93e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.43 E-value: 8.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKY-ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIG 554
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQ--ESKLFSGSISDNISMSKDNH-----DDLKVIDAAKKSGILEDilnspmgFETiisESGNNFSGGQRQRLLVARA 627
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQgipreEMIKRVDEALLAVNMLD-------FKT---REPARLSGGQKQRVAVAGI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 628 LYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQNADKIIYLEDG-MIKEIGTHE 694
Cdd:PRK13642 155 IALRPEIIILDESTSMLDPTGRQEIMRVIHEIkekyQLTVLSITHDLDEAASSDRILVMKAGeIIKEAAPSE 226
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
11-130 |
1.07e-13 |
|
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: 68.45 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 11 VEQMESVECGLACFAMIANYH-NIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCIIQWG 89
Cdd:cd02423 4 VRQSYDFSCGPAALATLLRYYgGINITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNALQIPVIVLVN 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 446631050 90 NN---HFVVLERIKKQSYIIVDPNRGKIEVPQDEFKQKYSGFAL 130
Cdd:cd02423 84 NGgygHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNAL 127
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
475-692 |
1.42e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 72.82 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 475 DIKFENVNFKYNQFskYILKDLNFTIKQGEKVAIVGPsgsgkssiskLL--LA-LYKVSEGQILINNKNIND---YDyhs 548
Cdd:COG3842 5 ALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPsgcg---kttLLrmIAgFETPDSGRILLDGRDVTGlppEK--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 lRtSIGTVLQESKLFSG-SISDNIS-------MSKDnhddlkviDAAKKsgiLEDILNSpMGfetiISESGNNF----SG 616
Cdd:COG3842 77 -R-NVGMVFQDYALFPHlTVAENVAfglrmrgVPKA--------EIRAR---VAELLEL-VG----LEGLADRYphqlSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 617 GQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRlrtiQN-----ADKIIYLEDGMI 687
Cdd:COG3842 139 GQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRrlqrELGITFIYVTHD----QEealalADRIAVMNDGRI 214
|
....*
gi 446631050 688 KEIGT 692
Cdd:COG3842 215 EQVGT 219
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
162-444 |
1.68e-13 |
|
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: 71.67 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFS------NSDINKLNSF-GWLIIIFSISFVLMSLLRGISIALLQKSLdLS 234
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEglggggGVDFSGLLRIlLLLLGLYLLSALFSYLQNRLMARVSQRTV-YD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 235 IMNDFMKKMFHLPYSFFDNRSSGDLLFRANSAV-FIRDIISTTMITIFIDLLLIITYTAVM--INFSLDLSLLLLslsml 311
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVdNISQALSQSLTQLISSILTIVGTLIMMlyISPLLTLIVLVT----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 312 lAVILFVNANVIRKMTKKNIQDKVNTQAVLT----ENMYNIVDIKSLGLEKKRLSLWSgNYSKEL-ESSQRLNIFQAVIH 386
Cdd:cd18547 155 -VPLSLLVTKFIAKRSQKYFRKQQKALGELNgyieEMISGQKVVKAFNREEEAIEEFD-EINEELyKASFKAQFYSGLLM 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 387 TITGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLIS 444
Cdd:cd18547 233 PIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQS 290
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
476-690 |
1.88e-13 |
|
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: 69.94 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINdyDYHSLRTSIGT 555
Cdd:cd03268 1 LKTNDLTKTYGK--KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFsgsisDNISmskdNHDDLKVIDAA--KKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:cd03268 77 LIEAPGFY-----PNLT----ARENLRLLARLlgIRKKRIDEVLDV-VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDG-MIKEI 690
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKvADRIGIINKGkLIEEG 208
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
162-442 |
1.91e-13 |
|
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: 71.36 E-value: 1.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSIS-FVLMSLLRGISIALlqkSLDL--SIMND 238
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAeAVLSFLRRYLAGRL---SLGVehDLRTD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 239 FMKKMFHLPYSFFDNRSSGDLLFRANS-----------AVFIrdIISTTMITI------FIDLLLIITYTAVMInfsldl 301
Cdd:cd18543 78 LFAHLQRLDGAFHDRWQSGQLLSRATSdlslvqrflafGPFL--LGNLLTLVVglvvmlVLSPPLALVALASLP------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 302 sllllslsmLLAVILFVNANVIRKMTKKnIQDKvntQAVLT----ENMYNIVDIKSLGLEKKRLSLWSGN----YSKELE 373
Cdd:cd18543 150 ---------PLVLVARRFRRRYFPASRR-AQDQ---AGDLAtvveESVTGIRVVKAFGRERRELDRFEAAarrlRATRLR 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 374 SSQRLNIFQAVIHTITGFFQVsvplLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18543 217 AARLRARFWPLLEALPELGLA----AVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMA 281
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
476-704 |
2.34e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.84 E-value: 2.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVS-----EGQILINNKNIND--YDYHS 548
Cdd:PRK14258 8 IKVNNLSFYYD--TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQESKLFSGSISDNISMSkdnhddLKVIDAAKK---SGILEDILNSPMGFETI---ISESGNNFSGGQRQRL 622
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYG------VKIVGWRPKleiDDIVESALKDADLWDEIkhkIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQ-----------NADKIIYL-EDGM 686
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSrlsdftaffkgNENRIGQLvEFGL 239
|
250
....*....|....*...
gi 446631050 687 IKEIGTHEQLLKNRSYYY 704
Cdd:PRK14258 240 TKKIFNSPHDSRTREYVL 257
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
492-699 |
2.71e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 70.38 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN---DYD----------YHSLRTSIGTVLQ 558
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrDKDgqlkvadknqLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 ESKLFSG-SISDNI--------SMSKDNHDDlKVIDAAKKSGILEDILNS-PMgfetiisesgnNFSGGQRQRLLVARAL 628
Cdd:PRK10619 100 HFNLWSHmTVLENVmeapiqvlGLSKQEARE-RAVKYLAKVGIDERAQGKyPV-----------HLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 629 YQEPSAIVFDEATSHLD--LFTE-RHIENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDpeLVGEvLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
450-689 |
3.06e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 450 SRIK--DVLRTKDEQEKS-----NVQAHSIKGD--IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSgsgkssis 520
Cdd:COG0488 281 SRIKalEKLEREEPPRRDktveiRFPPPERLGKkvLELEGLSKSYG--DKTLLDDLSLRIDRGDRIGLIGPNgagkstll 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 521 kLLLALYKVSEGQILINnknindydyHSLRtsIGTVLQESKLFSG--SISDNISMSKDNHDDLKVidaakkSGILEDILN 598
Cdd:COG0488 359 kLLAGELEPDSGTVKLG---------ETVK--IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEV------RGYLGRFLF 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 599 SPMGFETIISesgnNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAH-R--LRTIqn 675
Cdd:COG0488 422 SGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHdRyfLDRV-- 495
|
250
....*....|....
gi 446631050 676 ADKIIYLEDGMIKE 689
Cdd:COG0488 496 ATRILEFEDGGVRE 509
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
614-684 |
3.33e-13 |
|
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: 67.95 E-value: 3.33e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 614 FSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAHRLRTIQNADKIIYLED 684
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
494-704 |
4.44e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.89 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 494 KDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNI---NDYDYHSLRTSIGTVLQESkLFS----GS 566
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDP-LASlnprMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNIS---------MSKDNHDDlKVIDAAKKSGILEDILNS-PmgfetiisesgNNFSGGQRQRLLVARALYQEPSAIV 636
Cdd:PRK15079 117 IGEIIAeplrtyhpkLSRQEVKD-RVKAMMLKVGLLPNLINRyP-----------HEFSGGQCQRIGIARALILEPKLII 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 637 FDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKNRSYYY 704
Cdd:PRK15079 185 CDEPVSALDVSIQAQVVNLLQQLQremgLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
476-702 |
7.55e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.47 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKY---NQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN----DYDYHS 548
Cdd:PRK13641 3 IKFENVDYIYspgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQ--ESKLFSGSISDNISMS------KDNHDDLKVIDAAKKSGILEDILN-SPmgFEtiisesgnnFSGGQR 619
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpknfgfSEDEAKEKALKWLKKVGLSEDLISkSP--FE---------LSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 620 QRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNI---TQIIIAHRLRTI-QNADKIIYLEDGMIKEIGTHEQ 695
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
....*..
gi 446631050 696 LLKNRSY 702
Cdd:PRK13641 232 IFSDKEW 238
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
476-687 |
9.88e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 69.00 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQ---FSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN----DYDYHS 548
Cdd:PRK13649 3 INLQNVSYTYQAgtpFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQ--ESKLFSGSISDNISMSKDNHDdLKVIDAAKKS-------GILEDILN-SPmgFEtiisesgnnFSGGQ 618
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFG-VSQEEAEALAreklalvGISESLFEkNP--FE---------LSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHqsgMTIVLVTHLMDDVANyADFVYVLEKGKL 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
492-699 |
1.50e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.24 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHS--------LRTSIGTVLQESKLF 563
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglirqLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 564 SG-SISDNI-----SMSKDNHDDlkVIDAAKKsgilediLNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVF 637
Cdd:PRK11264 98 PHrTVLENIiegpvIVKGEPKEE--ATARARE-------LLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 638 DEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
476-696 |
1.86e-12 |
|
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: 67.39 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyiLKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDyDYHSLRTSIGT 555
Cdd:cd03265 1 IEVENLVKKYGDFEA--VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLfsgsisDNISMSKDN---HDDLKVIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEP 632
Cdd:cd03265 78 VFQDLSV------DDELTGWENlyiHARLYGVPGAERRERIDELLDF-VGLLEAADRLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 633 SAIVFDEATSHLDLFTERH----IENTLKELNITQIIIAHRLRTI-QNADKIIYLEDGMIKEIGTHEQL 696
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHvweyIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
479-682 |
2.08e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.05 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQ 558
Cdd:PRK10247 11 QNVGYLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 ESKLFSGSISDNI----SMSKDNHDDLKVIDAAKKSGILEDILNSPMgfetiisesgNNFSGGQRQRLLVARALYQEPSA 634
Cdd:PRK10247 89 TPTLFGDTVYDNLifpwQIRNQQPDPAIFLDDLERFALPDTILTKNI----------AELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446631050 635 IVFDEATSHLDLFTERH----IENTLKELNITQIIIAHRLRTIQNADKIIYL 682
Cdd:PRK10247 159 LLLDEITSALDESNKHNvneiIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
476-692 |
2.15e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.06 E-value: 2.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYI--LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNI---NDYDYHSLR 550
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQESKLFSG-SISDNISMSkdnhddLKvIDAAKKSGI------------LEDILNS-PmgfetiisesgNNFSG 616
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVALP------LE-LAGTPKAEIkarvtellelvgLSDKADRyP-----------AQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 617 GQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRLRTI-QNADKIIYLEDGMIKEIG 691
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdinrELGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
.
gi 446631050 692 T 692
Cdd:PRK11153 224 T 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
490-696 |
2.97e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKvSEGQILINNKNINDYDYHSL---RTSIGTVLQESklfSGS 566
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP---NSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNISMSKDNHDDLKV----IDAAKKS----GILEDILNSPMGFETIISEsgnnFSGGQRQRLLVARALYQEPSAIVFD 638
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVhqptLSAAQREqqviAVMEEVGLDPETRHRYPAE----FSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 639 EATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQL 696
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQqkhqLAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
166-421 |
3.28e-12 |
|
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: 67.89 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 166 VFLSIIIQGLMT-VIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKMF 244
Cdd:cd18575 1 ALIALLIAAAATlALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 245 HLPYSFFDNRSSGDLLFRANS-AVFIRDIISTTM------ITIFID--LLLIIT------YTAVMINFSLdlsllllsls 309
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTdTTLIQTVVGSSLsialrnLLLLIGglVMLFITspkltlLVLLVIPLVV---------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 310 mllAVILFVNANViRKMTKKNiQDKV-NTQAVLTENMYNIVDIKSLGLEKKRlslwSGNYSKELESS----QRLNIFQAV 384
Cdd:cd18575 151 ---LPIILFGRRV-RRLSRAS-QDRLaDLSAFAEETLSAIKTVQAFTREDAE----RQRFATAVEAAfaaaLRRIRARAL 221
|
250 260 270
....*....|....*....|....*....|....*..
gi 446631050 385 IHTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAF 421
Cdd:cd18575 222 LTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQF 258
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
479-699 |
3.31e-12 |
|
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: 66.30 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHS-LRTSIGTVL 557
Cdd:cd03224 4 ENLNAGYGKSQ--ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 558 QESKLFSG-SISDNISMSKDNHDdlkviDAAKKSGI---------LEDILNSPmgfetiisesGNNFSGGQRQRLLVARA 627
Cdd:cd03224 82 EGRRIFPElTVEENLLLGAYARR-----RAKRKARLervyelfprLKERRKQL----------AGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 628 LYQEPSAIVFDEATSHLD-LFTERhIENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLApKIVEE-IFEAIRELRdegVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
487-689 |
3.54e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 487 QFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHS---LRT-SIGTVLQESKL 562
Cdd:PRK11629 19 SVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNqKLGFIYQFHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 563 FSG-SISDNISMSKdnhddlkVIDAAKKSGILEDILN--SPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDE 639
Cdd:PRK11629 99 LPDfTALENVAMPL-------LIGKKKPAEINSRALEmlAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 640 ATSHLDLFTERHIENTLKELNITQ----IIIAHRLRTIQNADKIIYLEDGMIKE 689
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRLQgtafLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
476-691 |
4.77e-12 |
|
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: 66.04 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYnqfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHslRTSIGT 555
Cdd:TIGR01277 1 LALDKVRYEY----EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY--QRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNISMSKdnHDDLKvIDAAKKSGIlEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSA 634
Cdd:TIGR01277 75 LFQENNLFAHlTVRQNIGLGL--HPGLK-LNAEQQEKV-VDAAQQ-VGIADYLDRLPEQLSGGQRQRVALARCLVRPNPI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 635 IVFDEATSHLDLFTERH----IENTLKELNITQIIIAHRLR-TIQNADKIIYLEDGMIKEIG 691
Cdd:TIGR01277 150 LLLDEPFSALDPLLREEmlalVKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVS 211
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
471-699 |
4.95e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 4.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 471 SIKGDIKFENVNFKYNQFSKYILKDLN---FTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNI-----N 542
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 543 DYDYHSLRTSIGTVLQ--ESKLFSGSISDNISMSKDNHDDLKViDAAKKSGILEDILNSPmgfETIISESGNNFSGGQRQ 620
Cdd:PRK13645 82 IKEVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQ-EAYKKVPELLKLVQLP---EDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 621 RLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQ----IIIAHRL-RTIQNADKIIYLEDGMIKEIGTHEQ 695
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYkkriIMVTHNMdQVLRIADEVIVMHEGKVISIGSPFE 237
|
....
gi 446631050 696 LLKN 699
Cdd:PRK13645 238 IFSN 241
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
495-699 |
5.19e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 67.45 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 495 DLNFTIKQGEKVAIVGpsgsgkssiskLLLALYKVSEGQILINNKNINDYDYHSLRT---SIGTVLQESklfSGS----- 566
Cdd:COG4608 36 GVSFDIRRGETLGLVGesgcgkstlgrLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDP---YASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 -ISDNISMSKDNHddlKVIDAAKKSGILEDILnspmgfetiiSESGNN----------FSGGQRQRLLVARALYQEPSAI 635
Cdd:COG4608 113 tVGDIIAEPLRIH---GLASKAERRERVAELL----------ELVGLRpehadrypheFSGGQRQRIGIARALALNPKLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 636 VFDEATSHLDLFTERHIENTL----KELNITQIIIAHRL---RTIqnADKII--YLedGMIKEIGTHEQLLKN 699
Cdd:COG4608 180 VCDEPVSALDVSIQAQVLNLLedlqDELGLTYLFISHDLsvvRHI--SDRVAvmYL--GKIVEIAPRDELYAR 248
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
476-699 |
5.81e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 67.86 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPsgsgkssiskLL--LA-LYKVSEGQILINNKNINdYDYHSLRTS 552
Cdd:COG1118 3 IEVRNISKRFGSFT--LLDDVSLEIASGELVALLGPsgsg---kttLLriIAgLETPDSGRIVLNGRDLF-TNLPPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLFSG-SISDNISMSkdnhddLKVI--DAAKKSGILEDILnspmgfETI-ISESGNNF----SGGQRQRLLV 624
Cdd:COG1118 77 VGFVFQHYALFPHmTVAENIAFG------LRVRppSKAEIRARVEELL------ELVqLEGLADRYpsqlSGGQRQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLFTERHIE----NTLKELNITQIIIAH------RLrtiqnADKIIYLEDGMIKEIGTHE 694
Cdd:COG1118 145 ARALAVEPEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPD 219
|
....*
gi 446631050 695 QLLKN 699
Cdd:COG1118 220 EVYDR 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
489-694 |
6.68e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.42 E-value: 6.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 489 SKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNknindydyhslrtSIGTVLQESKLFSGSIS 568
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-------------SIAYVPQQAWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 569 DNIsMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFT 648
Cdd:PTZ00243 739 GNI-LFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446631050 649 ERHI--ENTLKEL-NITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHE 694
Cdd:PTZ00243 818 GERVveECFLGALaGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
615-687 |
6.80e-12 |
|
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: 63.99 E-value: 6.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLD------LFteRHIENtLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTpaeverLF--KVIRR-LRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
527-699 |
7.51e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.66 E-value: 7.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 527 YKVSeGQILINNKNINDY-DYHSLRTSIGTVLQESKLFSGSISDNISMSKDNHddlKVIDAAKKSGILEDILNSPMGFET 605
Cdd:PRK14271 77 YRYS-GDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH---KLVPRKEFRGVAQARLTEVGLWDA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 606 I---ISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRL-RTIQNADKI 679
Cdd:PRK14271 153 VkdrLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNLaQAARISDRA 232
|
170 180
....*....|....*....|
gi 446631050 680 IYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK14271 233 ALFFDGRLVEEGPTEQLFSS 252
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
476-696 |
7.82e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 68.29 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLAL--YKVSEGQIL------------------ 535
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 536 ---------------INNKNINDYDYHSLRTSIGTVLQESKLFSG--SISDNIsMSKDNHDDLKVIDAAKKSGILEDILN 598
Cdd:TIGR03269 79 gepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 599 spmgFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQ 674
Cdd:TIGR03269 158 ----LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkasGISMVLTSHWPEVIE 233
|
250 260
....*....|....*....|...
gi 446631050 675 N-ADKIIYLEDGMIKEIGTHEQL 696
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEV 256
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
476-709 |
7.97e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.30 E-value: 7.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQ--ESKLFSGSISDNISMSKDNHDdlkvIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPS 633
Cdd:PRK13647 84 VFQdpDDQVFSSTVWDDVAFGPVNMG----LDKDEVERRVEEALKA-VRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 634 AIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLR-TIQNADKIIYLEDGMI-----KEIGTHEQLLKNRSYYY 704
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHnqgKTVIVATHDVDlAAEWADQVIVLKEGRVlaegdKSLLTDEDIVEQAGLRL 238
|
....*
gi 446631050 705 NLYSQ 709
Cdd:PRK13647 239 PLVAQ 243
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
479-697 |
8.05e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.95 E-value: 8.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLAL---YKVSEGQILINNKNINDYDYHSLRTSIGT 555
Cdd:PRK13548 6 RNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPngag---kstLLRALsgeLSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKL-FSGSISDNISM-----SKDNHDDLKVIDAAkksgiLEdilnspmgfETIISESGNNF----SGGQRQRLLVA 625
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMgraphGLSRAEDDALVAAA-----LA---------QVDLAHLAGRDypqlSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 626 RALYQ------EPSAIVFDEATSHLDLFTERHIENTLKELNITQ----IIIAHRLR-TIQNADKIIYLEDGMIKEIGTHE 694
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglavIVVLHDLNlAARYADRIVLLHQGRLVADGTPA 226
|
...
gi 446631050 695 QLL 697
Cdd:PRK13548 227 EVL 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
493-704 |
9.18e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 67.37 E-value: 9.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINN---KNINDYDYHSL-RTSIGTVLQESKLFSG-SI 567
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVrRKKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNISMSKdnhdDLKVIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLF 647
Cdd:PRK10070 124 LDNTAFGM----ELAGINAEERREKALDALRQ-VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 648 TERHIENTLKELNI----TQIIIAHRL-RTIQNADKIIYLEDGMIKEIGTHEQLLKNRSYYY 704
Cdd:PRK10070 199 IRTEMQDELVKLQAkhqrTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
166-442 |
1.12e-11 |
|
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: 66.29 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 166 VFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRgISIALLQKSLDLSIMN----DFMK 241
Cdd:cd18554 5 IVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLILR-PPVEYYRQYFAQWIANkilyDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 242 KMFH----LPYSFFDNRSSGDLLFRA-NSAVFIRDIISTTMITIFIDLLLIITYTAVMINFSLDLSLLLLSLSMLLAVIL 316
Cdd:cd18554 84 DLFDhlqkLSLRYYANNRSGEIISRViNDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 317 FVNANVIRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEK---KRLSLWSGNY-SKELESSQRLNIFQAVIHTITGFf 392
Cdd:cd18554 164 KYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKheqKQFDKRNGHFlTRALKHTRWNAKTFSAVNTITDL- 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446631050 393 qvsVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18554 243 ---APLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTL 289
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
478-688 |
1.18e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 478 FENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLALYKVSEGQILINNknindydyhslRTSIGTVL 557
Cdd:COG0488 1 LENLSKSFG--GRPLLDDVSLSINPGDRIGLVGRngagkstllkILAGELEPDSGEVSIPK-----------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 558 QESKLFSG-SISDNISMS------------------KDNHDDLKVIDAA--------------------KKSGILEDILN 598
Cdd:COG0488 68 QEPPLDDDlTVLDTVLDGdaelraleaeleeleaklAEPDEDLERLAELqeefealggweaearaeeilSGLGFPEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 599 SPMGfetiisesgnNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAH-R--LRTIqn 675
Cdd:COG0488 148 RPVS----------ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHdRyfLDRV-- 215
|
250
....*....|...
gi 446631050 676 ADKIIYLEDGMIK 688
Cdd:COG0488 216 ATRILELDRGKLT 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
522-696 |
1.56e-11 |
|
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: 65.98 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 522 LLLALYKVSEGQILINNKNINDYDYHslRTSIGTVLQESKLFSG-SISDNISMSkdnhddLKvIDAAKKSGILEDILN-- 598
Cdd:TIGR01187 15 LLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFPHmTVEENVAFG------LK-MRKVPRAEIKPRVLEal 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 599 SPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRLR-TI 673
Cdd:TIGR01187 86 RLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiqeQLGITFVFVTHDQEeAM 165
|
170 180
....*....|....*....|...
gi 446631050 674 QNADKIIYLEDGMIKEIGTHEQL 696
Cdd:TIGR01187 166 TMSDRIAIMRKGKIAQIGTPEEI 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
479-694 |
1.68e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQ 558
Cdd:PRK10253 11 EQLTLGYGKYT--VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 ESKLfSGSISDNISMSKDNHDDLKVIDAAKKSGilEDILNSPM---GFETIISESGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:PRK10253 89 NATT-PGDITVQELVARGRYPHQPLFTRWRKED--EEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 636 VFDEATSHLDLFTERHIENTLKELNITQ----IIIAHRL-RTIQNADKIIYLEDGMI------KEIGTHE 694
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKgytlAAVLHDLnQACRYASHLIALREGKIvaqgapKEIVTAE 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
476-692 |
2.07e-11 |
|
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: 64.06 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINdYDYHSLRTSIGT 555
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSG-SISDNISM-----SKDNHDDLKVIDAAKKSGILEDILNSPMGfetiisesgnNFSGGQRQRLLVARALY 629
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLRVLGLTDKANKRAR----------TLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 630 QEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGT 692
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVrkGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
495-691 |
2.86e-11 |
|
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: 63.47 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 495 DLNFTIKqGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILIN-------NKNINdydYHSLRTSIGTVLQESKLFSG-S 566
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsRKKIN---LPPQQRKIGLVFQQYALFPHlN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNISMSkdnhddLKVIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDL 646
Cdd:cd03297 92 VRENLAFG------LKRKRNREDRISVDELLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446631050 647 FTERHIENTLKE----LNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIG 691
Cdd:cd03297 165 ALRLQLLPELKQikknLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
476-692 |
2.93e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 64.75 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKY---NQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINN----KNINDYDYHS 548
Cdd:PRK13643 2 IKFEKVNYTYqpnSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LRTSIGTVLQ--ESKLFSGSISDNISMSKDN----HDDLKVIDAAKksgiLEDILNSPMGFEtiisESGNNFSGGQRQRL 622
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgipKEKAEKIAAEK----LEMVGLADEFWE----KSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDlfTERHIE-----NTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGT 692
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLD--PKARIEmmqlfESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
495-687 |
3.09e-11 |
|
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: 63.28 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 495 DLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKnindyDYHSLRTS---IGTVLQESKLFSG-SISDN 570
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAPPAdrpVSMLFQENNLFAHlTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 ISMSKDNHDDLKVIDAAKKSGILedilnSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLD----- 645
Cdd:cd03298 91 VGLGLSPGLKLTAEDRQAIEVAL-----ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalra 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446631050 646 ----LFTERHientlKELNITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:cd03298 166 emldLVLDLH-----AETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
476-696 |
5.35e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYILKDLN---FTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIND--------- 543
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDnvsVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 544 ---------------YDYHSLRTSIGTVLQ--ESKLFSGSISDNI-----SMSKDNHDDLKVidaAKKsgILEdILNSPm 601
Cdd:PRK13651 83 vleklviqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQTIEKDIifgpvSMGVSKEEAKKR---AAK--YIE-LVGLD- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 602 gfETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNI---TQIIIAHRLRTI-QNAD 677
Cdd:PRK13651 156 --ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqgkTIILVTHDLDNVlEWTK 233
|
250 260
....*....|....*....|
gi 446631050 678 KIIYLEDG-MIKEIGTHEQL 696
Cdd:PRK13651 234 RTIFFKDGkIIKDGDTYDIL 253
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
476-690 |
5.70e-11 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 63.57 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKY--ILKDLNFTIKQGEKVAIVGPsgsgkssiskLL--LA-LYKVSEGQILINNKNIndydyHSLR 550
Cdd:COG1116 8 LELRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPsgcg---kstLLrlIAgLEKPTSGEVLVDGKPV-----TGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQESKLF---SgsISDNISMSkdnhddLKV--IDAAKKSGILEDILNSpMGfetiISESGNNF----SGGQRQR 621
Cdd:COG1116 80 PDRGVVFQEPALLpwlT--VLDNVALG------LELrgVPKAERRERARELLEL-VG----LAGFEDAYphqlSGGMRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTL----KELNITQIIIAH------RLrtiqnADKIIYLED--GMIKE 689
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
.
gi 446631050 690 I 690
Cdd:COG1116 222 E 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
480-704 |
5.72e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 65.65 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 480 NVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYK-----VSEGQILINNKN-----INDYDYHSL 549
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEqagglVQCDKMLLRRRSrqvieLSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 R----TSIGTVLQE-----SKLFsgSISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGfETIISESGNNFSGGQRQ 620
Cdd:PRK10261 99 RhvrgADMAMIFQEpmtslNPVF--TVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 621 RLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQ 695
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQ 255
|
....*....
gi 446631050 696 LLKNRSYYY 704
Cdd:PRK10261 256 IFHAPQHPY 264
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
476-697 |
7.72e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 62.68 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYN----QFSkyilkdlnFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNindydyHSL-- 549
Cdd:PRK10771 2 LKLTDITWLYHhlpmRFD--------LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 --RTSIGTVLQESKLFSG-SISDNISMSKdnHDDLKVIDAAKKSgiLEDILnSPMGFETIISESGNNFSGGQRQRLLVAR 626
Cdd:PRK10771 68 psRRPVSMLFQENNLFSHlTVAQNIGLGL--NPGLKLNAAQREK--LHAIA-RQMGIEDLLARLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 627 ALYQEPSAIVFDEATSHLD--LFTE--RHIENTLKELNITQIIIAHRLR-TIQNADKIIYLEDGMIKEIGTHEQLL 697
Cdd:PRK10771 143 CLVREQPILLLDEPFSALDpaLRQEmlTLVSQVCQERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
486-696 |
1.16e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.56 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 486 NQFSKY-----ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINdyDYHSLRTSIGTVLQES 560
Cdd:PRK10851 6 ANIKKSfgrtqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 561 KLFSG-SISDNIS-----MSKDNHDDLKVIDaaKKSGILEDILNspmgfetiISESGNNF----SGGQRQRLLVARALYQ 630
Cdd:PRK10851 84 ALFRHmTVFDNIAfgltvLPRRERPNAAAIK--AKVTQLLEMVQ--------LAHLADRYpaqlSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 631 EPSAIVFDEATSHLD--LFTE--RHIENTLKELNITQIIIAH-RLRTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:PRK10851 154 EPQILLLDEPFGALDaqVRKElrRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
164-447 |
1.62e-10 |
|
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: 62.56 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 164 GLVFLsiIIQGLMTV-IPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKK 242
Cdd:cd18572 1 AFVFL--VVAALSELaIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 243 MFHLPYSFFDNRSSGDLLFRANS-------------AVFIRDIISTTMITIFidlLLIITYTAVMINFSLDlsllllsls 309
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSdcqkvsdplstnlNVFLRNLVQLVGGLAF---MFSLSWRLTLLAFITV--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 310 mllAVILFVN---ANVIRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVI 385
Cdd:cd18572 147 ---PVIALITkvyGRYYRKLSKE-IQDALaEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGY 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 386 HTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAF----SSIAGSYItpivSVSNNYTQLI-SLGS 447
Cdd:cd18572 223 VAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFmlyqQQLGEAFQ----SLGDVFSSLMqAVGA 285
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
489-697 |
1.65e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.51 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 489 SKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQES--KLFSGS 566
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNISMSKDNHDdlkvIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLD- 645
Cdd:PRK13652 96 VEQDIAFGPINLG----LDEETVAHRVSSALHM-LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDp 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 646 -----LFteRHIENTLKELNITQIIIAHRLRTIQNADKIIYLED-------GMIKEIGTHEQLL 697
Cdd:PRK13652 171 qgvkeLI--DFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDkgrivayGTVEEIFLQPDLL 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
492-699 |
2.79e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKL---LLALYKVS--EGQILINNKNINDYDYHSLRTSIGTVLQ-ESKLFSG 565
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 566 SISDNISMS------KDNHDDL--KVIDAAKKSGILEDI---LNSPMGfetiisesgnNFSGGQRQRLLVARALYQEPSA 634
Cdd:PRK14247 98 SIFENVALGlklnrlVKSKKELqeRVRWALEKAQLWDEVkdrLDAPAG----------KLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 635 IVFDEATSHLDLFTERHIENTLKEL--NITQIIIAH-RLRTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELkkDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
493-704 |
2.85e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 2.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN---DYDYHSLRTSIGTVLQE---SKLFSGS 566
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlsPGKLQALRRDIQFIFQDpyaSLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNISMSKDNHDDLKVIDAAKK-SGILEDILNSPMGFETIISEsgnnFSGGQRQRLLVARALYQEPSAIVFDEATSHLD 645
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARvAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 646 LFTERHIENTL----KELNITQIIIAHRLRTIQNAD---KIIYLedGMIKEIGTHEQLLKNRSYYY 704
Cdd:PRK10261 496 VSIRGQIINLLldlqRDFGIAYLFISHDMAVVERIShrvAVMYL--GQIVEIGPRRAVFENPQHPY 559
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
492-687 |
2.94e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 63.59 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL----RTSIGTVLQESKLFSG-S 566
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 567 ISDNISMSKdnhddlkVIDAAKKSGILE--DILNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHL 644
Cdd:PRK10535 103 AAQNVEVPA-------VYAGLERKQRLLraQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGAL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446631050 645 DLFTERHIENTLKELNI---TQIIIAHRLRTIQNADKIIYLEDGMI 687
Cdd:PRK10535 176 DSHSGEEVMAILHQLRDrghTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
489-689 |
3.23e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 489 SKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNI---NDYDYHSLRTSIGTVLQES----- 560
Cdd:PRK10419 24 HQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQDSisavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 561 --KLFSGSISDNIsmskdNHddLKVIDAAKKSGILEDILNSpMGF-ETIISESGNNFSGGQRQRLLVARALYQEPSAIVF 637
Cdd:PRK10419 104 prKTVREIIREPL-----RH--LLSLDKAERLARASEMLRA-VDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 638 DEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMIKE 689
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLqqqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
159-432 |
4.56e-10 |
|
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: 61.31 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINklnsfgwLIIIFSISFVLMSLLRGISIALLQK---SLDLSI 235
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPLIVRYIIDDLLPSKNLR-------LILIIGAILLALYILRTLLNYFVTYwghVMGARI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 236 MNDFMKKMF----HLPYSFFDNRSSGDLLFRANSAVFirDI------------IST-TMITIFIDLLLI-ITYTAVMINF 297
Cdd:cd18549 74 ETDMRRDLFehlqKLSFSFFDNNKTGQLMSRITNDLF--DIselahhgpedlfISIiTIIGSFIILLTInVPLTLIVFAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 298 SldlsllllslsmllAVILFVNANVIRKMTKKNIQDKVNT---QAVLTENMYNIVDIKSLG---LEKKRLSlwSGNysKE 371
Cdd:cd18549 152 L--------------PLMIIFTIYFNKKMKKAFRRVREKIgeiNAQLEDSLSGIRVVKAFAneeYEIEKFD--EGN--DR 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 372 LESSQRLNIFQ-AVIHTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPI 432
Cdd:cd18549 214 FLESKKKAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPI 275
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
476-697 |
7.57e-10 |
|
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: 60.10 E-value: 7.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPsgsgkssisklLLAL-----YKVSEGQILINNKNINDYDYHSLR 550
Cdd:COG1119 4 LELRNVTVRRG--GKTILDDISWTVKPGEHWAILGPngag----kstLLSLitgdlPPTYGNDVRLFGERRGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGtvlqeskLFSGSISDNIsmskdnHDDLKVIDAAKkSG-----------------ILEDILNSpMGFETIISESGNN 613
Cdd:COG1119 78 KRIG-------LVSPALQLRF------PRDETVLDVVL-SGffdsiglyreptdeqreRARELLEL-LGLAHLADRPFGT 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 614 FSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQNA-DKIIYLEDGMIK 688
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVV 222
|
....*....
gi 446631050 689 EIGTHEQLL 697
Cdd:COG1119 223 AAGPKEEVL 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
492-699 |
8.20e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHS-LRTSIGTVLQESKLFSG-SISD 569
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 570 NISMSKDNHDDLKVIDAAKKSGILEDILNspmgFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLD---- 645
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDRANELMEEFH----IEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisv 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 646 LFTERHIENtLKELNITQIIIAHRLR-TIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK10895 174 IDIKRIIEH-LRDSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
205-437 |
8.31e-10 |
|
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: 60.53 E-value: 8.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 205 LIIIFSIsfvLMSLLRGISIALLQKSLDLSIMNDFMKKMFHLPYSFfDNRSSGDLLFRANSAVFIRDIISTTMITIFIDL 284
Cdd:cd18587 50 IALLFDF---ILKLLRAYFIDVAGKRADVILSSRLFERVLGLRLEA-RPASVGSFANNLREFESVRDFFTSATLTALIDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 285 ------LLIITYTA---VMInfsldlsllllsLSMLLAVILFVNANV---IRKMTKKNIQDKVNTQAVLTENMYNIVDIK 352
Cdd:cd18587 126 pfvllfLAVIALIGgplALV------------PLVAIPLVLLYGLLLqkpLRRLVEESMRESAQKNALLVESLSGLETIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 353 SLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFFQVSVPLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPI 432
Cdd:cd18587 194 ALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPL 273
|
....*
gi 446631050 433 VSVSN 437
Cdd:cd18587 274 GQIAG 278
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
615-699 |
8.94e-10 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 59.81 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLD--LFTE--RHIENtLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKE 689
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDpeLVGEvlKVMRD-LAEEGRTMLVVTHEMGFARDvSSHVVFLHQGRIEE 234
|
90
....*....|
gi 446631050 690 IGTHEQLLKN 699
Cdd:COG4598 235 QGPPAEVFGN 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
476-685 |
1.10e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.12 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN---DYDYHSLRTS 552
Cdd:PRK10908 2 IRFEHVSKAYLG-GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlkNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 553 IGTVLQESKLF-SGSISDNISM----SKDNHDDL--KVIDAAKKSGILEDILNSPMgfetiisesgnNFSGGQRQRLLVA 625
Cdd:PRK10908 81 IGMIFQDHHLLmDRTVYDNVAIpliiAGASGDDIrrRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 626 RALYQEPSAIVFDEATSHLDLFTERHIENTLKELN---ITQIIIAHRLRTIQNAD-KIIYLEDG 685
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSyRMLTLSDG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
493-687 |
1.18e-09 |
|
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: 58.92 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNknindYDYHS----LRTSIGTVLQESKLFSG-SI 567
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FDVVKepaeARRRLGFVSDSTGLYDRlTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNISMSKDNHDdLKViDAAKksGILEDiLNSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLF 647
Cdd:cd03266 96 RENLEYFAGLYG-LKG-DELT--ARLEE-LADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446631050 648 TERHIENTLKELNITQ---IIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:cd03266 171 ATRALREFIRQLRALGkciLFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
476-669 |
1.31e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 61.30 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKYIlKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKN----INDYDYHSLRT 551
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklfyVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 552 sigtvLQESKLFSGSISDNISMSKDNHDDLKVIDAAKksgiLEDILNSPMGFEtIISESGNNFSGGQRQRLLVARALYQE 631
Cdd:TIGR00954 531 -----LRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQ----LTHILEREGGWS-AVQDWMDVLSGGEKQRIAMARLFYHK 600
|
170 180 190
....*....|....*....|....*....|....*...
gi 446631050 632 PSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAHR 669
Cdd:TIGR00954 601 PQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHR 638
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
490-694 |
1.58e-09 |
|
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: 58.31 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGPSgsgKSSISKLLLAL-----YKVSEGQILINNKNINDYD-YHSLRTSIGTVLQESKLF 563
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPN---GSGKSTLAKTImghpkYEVTEGEILFKGEDITDLPpEERARLGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 564 SGsisdnismskdnhddLKVIDaakksgiledilnspmgfetIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSH 643
Cdd:cd03217 90 PG---------------VKNAD--------------------FLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 644 LDLFTERHIENTLKEL---NITQIIIAHRLRTIQ--NADKIIYLEDGMIKEIGTHE 694
Cdd:cd03217 135 LDIDALRLVAEVINKLreeGKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKE 190
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
479-700 |
1.69e-09 |
|
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: 58.84 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQFskYILKDLNFTIKQGEKVAIVGPsgsgkssiskLLLA---LYKVSEGQILINNKNINDYDYHSL-RTSIG 554
Cdd:COG0410 7 ENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRngag---kttLLKAisgLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQESKLFSG-SISDNISMSKDNHDDLKVIDAakksgILEDIL----------NSPmgfetiisesGNNFSGGQRQRLL 623
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRA-----DLERVYelfprlkerrRQR----------AGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 624 VARALYQEPSAIVFDEATSHLD-LFTERhIENTLKELN---ITqIII----AHRLRTIqnADKIIYLEDGMIKEIGTHEQ 695
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLApLIVEE-IFEIIRRLNregVT-ILLveqnARFALEI--ADRAYVLERGRIVLEGTAAE 222
|
....*
gi 446631050 696 LLKNR 700
Cdd:COG0410 223 LLADP 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
492-697 |
2.30e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.86 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKL-FSGSISDN 570
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 ISMSKDNH---------DDLKVIDAAKKSGiledilnspmGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEAT 641
Cdd:PRK09536 98 VEMGRTPHrsrfdtwteTDRAAVERAMERT----------GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 642 SHLDLFTE-RHIE--NTLKELNITQIIIAHRLR-TIQNADKIIYLEDGMIKEIGTHEQLL 697
Cdd:PRK09536 168 ASLDINHQvRTLElvRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
479-669 |
5.32e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 5.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYK--VSEGQILINNKNINdydyhslrtsigtv 556
Cdd:COG2401 32 EAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG-------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 557 lQESklfsgSISDNISMSKDNHDDLKVIDAAKksgilediLNSPMGFETIISEsgnnFSGGQRQRLLVARALYQEPSAIV 636
Cdd:COG2401 98 -REA-----SLIDAIGRKGDFKDAVELLNAVG--------LSDAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 446631050 637 FDEATSHLDLFTERHIENTL----KELNITQIIIAHR 669
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLqklaRRAGITLVVATHH 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
476-697 |
5.57e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.40 E-value: 5.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPsgsgkssisklLLA----LYKVSEGQILINNKNINDYDYHSLRT 551
Cdd:COG4604 2 IEIKNVSKRYGG--KVVLDDVSLTIPKGGITALIGPngag----kstLLSmisrLLPPDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 552 SIGTVLQE----SKLfsgSISDNISM-----SKDNH--DDLKVIDAAkksgI----LEDILNSPMgfetiisesgNNFSG 616
Cdd:COG4604 76 RLAILRQEnhinSRL---TVRELVAFgrfpySKGRLtaEDREIIDEA----IayldLEDLADRYL----------DELSG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 617 GQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRLrtiqN-----ADKIIYLEDGMI 687
Cdd:COG4604 139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRrladELGKTVVIVLHDI----NfascyADHIVAMKDGRV 214
|
250
....*....|
gi 446631050 688 KEIGTHEQLL 697
Cdd:COG4604 215 VAQGTPEEII 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
493-687 |
6.39e-09 |
|
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: 56.96 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNkNINDYDYHSLRTSIGTVL-QESKL-FSGSISDN 570
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgQKTQLwWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 ISMSKDNHDdLKVIDAAKKSGILEDILNspmgFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTER 650
Cdd:cd03267 116 FYLLAAIYD-LPPARFKKRLDELSELLD----LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446631050 651 HIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDGMI 687
Cdd:cd03267 191 NIRNFLKEYNrergTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
493-697 |
7.28e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN--DYDYHSLR---------TSIGTVLQESK 561
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRirmifqdpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 562 LFSGSISDNISMSKDNHDDlKVIDAAKKSGILEDILN-SPmgfetiisesgNNFSGGQRQRLLVARALYQEPSAIVFDEA 640
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREK-QIIETLRQVGLLPDHASyYP-----------HMLAPGQKQRLGLARALILRPKVIIADEA 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 641 TSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLL 697
Cdd:PRK15112 177 LASLDMSMRSQLINLMLELQekqgISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
492-645 |
7.45e-09 |
|
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: 56.33 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGsgkssiskLL--LA-LYKVSEGQILINNKNINDyDYHSLRTSIGTVLQESKLFSG-SI 567
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGsgk---ttLLriLAgLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNI----SMSKDNHDDLKVIDAAKKSGiLEDILNSPMGfetiisesgnNFSGGQRQRLLVARALYQEPSAIVFDEATSH 643
Cdd:COG4133 93 RENLrfwaALYGLRADREAIDEALEAVG-LAGLADLPVR----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
..
gi 446631050 644 LD 645
Cdd:COG4133 162 LD 163
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
614-699 |
9.12e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 57.67 E-value: 9.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 614 FSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTL----KELNITQIIIAHRLRTIQN-ADKII--YLedGM 686
Cdd:PRK11308 155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmdlqQELGLSYVFISHDLSVVEHiADEVMvmYL--GR 232
|
90
....*....|...
gi 446631050 687 IKEIGTHEQLLKN 699
Cdd:PRK11308 233 CVEKGTKEQIFNN 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
492-692 |
9.43e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDyHSLRtSIGTVLQESKLFSG-SISDN 570
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-PADR-DIAMVFQNYALYPHmSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 IS-------MSKDnHDDLKVIDAAKksgILEdilnspmgFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSH 643
Cdd:PRK11650 97 MAyglkirgMPKA-EIEERVAEAAR---ILE--------LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 644 LD--LFTERHIEntLKEL----NITQIIIAH-RLRTIQNADKIIYLEDGMIKEIGT 692
Cdd:PRK11650 165 LDakLRVQMRLE--IQRLhrrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
615-682 |
1.07e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 55.70 E-value: 1.07e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQNADKIIYL 682
Cdd:NF040873 121 SGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEharGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
178-442 |
1.48e-08 |
|
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: 56.75 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 178 VIPLSTKWVTDNAFSNSDINKLnsFGWLIIIFSI----SFVLMSLLRGIS---IALLQKSLdlsimndfMKKMFHLPYSF 250
Cdd:cd18573 22 LIDVASKESGDIEIFGLSLKTF--ALALLGVFVVgaaaNFGRVYLLRIAGeriVARLRKRL--------FKSILRQDAAF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 251 FDNRSSGDLLFR-------------ANSAVFIRDIISTT-----MITIFIDLLLIITYTAVMInfsldlsllllslsmll 312
Cdd:cd18573 92 FDKNKTGELVSRlssdtsvvgksltQNLSDGLRSLVSGVggigmMLYISPKLTLVMLLVVPPI----------------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 313 AVILFVNANVIRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLwsgnYSKELESSQRLN----IFQAVIHT 387
Cdd:cd18573 155 AVGAVFYGRYVRKLSKQ-VQDALaDATKVAEERLSNIRTVRAFAAERKEVER----YAKKVDEVFDLAkkeaLASGLFFG 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 388 ITGFF-QVSVpLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18573 230 STGFSgNLSL-LSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSEL 284
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
479-687 |
1.77e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 56.22 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIndydyHSLRTSIGTVLQ 558
Cdd:PRK11247 16 NAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 ESKLFS-GSISDNISMSKDNH---DDLKVIDAakksgiledilnspMGFETIISESGNNFSGGQRQRLLVARALYQEPSA 634
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGLKGQwrdAALQALAA--------------VGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 635 IVFDEATSHLDLFT----ERHIENTLKELNITQIIIAHRL-RTIQNADKIIYLEDGMI 687
Cdd:PRK11247 155 LLLDEPLGALDALTriemQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
493-699 |
2.08e-08 |
|
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: 55.52 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL-RTSIGTVLQESKLFSG-SISDN 570
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 ISM---SKDNHDDLKVIDAAKKSGI------------LEDILNSPMGfetiisesgnNFSGGQRQRLLVARALYQEPSAI 635
Cdd:cd03219 96 VMVaaqARTGSGLLLARARREEREAreraeellervgLADLADRPAG----------ELSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 636 VFDEATSHLDLfTERH-IENTLKELN---ITQIIIAHRLRTIQN-ADKIIYLEDG-MIKEiGTHEQLLKN 699
Cdd:cd03219 166 LLDEPAAGLNP-EETEeLAELIRELRergITVLLVEHDMDVVMSlADRVTVLDQGrVIAE-GTPDEVRNN 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
476-685 |
2.12e-08 |
|
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: 54.98 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSlrtsIGT 555
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----IGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLFSgsisdnismskdnhdDLKVIDAA---------KKSGILEDILNSPMGFEtiISESGN----NFSGGQRQRL 622
Cdd:cd03269 75 LPEERGLYP---------------KMKVIDQLvylaqlkglKKEEARRRIDEWLERLE--LSEYANkrveELSKGNQQKV 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 623 LVARALYQEPSAIVFDEATSHLDLFTERHIE---NTLKELNITQIIIAHRLRTIQN-ADKIIYLEDG 685
Cdd:cd03269 138 QFIAAVIHDPELLILDEPFSGLDPVNVELLKdviRELARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
461-697 |
2.34e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 57.12 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 461 EQEKSNVQAHSIkgdIKFENVNFKYNQFSKYILK---DLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQ--IL 535
Cdd:TIGR03269 268 EKECEVEVGEPI---IKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVR 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 536 INNKNINDYDYHSL-----RTSIGTVLQESKLFS-GSISDNI--SMSKDNHDDLKVIDAA---KKSGILEDILnspmgfE 604
Cdd:TIGR03269 345 VGDEWVDMTKPGPDgrgraKRYIGILHQEYDLYPhRTVLDNLteAIGLELPDELARMKAVitlKMVGFDEEKA------E 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 605 TIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTL----KELNITQIIIAHRLRTIQN-ADKI 679
Cdd:TIGR03269 419 EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDvCDRA 498
|
250
....*....|....*...
gi 446631050 680 IYLEDGMIKEIGTHEQLL 697
Cdd:TIGR03269 499 ALMRDGKIVKIGDPEEIV 516
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
478-673 |
2.83e-08 |
|
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: 54.97 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 478 FENVNFKYNQFSKY--ILKDLNFTIKQGEKVAIVGPSgsgKSSISKLLLAL------YKVSEGQILINNKNINDydyHSL 549
Cdd:cd03234 6 WWDVGLKAKNWNKYarILNDVSLHVESGQVMAILGSS---GSGKTTLLDAIsgrvegGGTTSGQILFNGQPRKP---DQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 550 RTSIGTVLQESKLFSG-----SISDNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIisesgNNFSGGQRQRLLV 624
Cdd:cd03234 80 QKCVAYVRQDDILLPGltvreTLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLV-----KGISGGERRRVSI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLFTERHIENTLKELnitqiiiAHRLRTI 673
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL-------ARRNRIV 196
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
492-689 |
2.94e-08 |
|
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: 55.13 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL----RTSIGTVLQESKLFsGSI 567
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLL-PTL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 S--DNISM--SKDNHDdlkviDAAKKSgilEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPsAIVF-DEATS 642
Cdd:COG4181 106 TalENVMLplELAGRR-----DARARA---RALLER-VGLGHRLDHYPAQLSGGEQQRVALARAFATEP-AILFaDEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446631050 643 HLDLFTERHIENTLKELN----ITQIIIAHRLRTIQNADKIIYLEDGMIKE 689
Cdd:COG4181 176 NLDAATGEQIIDLLFELNrergTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
15-127 |
3.01e-08 |
|
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: 52.63 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 15 ESVECGLACFAMIANYHNIKLSLNNLRNLYPAPREGFSFLNIREIANNYSFSADAYEIDMAELTAISLPCIIQWGNNHFV 94
Cdd:cd02417 3 TKPDSGLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPLPALAWDDDGGHF 82
|
90 100 110
....*....|....*....|....*....|....
gi 446631050 95 VLERIKKQSYIIVDPNRGKIEV-PQDEFKQKYSG 127
Cdd:cd02417 83 ILAKLDGQKYLIQDPISQRPEVlSREEFEARWSG 116
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
490-687 |
4.29e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.09 E-value: 4.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGpsgsgkssiskLLLAL---YKVSEGQILINNKNINDYDYHSLRTSIGTVLQESKL---F 563
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGsnga---gkstLLNAIagsLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 564 SGSISDNISM--------------SKDNHDDLKviDAAKKSGI-LEDILNSPMGfetiisesgnNFSGGQRQRLLVARAL 628
Cdd:COG1101 96 SMTIEENLALayrrgkrrglrrglTKKRRELFR--ELLATLGLgLENRLDTKVG----------LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446631050 629 YQEPSAIVFDEATSHLDLFTERHI----ENTLKELNITQIIIAHRLR-TIQNADKIIYLEDGMI 687
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVleltEKIVEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
545-703 |
1.24e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 545 DYHSLRTSIGTVLQ--ESKLFSGSISDNISMSKDNhddLKV--IDAAKKSGILediLNSpMGF-ETIISESGNNFSGGQR 619
Cdd:PRK13631 110 NFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPVA---LGVkkSEAKKLAKFY---LNK-MGLdDSYLERSPFGLSGGQK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 620 QRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRL-RTIQNADKIIYLEDGMIKEIGTHEQ 695
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGTPYE 262
|
....*...
gi 446631050 696 LLKNRSYY 703
Cdd:PRK13631 263 IFTDQHII 270
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
493-694 |
1.33e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.64 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGsgkssisklllA-----------LYKVSEGQILINNKninDYDYHSLRTS----IGTVL 557
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENG-----------AgkstlmkilsgVYQPDSGEILLDGE---PVRFRSPRDAqaagIAIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 558 QESKLFSG-SISDNISMSKDNH-----DDLKVIDAAKKsgILEDiLNSPMGFETIISEsgnnFSGGQRQRLLVARALYQE 631
Cdd:COG1129 86 QELNLVPNlSVAENIFLGREPRrggliDWRAMRRRARE--LLAR-LGLDIDPDTPVGD----LSVAQQQLVEIARALSRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 632 PSAIVFDEATSHLdlfTERHIEN------TLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIkeIGTHE 694
Cdd:COG1129 159 ARVLILDEPTASL---TEREVERlfriirRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRL--VGTGP 223
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
189-424 |
1.68e-07 |
|
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: 53.61 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 189 NAFSNSDINKLNSFG--WLIIIFSISFV--LMSLLRGISIALLQKSLDLSIMNDFMKKMFHLPYSFFD--NRSSGDLLFR 262
Cdd:cd18578 37 SVFSLPDDDELRSEAnfWALMFLVLAIVagIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 263 -ANSAVFIRDIISTTMITIFIDLLLIIT-----------YTAVMInfsldlsllllslsmllAVI------LFVNANVIR 324
Cdd:cd18578 117 lSTDASDVRGLVGDRLGLILQAIVTLVAgliiafvygwkLALVGL-----------------ATVpllllaGYLRMRLLS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 325 KMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKrlslWSGNYSKELESSQRLNIFQAVIHTIT-GFFQvSVPL----L 399
Cdd:cd18578 180 GFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDY----FLEKYEEALEEPLKKGLRRALISGLGfGLSQ-SLTFfayaL 254
|
250 260
....*....|....*....|....*.
gi 446631050 400 VLWVGGHALINGEITLGT-LIAFSSI 424
Cdd:cd18578 255 AFWYGGRLVANGEYTFEQfFIVFMAL 280
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
475-704 |
1.96e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 53.57 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 475 DIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKL---LLALYKVSEGQILINNK---NINDYDYHS 548
Cdd:PRK09473 14 DVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFAlmgLLAANGRIGGSATFNGReilNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 549 LR------------TS------IGTVLQES-KLFSGsisdnisMSKDN--HDDLKVIDAAKKSGILEDILNSPmgfetii 607
Cdd:PRK09473 94 LRaeqismifqdpmTSlnpymrVGEQLMEVlMLHKG-------MSKAEafEESVRMLDAVKMPEARKRMKMYP------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 608 sesgNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYL 682
Cdd:PRK09473 160 ----HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkrefNTAIIMITHDLGVVAGiCDKVLVM 235
|
250 260
....*....|....*....|..
gi 446631050 683 EDGMIKEIGTHEQLLKNRSYYY 704
Cdd:PRK09473 236 YAGRTMEYGNARDVFYQPSHPY 257
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
476-691 |
1.98e-07 |
|
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: 52.20 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGeKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDyDYHSLRTSIGT 555
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQEsklFSGsisdnismskdnHDDLKVIDAAKKSGILEDILNSP-----------MGFETIISESGNNFSGGQRQRLLV 624
Cdd:cd03264 77 LPQE---FGV------------YPNFTVREFLDYIAWLKGIPSKEvkarvdevlelVNLGDRAKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 625 ARALYQEPSAIVFDEATSHLDLfTERH-IENTLKELNITQIII--AHRLRTIQN-ADKIIYLEDGMIKEIG 691
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDP-EERIrFRNLLSELGEDRIVIlsTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
464-668 |
2.03e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 464 KSNVQAHSIKGDIKFENVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNK-NIN 542
Cdd:PRK11147 306 KMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 543 DYDYHSlrtsigTVLQESKlfsgSISDNISMSKD----NHDDLKVIdaakksGILEDILNSPMGFETIISEsgnnFSGGQ 618
Cdd:PRK11147 386 YFDQHR------AELDPEK----TVMDNLAEGKQevmvNGRPRHVL------GYLQDFLFHPKRAMTPVKA----LSGGE 445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446631050 619 RQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAH 668
Cdd:PRK11147 446 RNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSH 495
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
479-703 |
2.37e-07 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 52.34 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNqfSKYILKDLNFTIKQGEkvaIVGpsgsgkssiskLL--------------LALYKVSEGQILINNKNINDY 544
Cdd:COG1137 7 ENLVKSYG--KRTVVKDVSLEVNQGE---IVG-----------LLgpngagktttfymiVGLVKPDSGRIFLDGEDITHL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 545 D-YHSLRTSIGTVLQESKLFSG-SISDNI----SMSKdnhddlkvIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQ 618
Cdd:COG1137 71 PmHKRARLGIGYLPQEASIFRKlTVEDNIlavlELRK--------LSKKEREERLEELLEE-FGITHLRKSKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 619 RQRLLVARALYQEPSAIVFDE--------ATShlDLfteRHIENTLKELNITQIIIAHRLR-TIQNADK--IIYleDGMI 687
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEpfagvdpiAVA--DI---QKIIRHLKERGIGVLITDHNVReTLGICDRayIIS--EGKV 214
|
250
....*....|....*....
gi 446631050 688 KEIGTHEQLLKN---RSYY 703
Cdd:COG1137 215 LAEGTPEEILNNplvRKVY 233
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
430-700 |
3.72e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.44 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 430 TPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHSIKGDIKFENVNFKY--NQFSkyiLKDLNFTIKQGEKVA 507
Cdd:PRK10522 277 TPLLSAVGALPTLLSAQVAFNKLNKLALAPYKAEFPRPQAFPDWQTLELRNVTFAYqdNGFS---VGPINLTIKRGELLF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 508 IVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRtsigtvlqesKLFSGSISDNISMSKDNHDDLKVIDAA 587
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYR----------KLFSAVFTDFHLFDQLLGPEGKPANPA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 588 KKSGILEdILNspMGFETIISE---SGNNFSGGQRQRLLVARALYQEPSAIVFDEATS----HLDLFTERHIENTLKELN 660
Cdd:PRK10522 424 LVEKWLE-RLK--MAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAAdqdpHFRREFYQVLLPLLQEMG 500
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446631050 661 ITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTHEQLLKNR 700
Cdd:PRK10522 501 KTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASR 540
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
581-668 |
4.05e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 581 LKVIDA----AKKSGILEDILNSPmgfeTIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTL 656
Cdd:PLN03073 312 LELIDAytaeARAASILAGLSFTP----EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL 387
|
90
....*....|..
gi 446631050 657 KELNITQIIIAH 668
Cdd:PLN03073 388 LKWPKTFIVVSH 399
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
476-700 |
6.05e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 51.55 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSKyiLKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALY---KVSEGQILINNKNIN-----DYDYH 547
Cdd:PRK09984 5 IRVEKLAKTFNQHQA--LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQregrlARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 548 SLRTSIGTVLQESKLFSG-SISDNISMSKDNHDD-----LKVIDAAKKSGILEDIlnSPMGFETIISESGNNFSGGQRQR 621
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRlSVLENVLIGALGSTPfwrtcFSWFTREQKQRALQAL--TRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 622 LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLR-TIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINqndgITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
....
gi 446631050 697 LKNR 700
Cdd:PRK09984 241 DNER 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
493-691 |
6.70e-07 |
|
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: 50.93 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLrtsigTVLQESKLFSG-SISDNI 571
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 572 SMSKD--NHDdlkvIDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTE 649
Cdd:TIGR01184 76 ALAVDrvLPD----LSKSERRAIVEEHIAL-VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446631050 650 RHIENTL----KELNITQIIIAHRL-RTIQNADKIIYLEDGMIKEIG 691
Cdd:TIGR01184 151 GNLQEELmqiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
492-702 |
1.14e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.41 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLA--LYKVSEGQILINNKNINDYDyHSLRTSIGTVLQesklFSGSISD 569
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE-PEERAHLGIFLA----FQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 570 NismSKDNHDDLKVI-DAAKKSGILEDIlnSPMGFETIISESGN---------------NFSGGQRQRLLVARALYQEPS 633
Cdd:CHL00131 97 P---GVSNADFLRLAyNSKRKFQGLPEL--DPLEFLEIINEKLKlvgmdpsflsrnvneGFSGGEKKRNEILQMALLDSE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 634 AIVFDEATSHLDLFTERHIE---NTLKELNITQIIIAH--RLRTIQNADKIIYLEDGMIKEIGTHE--QLLKNRSY 702
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKGY 247
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
475-697 |
1.37e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.40 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 475 DIKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIG 554
Cdd:PRK11231 2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQE---------SKLFSGSISDNISM-----SKDNHddlKVIDAAKKSGILEdILNSPMgfetiisesgNNFSGGQRQ 620
Cdd:PRK11231 80 LLPQHhltpegitvRELVAYGRSPWLSLwgrlsAEDNA---RVNQAMEQTRINH-LADRRL----------TDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 621 RLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNI---TQIIIAHRL-RTIQNADKIIYLEDGMIKEIGTHEQL 696
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgkTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEV 225
|
.
gi 446631050 697 L 697
Cdd:PRK11231 226 M 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
476-703 |
1.66e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFSkyILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHS-LRTSIG 554
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 555 TVLQESKLFSG-SISDNISMSKdnhddlkviDAAKKSGILEDILNS----PMGFETIISESGnNFSGGQRQRLLVARALY 629
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGG---------FFAERDQFQERIKWVyelfPRLHERRIQRAG-TMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 630 QEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIahrLRTIQNADKIIYLED-GMIKEIG------THEQLLKN--- 699
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTI---FLVEQNANQALKLADrGYVLENGhvvledTGDALLANeav 230
|
....
gi 446631050 700 RSYY 703
Cdd:PRK11614 231 RSAY 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
614-699 |
2.39e-06 |
|
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: 50.84 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 614 FSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTIQN-ADKIIYLEDGMIK 688
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqrelGMALLLITHDLGVVRRfADRVAVMRQGEIV 236
|
90
....*....|.
gi 446631050 689 EIGTHEQLLKN 699
Cdd:COG4172 237 EQGPTAELFAA 247
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
476-689 |
3.07e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 49.83 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNqfSKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDyDYHSLRTSIGT 555
Cdd:PRK13536 42 IDLAGVSKSYG--DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQesklfsgsiSDNISMSKDNHDDLKVIDA--AKKSGILEDILNSPMGFETIISESG---NNFSGGQRQRLLVARALYQ 630
Cdd:PRK13536 119 VPQ---------FDNLDLEFTVRENLLVFGRyfGMSTREIEAVIPSLLEFARLESKADarvSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 631 EPSAIVFDEATSHLDLFTeRHientlkelnitqiIIAHRLRTIQNADKIIYLEDGMIKE 689
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHA-RH-------------LIWERLRSLLARGKTILLTTHFMEE 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
615-697 |
3.54e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTI-QNADKIIYLEDGMIKE 689
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqqelNMGLLFITHNLSIVrKLADRVAVMQNGRCVE 237
|
....*...
gi 446631050 690 IGTHEQLL 697
Cdd:PRK15134 238 QNRAATLF 245
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
591-668 |
3.58e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.28 E-value: 3.58e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 591 GILEDILNSPMgfetiisesgNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAH 668
Cdd:PRK15064 143 GIPEEQHYGLM----------SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISH 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
493-673 |
3.58e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.11 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINdydyHSLRTS-IGTVLQESKL---FSGSIS 568
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 569 DNISMSKDNHDDLKVIDAAKKSGILEDILNSPMGFETIISESGNnFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFT 648
Cdd:PRK15056 99 DVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....*...
gi 446631050 649 ERHIENTLKEL---NITQIIIAHRLRTI 673
Cdd:PRK15056 178 EARIISLLRELrdeGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
250-421 |
3.98e-06 |
|
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: 49.08 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 250 FFDNRSSGDLLFRANSAV--F---IRDIIS------TTMITIFIDLLLII-TYTAVMInfsldlsllllslSMLLAVILF 317
Cdd:cd18574 92 FFDTHRTGELVNRLTADVqeFkssFKQCVSqglrsvTQTVGCVVSLYLISpKLTLLLL-------------VIVPVVVLV 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 318 --VNANVIRKMTKKnIQDKV-NTQAVLTENMYNIVDIKSLGLEKKRLSLwsgnYSKELESSQRLN--------IFQAVih 386
Cdd:cd18574 159 gtLYGSFLRKLSRR-AQAQVaKATGVADEALGNIRTVRAFAMEDRELEL----YEEEVEKAAKLNeklglgigIFQGL-- 231
|
170 180 190
....*....|....*....|....*....|....*
gi 446631050 387 tiTGFFQVSVPLLVLWVGGHALINGEITLGTLIAF 421
Cdd:cd18574 232 --SNLALNGIVLGVLYYGGSLVSRGELTAGDLMSF 264
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
492-684 |
4.58e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 48.25 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGsgkSSISKLLLAL-------YKVSeGQILINNKNINDYDYHSLRtsIGTVLQESKLFS 564
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSG---SGKSTLLAAIagtlspaFSAS-GEVLLNGRRLTALPAEQRR--IGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 565 G-SISDNI------SMSKDNHDDLkvIDAAkksgiLEDILNSPMGFETIISesgnnFSGGQRQRLLVARALYQEPSAIVF 637
Cdd:COG4136 90 HlSVGENLafalppTIGRAQRRAR--VEQA-----LEEAGLAGFADRDPAT-----LSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 638 DEATSHLD----------LFTErhientLKELNITQIIIAHRLRTIQNADKIIYLED 684
Cdd:COG4136 158 DEPFSKLDaalraqfrefVFEQ------IRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
398-696 |
4.74e-06 |
|
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: 49.80 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 398 LLVLWVGGHALINGEITLGTLIAFSSIagsyITPIVSVSNNYTQLISLGSYFSRIKDVLRTKDEQEKSNVQAHSIKGD-- 475
Cdd:COG4615 249 LILFLLPALGWADPAVLSGFVLVLLFL----RGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPad 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 ---IKFENVNFKY------NQFSkyiLKDLNFTIKQGEKVAIVGpsgsgkssISKLLLALYKVSEGQILINNKNINDYDY 546
Cdd:COG4615 325 fqtLELRGVTYRYpgedgdEGFT---LGPIDLTIRRGELVFIVGgngsgkstLAKLLTGLYRPESGEILLDGQPVTADNR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 547 HSLRTSIGTVlqesklFSgsisdnismskDNH--DDLKVIDAAKKSGILEDILNSpMGFETIISESGNNF-----SGGQR 619
Cdd:COG4615 402 EAYRQLFSAV------FS-----------DFHlfDRLLGLDGEADPARARELLER-LELDHKVSVEDGRFsttdlSQGQR 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 620 QRL-LVArALYQEPSAIVFDEATSHLD-----LFTeRHIENTLKELNITQIIIAHRLRTIQNADKIIYLEDGMIKEIGTH 693
Cdd:COG4615 464 KRLaLLV-ALLEDRPILVFDEWAADQDpefrrVFY-TELLPELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVELTGP 541
|
...
gi 446631050 694 EQL 696
Cdd:COG4615 542 AAL 544
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
476-689 |
4.98e-06 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.03 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSlRTSIGT 555
Cdd:PRK13537 8 IDFRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKL---FSgsISDNI-------SMSKDNHDDL--KVIDAAKksgiLEDILNSPMGfetiisesgnNFSGGQRQRLL 623
Cdd:PRK13537 85 VPQFDNLdpdFT--VRENLlvfgryfGLSAAAARALvpPLLEFAK----LENKADAKVG----------ELSGGMKRRLT 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 624 VARALYQEPSAIVFDEATSHLDLfTERHientlkelnitqiIIAHRLRTIQNADKIIYLEDGMIKE 689
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDP-QARH-------------LMWERLRSLLARGKTILLTTHFMEE 200
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
164-428 |
5.56e-06 |
|
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: 48.62 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 164 GLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLnsFGWLIIIFSISFVLMSllrgISIALLQKS---LDLSIMNDFM 240
Cdd:cd18577 14 ALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKY--ALYFVYLGIGSFVLSY----IQTACWTITgerQARRIRKRYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 241 KKMFHLPYSFFDNRSSGDLLFRANSAVF-IRDIISTTM------ITIFI-----------DLLLIITYTAVMInfsldls 302
Cdd:cd18577 88 KALLRQDIAWFDKNGAGELTSRLTSDTNlIQDGIGEKLglliqsLSTFIagfiiafiyswKLTLVLLATLPLI------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 303 llllslsmllAVILFVNANVIRKMTKKniQDKVNTQA--VLTENMYNIVDIKSLGLEKKRLSlwsgNYSKELESSQRLNI 380
Cdd:cd18577 161 ----------AIVGGIMGKLLSKYTKK--EQEAYAKAgsIAEEALSSIRTVKAFGGEEKEIK----RYSKALEKARKAGI 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 381 FQAVIHTI-TGFFQVSVPL---LVLWVGGHALINGEITLGTLIA--FSSIAGSY 428
Cdd:cd18577 225 KKGLVSGLgLGLLFFIIFAmyaLAFWYGSRLVRDGEISPGDVLTvfFAVLIGAF 278
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
162-295 |
5.67e-06 |
|
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: 48.65 E-value: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 162 FFGLVFLSIIIQGLMTVIPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMK 241
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446631050 242 KMFHLPYSFFDNRSSGDLLFRansavFIRDI--ISTTMITIFIDLLLIITYTAVMI 295
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNR-----FSKDIglIDEELPLALLDFLQSLFSVLGSL 131
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
159-442 |
8.69e-06 |
|
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: 48.02 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 159 KGRFFGLVFLSIIIQGLMTVIPLSTKWVTDNaFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIAL---LQKSLDLSI 235
Cdd:cd18556 1 KLLFFSILFISLLSSILISISPVILAKITDL-LTSSSSDSYNYIVVLAALYVITISATKLLGFLSLYLqssLRVELIISI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 236 MNDFMKKMFHLPYSFFDNRSSGDLLFRANSA-----VFIRDIISTtmitiFIDLLLIITYTAVMINFSLDLSLLLLSLSM 310
Cdd:cd18556 80 SSSYFRYLYEQPKTFFVKENSGDITQRLNQAsndlyTLVRNLSTN-----ILPPLLQLIIAIVVILSSGDYFVAALFLLY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 311 llaVILFVNANVI--RKMTK---KNIQDKVNTQAVLTENMYNIVDIKSLG------------LEKKRLSlwSGNYSKELE 373
Cdd:cd18556 155 ---AVLFVINNTIftKKIVSlrnDLMDAGRKSYSLLTDSVKNIVAAKQNNafdflfkryeatLTNDRNS--QKRYWKLTF 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 374 SSQRLNIFQAVIhtitgFFQVSVpLLVLwvggHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQL 442
Cdd:cd18556 230 KMLILNSLLNVI-----LFGLSF-FYSL----YGVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSEL 288
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
578-689 |
9.72e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 578 HDDLKVIDA----AKKSGILedilnSPMGF-ETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHI 652
Cdd:PRK10636 114 HGKLDAIDAwtirSRAASLL-----HGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWL 188
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446631050 653 ENTLKELNITQIIIAHR---LRTIqnADKIIYLEDGMIKE 689
Cdd:PRK10636 189 EKWLKSYQGTLILISHDrdfLDPI--VDKIIHIEQQSLFE 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
476-670 |
1.15e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.42 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINnknindydyHSLRtsIGT 555
Cdd:PRK09544 5 VSLENVSVSFGQ--RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 556 VLQESKLfsgsisdNISMSKDNHDDLKVIDAAKKSGIL--------EDILNSPMgfetiisesgNNFSGGQRQRLLVARA 627
Cdd:PRK09544 72 VPQKLYL-------DTTLPLTVNRFLRLRPGTKKEDILpalkrvqaGHLIDAPM----------QKLSGGETQRVLLARA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446631050 628 LYQEPSAIVFDEATSHLDLFTERH----IENTLKELNITQIIIAHRL 670
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVDVNGQVAlydlIDQLRRELDCAVLMVSHDL 181
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
493-659 |
1.34e-05 |
|
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: 46.27 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYH-SLRTSIGTVLQESK---LFSG-SI 567
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIAYVPEDRKregLVLDlSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNISMSkdnhddlkvidaakksgileDILnspmgfetiisesgnnfSGGQRQRLLVARALYQEPSAIVFDEATSHLDLF 647
Cdd:cd03215 96 AENIALS--------------------SLL-----------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170
....*....|..
gi 446631050 648 TERHIENTLKEL 659
Cdd:cd03215 139 AKAEIYRLIREL 150
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
614-697 |
1.51e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 614 FSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHRL---RTIqnADKIIYLEDGM 686
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRglvrELGLAVVIVTHDLavaRLL--AHRLLVMKQGR 229
|
90
....*....|.
gi 446631050 687 IKEIGTHEQLL 697
Cdd:PRK11701 230 VVESGLTDQVL 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
472-690 |
1.54e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 472 IKGDIKFENVNFKYNQFSKyiLKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN-DYDYHSLR 550
Cdd:PRK09700 260 LAHETVFEVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 551 TSIGTVLQ---ESKLFSG-SISDNISMSK--------------DNHDDLKVIDAAKKsgILEDILNSpmgfetiISESGN 612
Cdd:PRK09700 338 KGMAYITEsrrDNGFFPNfSIAQNMAISRslkdggykgamglfHEVDEQRTAENQRE--LLALKCHS-------VNQNIT 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 613 NFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQNA-DKIIYLEDGMIK 688
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaddGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
|
..
gi 446631050 689 EI 690
Cdd:PRK09700 489 QI 490
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
492-645 |
1.57e-05 |
|
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: 46.33 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIndydyHSLRTSIgtvlQESKLFSG------ 565
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-----DFQRDSI----ARGLLYLGhapgik 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 566 ---SISDNISMSKDNHDDLKVIDAAKKSGIledilnspMGFETIISesgNNFSGGQRQRLLVARALYQEPSAIVFDEATS 642
Cdd:cd03231 86 ttlSVLENLRFWHADHSDEQVEEALARVGL--------NGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
...
gi 446631050 643 HLD 645
Cdd:cd03231 155 ALD 157
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
493-690 |
1.58e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYH-SLRTSIGTVLQE-SKLFSGSISDN 570
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 571 ISMSKdnHDDLKV-----IDAAKKSGILEDILNSpMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLD 645
Cdd:PRK09700 101 LYIGR--HLTKKVcgvniIDWREMRVRAAMMLLR-VGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 646 ------LFTerhIENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDG------MIKEI 690
Cdd:PRK09700 178 nkevdyLFL---IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGssvcsgMVSDV 232
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
375-452 |
1.86e-05 |
|
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: 47.10 E-value: 1.86e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 375 SQRLN-IFQAVIHTITGFFQVsvplLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSNNYTQLISLGSYFSRI 452
Cdd:cd18546 218 AQRLVaIYFPGVELLGNLATA----AVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
615-680 |
1.96e-05 |
|
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: 45.78 E-value: 1.96e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 615 SGGQRQRLLVARALYQEP--SAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHRLRTIQNADKII 680
Cdd:cd03238 89 SGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEHNLDVLSSADWII 159
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
493-694 |
1.99e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 47.71 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGsgkssisklllA-----------LYKVSEGQILINNK--NINDYDyHSLRTSIGTVLQE 559
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENG-----------AgkstlmkilygLYQPDSGEILIDGKpvRIRSPR-DAIALGIGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 560 SKLFSG-SISDNISMSKDNHDDLkVIDAAKKSGILEDILNSpMGFE----TIISEsgnnFSGGQRQRLLVARALYQEPSA 634
Cdd:COG3845 89 FMLVPNlTVAENIVLGLEPTKGG-RLDRKAARARIRELSER-YGLDvdpdAKVED----LSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 635 IVFDEATSHL------DLFTerhienTLKEL---NITQIIIAHRLRTI-QNADKIIYLEDGmiKEIGTHE 694
Cdd:COG3845 163 LILDEPTAVLtpqeadELFE------ILRRLaaeGKSIIFITHKLREVmAIADRVTVLRRG--KVVGTVD 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
615-695 |
2.42e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTER----HIENTLKELNITQIIIAHRLRTI-QNADKIIYLEDGMIKE 689
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRellpYLERLAREINIPILYVSHSLDEIlRLADRVVVLEQGKVKA 209
|
....*.
gi 446631050 690 IGTHEQ 695
Cdd:PRK11144 210 FGPLEE 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
615-698 |
2.53e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 47.04 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL----NITQIIIAHRLRTI-QNADKIIYLEDGMIKE 689
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqqkeNMALVLITHDLALVaEAAHKIIVMYAGQVVE 234
|
....*....
gi 446631050 690 IGTHEQLLK 698
Cdd:PRK11022 235 TGKAHDIFR 243
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
490-645 |
3.17e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 45.64 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSLRTSIG------TVLqesklf 563
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhrnamkPAL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 564 sgSISDNISMSKD--NHDDLKVIDAAKKSGiLEDILNSPmgfetiisesGNNFSGGQRQRLLVARAL-YQEPSAIVfDEA 640
Cdd:PRK13539 89 --TVAENLEFWAAflGGEELDIAAALEAVG-LAPLAHLP----------FGYLSAGQKRRVALARLLvSNRPIWIL-DEP 154
|
....*
gi 446631050 641 TSHLD 645
Cdd:PRK13539 155 TAALD 159
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
615-689 |
3.41e-05 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 45.93 E-value: 3.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQNADKIIYLEDGMIKE 689
Cdd:PRK10584 148 SGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNrehgTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
165-437 |
4.42e-05 |
|
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: 45.85 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 165 LVFLSIIIQGLMTV-IPLSTKWVTDNAFSNSDINKLNSFGWLIIIFSISFVLMSLLRGISIALLQKSLDLSIMNDFMKKM 243
Cdd:cd18548 3 LAPLFKLLEVLLELlLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 244 FHLPYSFFDNRSSGDLLFRANS---------AVFIRDIISTTMITIF-------IDLLLIITYTAVMInfsldlslllls 307
Cdd:cd18548 83 QSFSFAEIDKFGTSSLITRLTNdvtqvqnfvMMLLRMLVRAPIMLIGaiimafrINPKLALILLVAIP------------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 308 lsmllaVILFVNANVIRKMTK--KNIQ---DKVNTqaVLTENMYNIVDIKSLGL---EKKRLSLWSGNYSKeleSSQRLN 379
Cdd:cd18548 151 ------ILALVVFLIMKKAIPlfKKVQkklDRLNR--VVRENLTGIRVIRAFNRedyEEERFDKANDDLTD---TSLKAG 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446631050 380 IFQAVIH-TITGFFQVSVpLLVLWVGGHALINGEITLGTLIAFSSIAGSYITPIVSVSN 437
Cdd:cd18548 220 RLMALLNpLMMLIMNLAI-VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSM 277
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
489-699 |
4.53e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.91 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 489 SKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL---RTSIGTVLQESKLFSG 565
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 566 -SISDNISMSKDNHDDLKvidaakksgilEDILNSP--MGFETIISESGNN-----FSGGQRQRLLVARALYQEPSAIVF 637
Cdd:PRK11831 99 mNVFDNVAYPLREHTQLP-----------APLLHSTvmMKLEAVGLRGAAKlmpseLSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 638 DEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK11831 168 DEPFVGQDPITMGVLVKLISELNsalgVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQAN 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
615-697 |
4.94e-05 |
|
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: 46.25 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHI----ENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKE 689
Cdd:COG4148 135 SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIlpylERLRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVA 214
|
....*...
gi 446631050 690 IGTHEQLL 697
Cdd:COG4148 215 SGPLAEVL 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
494-687 |
6.04e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 494 KDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSlRTSIGTVL-----QESKLF-SGSI 567
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSGLYlDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 568 SDNISmSKDNHDDLKVIDAAKKSGILEDILNSpMGFE-TIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDL 646
Cdd:PRK15439 359 AWNVC-ALTHNRRGFWIKPARENAVLERYRRA-LNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446631050 647 FTERHIENTLKEL---NITQIIIAHRLRTI-QNADKIIYLEDGMI 687
Cdd:PRK15439 437 SARNDIYQLIRSIaaqNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
209-421 |
7.24e-05 |
|
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: 45.38 E-value: 7.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 209 FSISFVLMSLL----------RGISIALLQKSLDLSIMNDFMKKMFHLPYSFFDNRSSGDLLFRANS------------- 265
Cdd:cd18784 35 FSRAIIIMGLLaiassvaagiRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSdtttmsdtvslnl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 266 AVFIRDIISTTMITIFI-------DLLLIITYTAVMInfsldlsllllslsmllavILFVNANVIRKMTKKnIQDKV-NT 337
Cdd:cd18784 115 NIFLRSLVKAIGVIVFMfklswqlSLVTLIGLPLIAI-------------------VSKVYGDYYKKLSKA-VQDSLaKA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 338 QAVLTENMYNIVDIKSLGLEKKRLSlwsgNYSKELESSQRLNIFQAVIHT----ITGFFQVSVPLLVLWVGGHALINGEI 413
Cdd:cd18784 175 NEVAEETISSIRTVRSFANEDGEAN----RYSEKLKDTYKLKIKEALAYGgyvwSNELTELALTVSTLYYGGHLVITGQI 250
|
....*...
gi 446631050 414 TLGTLIAF 421
Cdd:cd18784 251 SGGNLISF 258
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
495-699 |
7.87e-05 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 45.60 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 495 DLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHslRTSIGTVLQESKLFSG-SISDNISM 573
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNIAF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 574 SkdnhddLKViDAAKKSGI---LEDILnSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLD--LFT 648
Cdd:PRK11607 115 G------LKQ-DKLPKAEIasrVNEML-GLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 649 ERHIE--NTLKELNITQIIIAH-RLRTIQNADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK11607 187 RMQLEvvDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
476-692 |
9.03e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 44.69 E-value: 9.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 476 IKFENVNFKYNQFS--------------------KYILKDLNFTIKQGEKVAIVGPSgsgkssiskLL--LA-LYKVSEG 532
Cdd:COG1134 5 IEVENVSKSYRLYHepsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNgag---kstLLklIAgILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 533 QILINNknindydyhslRTS----IGTVLQESklFSGsiSDNI-------SMSKDNHDDL--KVIDAAKksgiLEDILNS 599
Cdd:COG1134 82 RVEVNG-----------RVSalleLGAGFHPE--LTG--RENIylngrllGLSRKEIDEKfdEIVEFAE----LGDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 600 PMGfetiisesgnNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDL-FTER---HIENtLKELNITQIIIAHRLRTIQN 675
Cdd:COG1134 143 PVK----------TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAaFQKKclaRIRE-LRESGRTVIFVSHSMGAVRR 211
|
250
....*....|....*...
gi 446631050 676 -ADKIIYLEDGMIKEIGT 692
Cdd:COG1134 212 lCDRAIWLEKGRLVMDGD 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
490-691 |
9.84e-05 |
|
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: 44.45 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKnindydyhslrtsIGTVLQESKLFSGSIS- 568
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-------------VSSLLGLGGGFNPELTg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 569 -DNISMS------KDNHDDLKVIDAAKKSGiLEDILNSPMGfetiisesgnNFSGGQRQRLLVARALYQEPSAIVFDEAT 641
Cdd:cd03220 102 rENIYLNgrllglSRKEIDEKIDEIIEFSE-LGDFIDLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 642 SHLDLFT----ERHIENTLKELNITqIIIAHRLRTI-QNADKIIYLEDGMIKEIG 691
Cdd:cd03220 171 AVGDAAFqekcQRRLRELLKQGKTV-ILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
615-685 |
1.34e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.33 E-value: 1.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDG 685
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNmATRIVDLDRG 229
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
496-666 |
1.44e-04 |
|
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: 45.39 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 496 LNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNInDYDYHSLRTSIGTVLQESKLFSG-SISDNI--- 571
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHIlfy 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 572 -SMSKDNHDDLKVidaaKKSGILEDilnspMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTER 650
Cdd:TIGR01257 1028 aQLKGRSWEEAQL----EMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170
....*....|....*.
gi 446631050 651 HIENTLKELNITQIII 666
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTII 1114
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
612-668 |
1.74e-04 |
|
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: 44.93 E-value: 1.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 612 NNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAH 668
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTH 216
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
323-421 |
1.76e-04 |
|
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: 44.16 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 323 IRKMTKKNIQDKVNTQAVLTENMYNIVDIKSLGLEKKRLSLWSGNYSKELESSQRLNIFQAVIHTITGFF-QVSVpLLVL 401
Cdd:cd18780 166 VRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAaQLAI-VLVL 244
|
90 100
....*....|....*....|
gi 446631050 402 WVGGHALINGEITLGTLIAF 421
Cdd:cd18780 245 WYGGRLVIDGELTTGLLTSF 264
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
607-687 |
1.77e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.78 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 607 ISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAHRLRTIQNADKIIYL-EDG 685
Cdd:PRK10636 424 VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLvHDG 503
|
..
gi 446631050 686 MI 687
Cdd:PRK10636 504 KV 505
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
490-659 |
1.84e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 43.92 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 490 KYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSlrtsiGTVLQESKLFS-GSIS 568
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLPwRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 569 DNISMSKDnhddLKVIDAAKKSGILEDILNSpMGFEtiisESGNNF----SGGQRQRLLVARALYQEPSAIVFDEATSHL 644
Cdd:PRK11248 89 DNVAFGLQ----LAGVEKMQRLEIAHQMLKK-VGLE----GAEKRYiwqlSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170
....*....|....*
gi 446631050 645 DLFTERHIENTLKEL 659
Cdd:PRK11248 160 DAFTREQMQTLLLKL 174
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
479-700 |
2.22e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 479 ENVNFKYNQfsKYILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQIlinnknindydYHSLRTSIGTVLQ 558
Cdd:PRK15064 323 ENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 E-SKLFSGSISDNISMS---KDNHDDLKVidaakkSGILEDILNSpmgfETIISESGNNFSGGQRQRLLVARALYQEPSA 634
Cdd:PRK15064 390 DhAYDFENDLTLFDWMSqwrQEGDDEQAV------RGTLGRLLFS----QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446631050 635 IVFDEATSHLDLFTERHIENTLKELNITQIIIAH-RLRTIQNADKIIYL-EDGMIKEIGTHEQLLKNR 700
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHdREFVSSLATRIIEItPDGVVDFSGTYEEYLRSQ 527
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
615-698 |
2.41e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 44.27 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL---NITQIIIAHR--LRTIQNADKIIYLEDGMIKE 689
Cdd:TIGR00955 168 SGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaqkGKTIICTIHQpsSELFELFDKIILMAEGRVAY 247
|
....*....
gi 446631050 690 IGTHEQLLK 698
Cdd:TIGR00955 248 LGSPDQAVP 256
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
492-648 |
2.68e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 43.31 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 492 ILKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN--DYDyhslRtsiGTVLQESKLFSG-SIS 568
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpGAD----R---GVVFQKDALLPWlNVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 569 DNISMSkdnhddLKV--IDAAKKSGILEDILnSPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLDL 646
Cdd:COG4525 95 DNVAFG------LRLrgVPKAERRARAEELL-ALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
..
gi 446631050 647 FT 648
Cdd:COG4525 168 LT 169
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
480-685 |
2.90e-04 |
|
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: 42.63 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 480 NVNFKYNQFSKYILKDLNFTIKQGEKVAIVGPsgsGKSSISKLLLALYKVSEGQILINNK-NINDYDYHslrtsigtvlQ 558
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGR---PGSGCSTLLKALANRTEGNVSVEGDiHYNGIPYK----------E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 559 ESKLFSGSISDNismskdNHDDLKVidaakKSGILEDILnspmgfETIISESGNNF----SGGQRQRLLVARALYQEPSA 634
Cdd:cd03233 77 FAEKYPGEIIYV------SEEDVHF-----PTLTVRETL------DFALRCKGNEFvrgiSGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446631050 635 IVFDEATSHLDLFTERHIENTLK----ELNITQIIIAHR--LRTIQNADKIIYLEDG 685
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRtmadVLKTTTFVSLYQasDEIYDLFDKVLVLYEG 196
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
202-432 |
3.73e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 43.32 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 202 FGWLIIIFSISFVLMSL---LRGISIALLQKSLDLSIMNDFMKKMFHLPYSFFDNRSSGDLLFRANSAV---------FI 269
Cdd:cd18565 53 LWLLGGLTVAAFLLESLfqyLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVnqlerflddGA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 270 RDII--STTMITIFIDLLLI------ITYTAVminfsldlsllllslsmllAVILFVNANVIRKMTKK--NIQDKV---N 336
Cdd:cd18565 133 NSIIrvVVTVLGIGAILFYLnwqlalVALLPV-------------------PLIIAGTYWFQRRIEPRyrAVREAVgdlN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 337 TQavLTENMYNIVDIKSLG---LEKKRLSLWSGNYSKELESSQRLNI-FQAVIHTITGFFQVsvplLVLWVGGHALING- 411
Cdd:cd18565 194 AR--LENNLSGIAVIKAFTaedFERERVADASEEYRDANWRAIRLRAaFFPVIRLVAGAGFV----ATFVVGGYWVLDGp 267
|
250 260
....*....|....*....|....*.
gi 446631050 412 -----EITLGTLIAFSSIAGSYITPI 432
Cdd:cd18565 268 plftgTLTVGTLVTFLFYTQRLLWPL 293
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
497-699 |
4.14e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 42.67 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 497 NFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNINDYDYHSL-RTSIGTVLQESKLF-SGSISDNISMS 574
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFrEMTVIENLLVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 575 KDNHddlkvidaaKKSGILEDILNSP-------------------MGFETIISESGNNFSGGQRQRLLVARALYQEPSAI 635
Cdd:PRK11300 105 QHQQ---------LKTGLFSGLLKTPafrraesealdraatwlerVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446631050 636 VFDEATSHL------DLftERHIENTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGMIKEIGTHEQLLKN 699
Cdd:PRK11300 176 MLDEPAAGLnpketkEL--DELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNN 244
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
554-670 |
4.30e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQE--SKLFSGSIS--------DNISMSKDNhddlKVIDAAKK---SGILEDILnSPMGFETIISESGNNFSGGQRQ 620
Cdd:PRK13409 145 GTELQNyfKKLYNGEIKvvhkpqyvDLIPKVFKG----KVRELLKKvdeRGKLDEVV-ERLGLENILDRDISELSGGELQ 219
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 446631050 621 RLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKEL--NITQIIIAHRL 670
Cdd:PRK13409 220 RVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELaeGKYVLVVEHDL 271
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
615-696 |
4.79e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQ----IIIAHRLRTIQN-ADKIIYLEDGMIKE 689
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRalgmLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
....*..
gi 446631050 690 IGTHEQL 696
Cdd:PRK10418 222 QGDVETL 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
493-692 |
6.00e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVS--EGQILINN-----KNINDydyhSLRTSIGTVLQESKLFSG 565
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGeelqaSNIRD----TERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 566 -SISDNISMSKDNH-----DDLKVIDAAKKsgILEDiLNSPMGFETIISESGnnfsGGQRQRLLVARALYQEPSAIVFDE 639
Cdd:PRK13549 97 lSVLENIFLGNEITpggimDYDAMYLRAQK--LLAQ-LKLDINPATPVGNLG----LGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 640 ATSHLdlfTERHIE------NTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGmiKEIGT 692
Cdd:PRK13549 170 PTASL---TESETAvlldiiRDLKAHGIACIYISHKLNEVKAiSDTICVIRDG--RHIGT 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
499-645 |
6.64e-04 |
|
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: 42.01 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 499 TIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKNIN--------DYDyhslrtsiGTVlqesklfsgsisDN 570
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYE--------GTV------------RD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 571 ISMSKDNhddlkviDAAKKSGILEDILNsPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATSHLD 645
Cdd:cd03237 81 LLSSITK-------DFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
493-641 |
9.55e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.31 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGpsgsgkssiskLL------LA-----LYKVSEGQILINNKNIndyDYHSLRTSI--GTVL-- 557
Cdd:COG1129 268 VRDVSFSVRAGEILGIAG-----------LVgagrteLAralfgADPADSGEIRLDGKPV---RIRSPRDAIraGIAYvp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 558 ---QESKLFSG-SISDNISMSkdNHDDLK---VIDAAKKSGILEDILNS----PMGFETIISesgnNFSGGQRQRLLVAR 626
Cdd:COG1129 334 edrKGEGLVLDlSIRENITLA--SLDRLSrggLLDRRRERALAEEYIKRlrikTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170
....*....|....*
gi 446631050 627 ALYQEPSAIVFDEAT 641
Cdd:COG1129 408 WLATDPKVLILDEPT 422
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
495-697 |
9.79e-04 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 42.12 E-value: 9.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 495 DLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVS-EGQILINNKNINDYD-YHSLRTSIGTVLQESKLfSGSISD--- 569
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKR-HGIVPIlgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 570 --NISMSK-DNHDDLKVIDAAKKSG-ILEDI----LNSPMGFETIISesgnnFSGGQRQRLLVARALYQEPSAIVFDEAT 641
Cdd:TIGR02633 357 gkNITLSVlKSFCFKMRIDAAAELQiIGSAIqrlkVKTASPFLPIGR-----LSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446631050 642 SHLDLFTERHIE---NTLKELNITQIIIAHRLRTIQN-ADKIIYLEDG-----MIKEIGTHEQLL 697
Cdd:TIGR02633 432 RGVDVGAKYEIYkliNQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGklkgdFVNHALTQEQVL 496
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
563-645 |
1.15e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 563 FSGSISDNISMSKDNHDDlkvidaakkSGILEDILNsPMGFETIISESGNNFSGGQRQRLLVARALYQEPSAIVFDEATS 642
Cdd:PRK13409 413 YDGTVEDLLRSITDDLGS---------SYYKSEIIK-PLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482
|
...
gi 446631050 643 HLD 645
Cdd:PRK13409 483 HLD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
554-650 |
1.49e-03 |
|
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: 41.69 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 554 GTVLQE--SKLFSGSIS--------DNISMSKDNhddlKVIDAAKK---SGILEDILnSPMGFETIISESGNNFSGGQRQ 620
Cdd:COG1245 145 GTELQDyfKKLANGEIKvahkpqyvDLIPKVFKG----TVRELLEKvdeRGKLDELA-EKLGLENILDRDISELSGGELQ 219
|
90 100 110
....*....|....*....|....*....|
gi 446631050 621 RLLVARALYQEPSAIVFDEATSHLDLFtER 650
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDIY-QR 248
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
493-645 |
2.10e-03 |
|
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: 40.11 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVSEGQILINNKN-------INDYDYHSLR-TSIGTVLQesklFs 564
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqASPREILALRrRTIGYVSQ----F- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 565 gsisdnismskdnhddLKVI---------------------DAAKKSGILEDILNSPmgfETIISESGNNFSGGQRQRLL 623
Cdd:COG4778 102 ----------------LRVIprvsaldvvaepllergvdreEARARARELLARLNLP---ERLWDLPPATFSGGEQQRVN 162
|
170 180
....*....|....*....|..
gi 446631050 624 VARALYQEPSAIVFDEATSHLD 645
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLD 184
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
615-668 |
2.35e-03 |
|
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: 41.07 E-value: 2.35e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446631050 615 SGGQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQIIIAH 668
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISH 498
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
493-645 |
3.27e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.78 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGpsgsgkssiskLLLALYKVSEGQILINNKNINDYDYHSL-----------RTSIGTVLqesk 561
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGvagngqselaeALAGLRPPASGSIRLDGEDITGLSPRERrrlgvayipedRLGRGLVP---- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 562 lfSGSISDNISMskDNHD----------DLKVIDA-AKKsgILE--DI----LNSPMGfetiisesgnNFSGGQRQRLLV 624
Cdd:COG3845 350 --DMSVAENLIL--GRYRrppfsrggflDRKAIRAfAEE--LIEefDVrtpgPDTPAR----------SLSGGNQQKVIL 413
|
170 180
....*....|....*....|.
gi 446631050 625 ARALYQEPSAIVFDEATSHLD 645
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
617-697 |
3.72e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 617 GQRQRLLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELN----ITQIIIAHRLRTI-QNADKIIYLEDGMIKEIG 691
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqnnnTTILLISHDLQMLsQWADKINVLYCGQTVETA 241
|
....*.
gi 446631050 692 THEQLL 697
Cdd:PRK15093 242 PSKELV 247
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
615-680 |
4.22e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.49 E-value: 4.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446631050 615 SGGQRQR----LLVARALYQEPSAIVFDEATSHLDLFTERHIENTLKELNITQ---IIIAHRLRTIQNADKII 680
Cdd:cd03227 79 SGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGaqvIVITHLPELAELADKLI 151
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
493-692 |
9.76e-03 |
|
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: 39.04 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 493 LKDLNFTIKQGEKVAIVGPSGSGKSSISKLLLALYKVS--EGQIL-----INNKNINDYDyhslRTSIGTVLQESKLFSG 565
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYwsgspLKASNIRDTE----RAGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446631050 566 -SISDNISMSKD-------NHDDLKVIDAAKksgILEDILNSPMGFETIISESGnnfsGGQRQRLLVARALYQEPSAIVF 637
Cdd:TIGR02633 93 lSVAENIFLGNEitlpggrMAYNAMYLRAKN---LLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446631050 638 DEATSHLdlfTERHIE------NTLKELNITQIIIAHRLRTIQN-ADKIIYLEDGmiKEIGT 692
Cdd:TIGR02633 166 DEPSSSL---TEKETEilldiiRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG--QHVAT 222
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