|
Name |
Accession |
Description |
Interval |
E-value |
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
9-707 |
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: 601.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 9 KKRLPLIRQTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPC 88
Cdd:COG2274 1 RRKVPFVLQMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 89 ILHWNMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALELMPSSDFTVRdERKKIHLRQLTGKTPGLLAAMS 168
Cdd:COG2274 81 ILHWDGNHFVVLEGVDGDKVTIADPATGRRKLSLEEFAESWTGVALLLEPTPEFDKR-GEKPFGLRWFLRLLRRYRRLLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 169 RIITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHL 248
Cdd:COG2274 160 QVLLASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 249 VRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSL 328
Cdd:COG2274 240 LRLPLSFFESRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 329 RQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILWK 408
Cdd:COG2274 320 RRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 409 GAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERLADIVLTPTEgnqqqtaQENNSTSTTPSIFQE 488
Cdd:COG2274 400 GAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE-------REEGRSKLSLPRLKG 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 489 RVtedtdlplTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDY 568
Cdd:COG2274 473 DI--------ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDP 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 569 YQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLAR 648
Cdd:COG2274 545 ASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIAR 624
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 649 ALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP--VLLIAHRPETIASADRVLYLTDG 707
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRLADRIIVLDKG 685
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
153-707 |
1.30e-105 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 334.06 E-value: 1.30e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 153 LRQLTGKTPGLLAAMsriITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITL 232
Cdd:COG1132 12 LLRYLRPYRGLLILA---LLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 233 SVNFNMQWTARVFHHLVRLPLAWFDARSRGSVNARF-DAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAV 311
Cdd:COG1132 89 AQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLtNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 312 LAAVIYGVMRTLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYD 391
Cdd:COG1132 169 LVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 392 IAHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERLADIVLTPTEGNQQQ 471
Cdd:COG1132 249 PLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 472 TAQEnnststtpsifqervTEDTDLPLTLTHIAFSHKGsNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLP 551
Cdd:COG1132 329 GAVP---------------LPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 552 NEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGE 631
Cdd:COG1132 393 TSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGE 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 632 TGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP--VLLIAHRPETIASADRVLYLTDG 707
Cdd:COG1132 473 RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
166-457 |
2.65e-104 |
|
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: 320.56 E-value: 2.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 166 AMSRIITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVF 245
Cdd:cd18567 3 ALLQILLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 246 HHLVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWY 325
Cdd:cd18567 83 RHLLRLPLSYFEKRHLGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 326 PSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAII 405
Cdd:cd18567 163 PPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 406 LWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERL 457
Cdd:cd18567 243 IYLGALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKLFELRMLRLHLERL 294
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
11-707 |
4.31e-99 |
|
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: 320.74 E-value: 4.31e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 11 RLPLIRQTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCIL 90
Cdd:TIGR03796 1 RTPTVLQMEAVECGAASLAMILAYYGRYVPLEELREECGVSRDGSKASNLLKAARSYGLEAKGFRKELDALAELPLPYIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 91 HWNMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALELMPSSDFTvRDERKKIHLRQLTGKTPGLLAAMSRI 170
Cdd:TIGR03796 81 FWNFNHFVVVEGFRGGRVYLNDPALGPRTVSLEEFDESFTGVVLTFEPGPEFQ-KGGRKPSLLRALWRRLRGSRGALLYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 171 ITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLVR 250
Cdd:TIGR03796 160 LLAGLLLVLPGLVIPAFSQIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 251 LPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVmrtLWYPSLRQ 330
Cdd:TIGR03796 240 LPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVL---ALQLVSRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 331 SAEDA----WDAGaRESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIIL 406
Cdd:TIGR03796 317 RVDANrrlqQDAG-KLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 407 WKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDkfFAWRMLDVYNE--RLADiVLTPTEGNQQQTAQENNSTSTTPS 484
Cdd:TIGR03796 396 VVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVG--FGGTLQELEGDlnRLDD-VLRNPVDPLLEEPEGSAATSEPPR 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 485 IFQERVtedtdlplTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT 564
Cdd:TIGR03796 473 RLSGYV--------ELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPRE 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 565 hpdyyQIRRRI-----GTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGG 639
Cdd:TIGR03796 545 -----EIPREVlansvAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGG 619
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 640 QKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERG 687
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
24-707 |
4.87e-85 |
|
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: 283.17 E-value: 4.87e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 24 GLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCILhWNMNHFVVLHKV 103
Cdd:TIGR01846 1 GLEALSLLAQVHNIAVTPSQLRHMLGHAGASLDDLEILLAAKQLGLKAKAVKVSIGRLNKLPLPALI-DGEGGWFVLGKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 104 RRSRLVIHDPDKGKI-TLSLQDAGKHFTGvalELMPSSDFTVRDERKKIHLRQLTGKTPGLLAAMSRIITFALSLEILTL 182
Cdd:TIGR01846 80 TANGVTIYDPPGDAPeVLSREVLEALWSG---TVILLATRSVAGKALKFGFSWFIPAIIRYRKQFREVLLISLALQLFAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 183 GSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLVRLPLAWFDARSRG 262
Cdd:TIGR01846 157 VTPLLFQVVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 263 SVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLRQSAEDAWDAGARE 342
Cdd:TIGR01846 237 DTVARVRELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 343 SGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILWKGAGEVLNGTFTVGM 422
Cdd:TIGR01846 317 TSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 423 LVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERLADIVLTPTEGNQQqtaqennSTSTTPSIfqervtedtDLPLTLTH 502
Cdd:TIGR01846 397 LVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSA-------GLAALPEL---------RGAITFEN 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 503 IAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQED 582
Cdd:TIGR01846 461 IRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 583 HLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:TIGR01846 541 VLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEA 620
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 749181994 663 TSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDG 707
Cdd:TIGR01846 621 TSALDYESEALIMRNMREICRgrTVIIIAHRLSTVRACDRIIVLEKG 667
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
68-707 |
3.26e-73 |
|
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: 251.03 E-value: 3.26e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 68 QLSSRAVRLEPEDLKSLSLPCILHWNMNHF-VVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALELMPSSdftvrd 146
Cdd:TIGR03797 43 RLRIRRVRLEGGWWRQDSGPLLAYTAEDGRpVALLPVSRGGYEIFDPATGTRRRVDAAMAATLAPEAYMFYRPL------ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 147 ERKKIHLRQL-------TGKTPGLLAAMSRIITfalsleILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQM 219
Cdd:TIGR03797 117 PDKALGLRDLlrfalrgARRDLLAILAMGLLGT------LLGMLVPIATGILIGTAIPDADRSLLVQIALALLAAAVGAA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 220 llslACQWAS--ITLSVNFNMQWT--ARVFHHLVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTA 295
Cdd:TIGR03797 191 ----AFQLAQslAVLRLETRMDASlqAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLLSGIFALLN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 296 LCMMLLYSPEMTLIAV-LAAVIYGVMRTLWYPSLRQSAEdAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNV 374
Cdd:TIGR03797 267 LGLMFYYSWKLALVAVaLALVAIAVTLVLGLLQVRKERR-LLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 375 TRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFF-AWRMLDVY 453
Cdd:TIGR03797 346 RQRKLELSAQRIENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLIsILAVIPLW 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 454 nERLADIVltptegnqqQTAQENNSTSTTPSIFQERVTedtdlpltLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGK 533
Cdd:TIGR03797 426 -ERAKPIL---------EALPEVDEAKTDPGKLSGAIE--------VDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGP 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 534 SGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFfSEDRNHERMIQCARLAL 613
Cdd:TIGR03797 488 SGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAG-GAPLTLDEAWEAARMAG 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 614 IDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHRPE 693
Cdd:TIGR03797 567 LAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTRIVIAHRLS 646
|
650
....*....|....
gi 749181994 694 TIASADRVLYLTDG 707
Cdd:TIGR03797 647 TIRNADRIYVLDAG 660
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
17-707 |
9.60e-69 |
|
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: 239.26 E-value: 9.60e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 17 QTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPE--DLKSLSLPCILHWNM 94
Cdd:TIGR01193 1 QVDEKDCGIAALSMILKKYGTEYSLAKLRQLAKTDLEGTTVLGLVKAAEYLNFEAKAIQADMSlfEDKNLPLPFIAHVIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 95 N----HFVVLHKVRRSRLVIHDPDK--GKITLSLQDAGKHFTGVALELMPSSDFTVRDERKkihlRQLTGKTPGLLAAMS 168
Cdd:TIGR01193 81 NgklpHYYVVYGVTKNHLIIADPDPtvGITKISKEDFYEEWTGIAIFISPTPEYKPIKEKE----NSLLKFIPLITRQKK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 169 RIITFALSLEILTL----GSPLLnQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARV 244
Cdd:TIGR01193 157 LIVNIVIAAIIVTLisiaGSYYL-QKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 245 FHHLVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLW 324
Cdd:TIGR01193 236 IKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 325 YPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGV-------TTHREAAWLNLNVtrRNTQLRQSRLLMyydiaHTLT 397
Cdd:TIGR01193 316 KRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSeaeryskIDSEFGDYLNKSF--KYQKADQGQQAI-----KAVT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 398 GSVVSAIILWKGAGEVLNGTFTVGMLVAY---LSYQMRFSSSISSLTDKFFAWRmldVYNERLADIVLTPTEgnqqqtaq 474
Cdd:TIGR01193 389 KLILNVVILWTGAYLVMRGKLTLGQLITFnalLSYFLTPLENIINLQPKLQAAR---VANNRLNEVYLVDSE-------- 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 475 ENNSTSTTPsifqervTEDTDLPLTLTHIAFSHkGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEG 554
Cdd:TIGR01193 458 FINKKKRTE-------LNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSG 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 555 TIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFS-EDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETG 633
Cdd:TIGR01193 530 EILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEG 609
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 634 GGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK-VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAHRLSVAKQSDKIIVLDHG 684
|
|
| Peptidase_C39C |
cd02419 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
12-138 |
5.56e-61 |
|
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: 200.56 E-value: 5.56e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 12 LPLIRQTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCILH 91
Cdd:cd02419 1 LPVILQTEAAECGLACLAMIASYHGHHVDLASLRQRFPVSLKGATLADLIDIAQQLGLSTRALRLDLEELGQLKLPCILH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 749181994 92 WNMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALELMP 138
Cdd:cd02419 81 WDMNHFVVLKKVSRRRIVIHDPALGKRKLSLEEASRHFTGVALELWP 127
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
498-707 |
2.47e-56 |
|
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: 189.52 E-value: 2.47e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIifFSEdrnhermiqcarlalidsdimtmpmGyqtligetggglsggQKQRILLARALYKKPGFL 657
Cdd:cd03228 81 VPQDPFLFSGTIRENI--LSG-------------------------G---------------QRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALakGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
498-707 |
6.38e-56 |
|
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: 188.58 E-value: 6.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIifFSedrnhermiqcarlalidsdimtmpmgyqtligetggglsGGQKQRILLARALYKKPGFL 657
Cdd:cd03246 81 LPQDDELFSGSIAENI--LS----------------------------------------GGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLKVP---VLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETLASADRILVLEDG 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
242-707 |
1.10e-55 |
|
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: 199.99 E-value: 1.10e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 242 ARVFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVM 320
Cdd:COG4987 92 VRLYRRLEPLAPAGLARLRSGDLLNRLVAdVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 321 RTLW-YPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGS 399
Cdd:COG4987 172 LPLLaARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAG 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 400 VVSAIILWKGAGEVLNGTFTVGMLVAYLsyqmrFSS-----SISSLTDKFFAWRMLDVYNERLADIVltptegNQQQTAQ 474
Cdd:COG4987 252 LAVVAVLWLAAPLVAAGALSGPLLALLV-----LAAlalfeALAPLPAAAQHLGRVRAAARRLNELL------DAPPAVT 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 475 ENNSTSTTPsifqervtedTDLPLTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEG 554
Cdd:COG4987 321 EPAEPAPAP----------GGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 555 TIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGG 634
Cdd:COG4987 391 SITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 635 GLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP--VLLIAHRPETIASADRVLYLTDG 707
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLERMDRILVLEDG 545
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
487-707 |
4.97e-55 |
|
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: 198.06 E-value: 4.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 487 QERVTEDTDLPLTLTHIAFSHkGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHP 566
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 567 DYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILL 646
Cdd:COG4988 405 DPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 647 ARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK--VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:COG4988 485 ARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAkgRTVILITHRLALLAQADRILVLDDG 547
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
242-707 |
1.00e-54 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 200.33 E-value: 1.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 242 ARVFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVL-------A 313
Cdd:TIGR00958 238 EDLFRSLLRQDLGFFDENKTGELTSRLSSdTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLInlplvflA 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 314 AVIYGVmrtlWYPSLrqsAEDAWDAGARESGYFLETLSGILSLRI-----NGVTTHREAawlnLNVTRrntQLRQSRLLM 388
Cdd:TIGR00958 318 EKVFGK----RYQLL---SEELQEAVAKANQVAEEALSGMRTVRSfaaeeGEASRFKEA----LEETL---QLNKRKALA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 389 Y--YDIAHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLtdkffawrmLDVYNERL-----ADIV 461
Cdd:TIGR00958 384 YagYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVL---------SYVYSGMMqavgaSEKV 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 462 LTPTEgnqqQTAQENNSTSTTPSIFQERVTedtdlpltLTHIAFSHKG-SNKPILRGVSLTLHTGEVVAITGKSGCGKST 540
Cdd:TIGR00958 455 FEYLD----RKPNIPLTGTLAPLNLEGLIE--------FQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKST 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 541 LVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMT 620
Cdd:TIGR00958 523 VAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIME 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 621 MPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHRPETIASADR 700
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTVERADQ 682
|
....*..
gi 749181994 701 VLYLTDG 707
Cdd:TIGR00958 683 ILVLKKG 689
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
498-707 |
4.60e-52 |
|
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: 180.50 E-value: 4.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFL 657
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKnrTTFVIAHRLSTIENADRIVVLEDG 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
513-708 |
2.63e-51 |
|
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: 178.50 E-value: 2.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI-------RTFGIPHthpdyyqIRRRIGTVLQEDHLF 585
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdiRDLNLRW-------LRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSH 665
Cdd:cd03249 90 DGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 666 LDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDGY 708
Cdd:cd03249 170 LDAESEKLVQEALDRAMKgrTTIVIAHRLSTIRNADLIAVLQNGQ 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
503-707 |
3.36e-50 |
|
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: 175.11 E-value: 3.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 503 IAFSHKGsNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQED 582
Cdd:cd03254 8 VNFSYDE-KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 583 HLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:cd03254 87 FLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 663 TSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMKgrTSIIIAHRLSTIKNADKILVLDDG 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
232-707 |
6.60e-50 |
|
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: 183.80 E-value: 6.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 232 LSVNFNMQWTARVFHHLVRLPLAwfdaRSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAV 311
Cdd:COG4618 87 VGARLDRRLGPRVFDAAFRAALR----GGGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLGLLAL 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 312 LAAVIYGVMrTLWYPSL-RQSAEDAWDAGARESGYFLETLSG---ILSLRINGVTTHReaaWLNLNVTRRNTQLRQSrll 387
Cdd:COG4618 163 VGALVLVAL-ALLNERLtRKPLKEANEAAIRANAFAEAALRNaevIEAMGMLPALRRR---WQRANARALALQARAS--- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 388 myyDIAHTLTGS------VVSAIILWKGAGEVLNGTFTVGMLVAylsyqmrfSSSISSLT----DKFFA-WRML----DV 452
Cdd:COG4618 236 ---DRAGGFSALskflrlLLQSAVLGLGAYLVIQGEITPGAMIA--------ASILMGRAlapiEQAIGgWKQFvsarQA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 453 YnERLADIVltptegnqQQTAQENNSTSttpsifqervtedtdLP-----LTLTHIAFSHKGSNKPILRGVSLTLHTGEV 527
Cdd:COG4618 305 Y-RRLNELL--------AAVPAEPERMP---------------LPrpkgrLSVENLTVVPPGSKRPILRGVSFSLEPGEV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 528 VAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDrNHERMIQ 607
Cdd:COG4618 361 LGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIARFGDA-DPEKVVA 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 608 CARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VP 684
Cdd:COG4618 440 AAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKargAT 519
|
490 500
....*....|....*....|...
gi 749181994 685 VLLIAHRPETIASADRVLYLTDG 707
Cdd:COG4618 520 VVVITHRPSLLAAVDKLLVLRDG 542
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
180-715 |
3.19e-49 |
|
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: 182.21 E-value: 3.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 180 LTLGSPLLNQLVIDEVLVAADRSLLTVVIvALLLLSLTQMLLSLACQWASIT-LSVNFNMQWTARVFHHLVRLPLAWFDA 258
Cdd:TIGR02204 33 ATLSLPYAVRLMIDHGFSKDSSGLLNRYF-AFLLVVALVLALGTAARFYLVTwLGERVVADIRRAVFAHLISLSPSFFDK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 259 RSRGSVNARFDAIDT-IQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLRQSAEDAWD 337
Cdd:TIGR02204 112 NRSGEVVSRLTTDTTlLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 338 AGARESGYFLETLSGILSLRINGVTTHrEAAWLNLNVTRRNTQLRQS---RLLMYYDIAHTLTGSVVsaIILWKGAGEVL 414
Cdd:TIGR02204 192 RIADAGSYAGETLGAIRTVQAFGHEDA-ERSRFGGAVEKAYEAARQRirtRALLTAIVIVLVFGAIV--GVLWVGAHDVI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 415 NGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERLADIVltptegNQQQTAQENNSTSTTPSIFQERVTEDT 494
Cdd:TIGR02204 269 AGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELL------QAEPDIKAPAHPKTLPVPLRGEIEFEQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 495 dlpltlTHIAFSHKgSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRR 574
Cdd:TIGR02204 343 ------VNFAYPAR-PDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 575 IGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKP 654
Cdd:TIGR02204 416 MALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDA 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDGYFTDL-THQ 715
Cdd:TIGR02204 496 PILLLDEATSALDAESEQLVQQALETLMKgrTTLIIAHRLATVLKADRIVVMDQGRIVAQgTHA 559
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
170-457 |
2.84e-48 |
|
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: 171.92 E-value: 2.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLV 249
Cdd:cd18555 7 ILLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 250 RLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLR 329
Cdd:cd18555 87 KLPYSFFENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 330 QSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILWKG 409
Cdd:cd18555 167 KLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 749181994 410 AGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERL 457
Cdd:cd18555 247 AYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
502-708 |
2.98e-48 |
|
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: 170.10 E-value: 2.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 502 HIAFSHKGsNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQE 581
Cdd:cd03253 5 NVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDE 661
Cdd:cd03253 84 TVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 662 ATSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDGY 708
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKgrTTIVIAHRLSTIVNADKIIVLKDGR 212
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
173-707 |
6.41e-48 |
|
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: 177.93 E-value: 6.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 173 FALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLVRLP 252
Cdd:TIGR01842 14 FSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSAT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 253 LAwfdaRSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLRQSA 332
Cdd:TIGR01842 94 LR----RGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 333 EDAWDAGAReSGYFLE-TLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQS-RLLMYYDIAHTLTGSVVSAIILWkGA 410
Cdd:TIGR01842 170 KEATEASIR-ANNLADsALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASdRAGMLSNLSKYFRIVLQSLVLGL-GA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 411 GEVLNGTFTVGMLVAylsyqmrfsSSIssltdkffawrmldvynerLADIVLTPTEGNQQQTAQENNSTSTTPSI---FQ 487
Cdd:TIGR01842 248 YLAIDGEITPGMMIA---------GSI-------------------LVGRALAPIDGAIGGWKQFSGARQAYKRLnelLA 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 488 ERVTEDTDLPL-------TLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG 560
Cdd:TIGR01842 300 NYPSRDPAMPLpepeghlSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 561 IPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQ 640
Cdd:TIGR01842 380 ADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQ 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCVDKILVLQDG 529
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
162-707 |
1.92e-47 |
|
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: 176.83 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 162 GLLAAMSRIITFALSLEIL-TLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSlACQWASITLSVNFNMqw 240
Cdd:TIGR02203 15 GLVLAGVAMILVAATESTLaALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTY-LLSWVSNKVVRDIRV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 241 taRVFHHLVRLPLAWFDARSRGSVNARFdaidTIQQALTTQVLEGILDVL----LVVTALCMMLLY-SPEMTLIAVLAAV 315
Cdd:TIGR02203 92 --RMFEKLLGLPVSFFDRQPTGTLLSRI----TFDSEQVASAATDAFIVLvretLTVIGLFIVLLYySWQLTLIVVVMLP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 316 IYGVMRTLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRING---VTTHREAAwlnlnVTRRNT--QLRQSRLLMYY 390
Cdd:TIGR02203 166 VLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGgqaYETRRFDA-----VSNRNRrlAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 391 DIAHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERLADIVLTPTEGNqq 470
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD-- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 471 qtaqennsTSTTPsifQERVTEDtdlpLTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHL 550
Cdd:TIGR02203 319 --------TGTRA---IERARGD----VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 551 PNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFS-EDRNHERMIQCARLALIDSDIMTMPMGYQTLI 629
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 630 GETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLmqGRTTLVIAHRLSTIEKADRIVVMDDG 543
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
498-707 |
9.08e-47 |
|
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: 166.12 E-value: 9.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFL 657
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAgrTVIIIAHRLSTVKNADRIIVMEKG 212
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
498-707 |
1.47e-45 |
|
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: 161.99 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFL 657
Cdd:cd03245 83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLKVP--VLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
487-704 |
1.13e-41 |
|
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: 159.76 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 487 QERVTEDTDLPLTLTHIAFSHKGSNkPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHP 566
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 567 DYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILL 646
Cdd:TIGR02857 390 DADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 647 ARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK--VPVLLIAHRPETIASADRVLYL 704
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAqgRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
510-707 |
5.85e-41 |
|
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: 149.54 E-value: 5.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSI 589
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVE 669
Cdd:cd03248 105 QDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 749181994 670 SEIQISQTLRQ--LKVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03248 185 SEQQVQQALYDwpERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
242-692 |
6.07e-38 |
|
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: 148.66 E-value: 6.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 242 ARVFHHLVRLPLAWFDARSRGSVNARF-DAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVM 320
Cdd:TIGR02868 90 VRVYERLARQALAGRRRLRRGDLLGRLgADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 321 RTLWYPSLRQSAEDAWDAGARE-SGYFLETLSGILSLRINGVTTHREAAwlnlnVTRRNTQL-----RQSRLLMYYDIAH 394
Cdd:TIGR02868 170 APLVSLRAARAAEQALARLRGElAAQLTDALDGAAELVASGALPAALAQ-----VEEADRELtraerRAAAATALGAALT 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 395 TLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERLADivLTPTEGNQQQTAQ 474
Cdd:TIGR02868 245 LLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVE--VLDAAGPVAEGSA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 475 ENNSTSttpsifqervtEDTDLPLTLTHIAFSHKGSNkPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEG 554
Cdd:TIGR02868 323 PAAGAV-----------GLGKPTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 555 TIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGG 634
Cdd:TIGR02868 391 EVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGA 470
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 635 GLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRP 692
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAlsGRTVVLITHHL 530
|
|
| Peptidase_C39 |
pfam03412 |
Peptidase C39 family; Lantibiotic and non-lantibiotic bacteriocins are synthesized as ... |
11-141 |
1.82e-37 |
|
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: 136.20 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 11 RLPLIRQTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCIL 90
Cdd:pfam03412 1 KYKIVLQVDENDCGLACLAMILKYYGSNVSLEELRELAGTPAEGTSLLGLKKAAEKLGFKAKAIKADLSELKELPLPFIA 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 91 HWNMN--HFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALELMPSSD 141
Cdd:pfam03412 81 HWDGNggHFVVVYGIKKNKVLIADPAVGKIKLSREEFEKEWTGVALLVAPKPS 133
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
500-707 |
2.90e-37 |
|
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: 138.37 E-value: 2.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 500 LTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVL 579
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 580 Q--EDHLFRGSIADNIIF------FSEDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRILLA 647
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFglenlgLPEEEIEERVEEALELvgleGLRDRSPFTLSGG---------------QKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 648 RALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
512-707 |
6.97e-37 |
|
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: 137.62 E-value: 6.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIAD 591
Cdd:cd03244 17 PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIFFSEdRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESE 671
Cdd:cd03244 97 NLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 749181994 672 IQISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03244 176 ALIQKTIREAfkDCTVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
169-441 |
1.39e-36 |
|
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: 139.23 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 169 RIITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHL 248
Cdd:cd18568 6 EILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 249 VRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSL 328
Cdd:cd18568 86 LSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 329 RQSAEDAWDAGARESGYFLETLSGILSlrINGVTTHREAAWLNLNVTRR--NTQLRQSRLLMYYDIAHTLTGSVVSAIIL 406
Cdd:cd18568 166 KRNSREIFQANAEQQSFLVEALTGIAT--IKALAAERPIRWRWENKFAKalNTRFRGQKLSIVLQLISSLINHLGTIAVL 243
|
250 260 270
....*....|....*....|....*....|....*
gi 749181994 407 WKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18568 244 WYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALV 278
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
403-707 |
1.24e-35 |
|
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: 143.04 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 403 AIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTdkfFAWR-----MLDVynERLADIVLTPTEGNQQQTAQenn 477
Cdd:COG5265 278 TAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLG---FVYReirqaLADM--ERMFDLLDQPPEVADAPDAP--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 478 ststtpsifqervtedtDLPLTLTHIAFSH----KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNE 553
Cdd:COG5265 350 -----------------PLVVGGGEVRFENvsfgYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 554 GTIRTFG--IPHTHPDYyqIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGE 631
Cdd:COG5265 413 GRILIDGqdIRDVTQAS--LRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 632 TGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDG 707
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARgrTTLVIAHRLSTIVDADEILVLEAG 568
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
498-707 |
1.28e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.79 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIafSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:COG4619 1 LELEGL--SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIIF---FSEDR-NHERMIQ-CARLALiDSDIMTMPM-----GyqtligetggglsggQKQRILLA 647
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFpfqLRERKfDRERALElLERLGL-PPDILDKPVerlsgG---------------ERQRLALI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 648 RALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG4619 143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
161-457 |
1.39e-35 |
|
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: 136.52 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 161 PGLLAamsRIITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQW 240
Cdd:cd18779 1 PGLLG---QILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 241 TARVFHHLVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVM 320
Cdd:cd18779 78 TLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 321 RTLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSV 400
Cdd:cd18779 158 LLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 401 VSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERL 457
Cdd:cd18779 238 APLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLLGSHLERL 294
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
162-708 |
1.92e-35 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 142.08 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 162 GLLAAMSRIITFALS-LEILTLGSPLLnqlviDEVLVAADRSLLT---VVIVALLLLSLTQMLLSLAC-QWasitLSVNF 236
Cdd:PRK11176 26 GLIVAGVALILNAASdTFMLSLLKPLL-----DDGFGKADRSVLKwmpLVVIGLMILRGITSFISSYCiSW----VSGKV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 237 NMQWTARVFHHLVRLPLAWFDARSRGSVNARFdAIDTIQ------QALTTQVLEGILdvllVVTALCMMLLYSPEMTLIA 310
Cdd:PRK11176 97 VMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRI-TYDSEQvassssGALITVVREGAS----IIGLFIMMFYYSWQLSLIL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 311 VLAAVIYGVMRTLWYPSLRQSAEDAWDAGARESGYFLETLSG---ILSLRINGVTTHREAAWLNlnvtrrntQLRQSRLL 387
Cdd:PRK11176 172 IVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGhkeVLIFGGQEVETKRFDKVSN--------RMRQQGMK 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 388 MY-----YDIAHTLTGSVVSAIILWKG-----AGEVLNGTFTV---GMLVAylsyqMRFSSSISSLTDKF---------- 444
Cdd:PRK11176 244 MVsassiSDPIIQLIASLALAFVLYAAsfpsvMDTLTAGTITVvfsSMIAL-----MRPLKSLTNVNAQFqrgmaacqtl 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 445 FAwrMLDVYNERladivltptegnqqqtaqeNNSTSTTpsifqERVTEDtdlpLTLTHIAFSHKGSNKPILRGVSLTLHT 524
Cdd:PRK11176 319 FA--ILDLEQEK-------------------DEGKRVI-----ERAKGD----IEFRNVTFTYPGKEVPALRNINFKIPA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 525 GEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGipHTHPDYY--QIRRRIGTVLQEDHLFRGSIADNIIFFSEDR-N 601
Cdd:PRK11176 369 GKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDLRDYTlaSLRNQVALVSQNVHLFNDTIANNIAYARTEQyS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 602 HERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL 681
Cdd:PRK11176 447 REQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL 526
|
570 580
....*....|....*....|....*....
gi 749181994 682 KV--PVLLIAHRPETIASADRVLYLTDGY 708
Cdd:PRK11176 527 QKnrTSLVIAHRLSTIEKADEILVVEDGE 555
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
498-707 |
5.30e-35 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 132.84 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQ--EDHLFRGSIADNIIF------FSEDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRIL 645
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAFgpenlgLPREEIRERVEEALELvgleHLADRPPHELSGG---------------QKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 646 LARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAElADRVIVLDDG 210
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
166-438 |
7.74e-35 |
|
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: 134.16 E-value: 7.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 166 AMSRIITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVF 245
Cdd:cd18588 3 LLGEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 246 HHLVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWY 325
Cdd:cd18588 83 RHLLRLPLSYFESRQVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 326 PSLRQSAEDAWDAGARESGYFLETLSGI---LSLRINGVTTHReaaWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVS 402
Cdd:cd18588 163 PILRRRLEEKFQRGAENQSFLVETVTGIetvKSLAVEPQFQRR---WEELLARYVKASFKTANLSNLASQIVQLIQKLTT 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 749181994 403 AIILWKGAGEVLNGTFTVGMLVAylsYQMrFSSSIS 438
Cdd:cd18588 240 LAILWFGAYLVMDGELTIGQLIA---FNM-LAGQVS 271
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
498-707 |
1.18e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 133.22 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQE-DHLFRGS-IADNIIFFSEDRN--HERMIQCARLALidsdimtMPMGYQTLIGETGGGLSGGQKQRILLARALYKK 653
Cdd:PRK13635 86 VFQNpDNQFVGAtVQDDVAFGLENIGvpREEMVERVDQAL-------RQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 654 PGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKeqkgITVLSITHDLDEAAQADRVIVMNKG 216
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
170-442 |
1.19e-33 |
|
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: 130.75 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSL--EILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHH 247
Cdd:cd07346 2 LLALLLLLlaTALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 248 LVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYP 326
Cdd:cd07346 82 LQRLSLSFFDRNRTGDLMSRLTSdVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 327 SLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIIL 406
Cdd:cd07346 162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 749181994 407 WKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTD 442
Cdd:cd07346 242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLAN 277
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
502-707 |
1.53e-33 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 136.24 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 502 HIAFSHKGSnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQE 581
Cdd:PRK13657 339 DVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDE 661
Cdd:PRK13657 418 AGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 749181994 662 ATSHLDVESEIQISQTLRQLKV--PVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKgrTTFIIAHRLSTVRNADRILVFDNG 545
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
170-440 |
5.03e-33 |
|
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: 129.10 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLV 249
Cdd:cd18570 7 ILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 250 RLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLR 329
Cdd:cd18570 87 KLPLSFFETRKTGEIISRFNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 330 QSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILWKG 409
Cdd:cd18570 167 KKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIG 246
|
250 260 270
....*....|....*....|....*....|.
gi 749181994 410 AGEVLNGTFTVGMLVAYLSYQMRFSSSISSL 440
Cdd:cd18570 247 SYLVIKGQLSLGQLIAFNALLGYFLGPIENL 277
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
515-664 |
1.27e-32 |
|
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: 123.14 E-value: 1.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRG-SIADNI 593
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 594 IFFSEDRNHERMIQCARLALIDSdimTMPMGYQ--TLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATS 664
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALE---KLGLGDLadRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
499-707 |
2.59e-32 |
|
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: 122.74 E-value: 2.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 499 TLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTV 578
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 579 LQedhLFRGsiadniiffsedrnhermiqcarlalidsdimtmpmgyqtligetggglsggQKQRILLARALYKKPGFLL 658
Cdd:cd00267 79 PQ---LSGG----------------------------------------------------QRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 659 LDEATSHLDVESEIQISQTLRQL---KVPVLLIAHRPETIA-SADRVLYLTDG 707
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAElAADRVIVLKDG 156
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
502-707 |
1.30e-31 |
|
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: 123.00 E-value: 1.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 502 HIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ---IRRRIGTV 578
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkiRRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 579 LQE-----DHLFR--GSIADNIIFFSEDRNHERMIQCARLALI----DSDIMTM-PM----GyqtligetggglsggQKQ 642
Cdd:cd03257 88 FQDpmsslNPRMTigEQIAEPLRIHGKLSKKEARKEAVLLLLVgvglPEEVLNRyPHelsgG---------------QRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 643 RILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeelgLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| Peptidase_C39B |
cd02418 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
13-141 |
2.73e-31 |
|
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: 118.85 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 13 PLIRQTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPE--DLKSLSLPCIL 90
Cdd:cd02418 2 PYVLQVDEMDCGAACLAMIAKYYGKNYSLAKLRELAGTDREGTSLLGLVKAAEKLGFETRAVKADMDlfELKDIPLPFIA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 91 H----WNMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALELMPSSD 141
Cdd:cd02418 82 HvikeWKLNHYVVVYKIKKKKILIADPAVGITKISKEEFEKEWTGVALFLEPTPN 136
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
170-426 |
4.92e-31 |
|
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: 123.47 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALS--LEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHH 247
Cdd:cd18782 5 IEVLALSfvVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 248 LVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPS 327
Cdd:cd18782 85 LLRLPLGFFDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 328 LRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILW 407
Cdd:cd18782 165 LRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLW 244
|
250
....*....|....*....
gi 749181994 408 KGAGEVLNGTFTVGMLVAY 426
Cdd:cd18782 245 VGAYLVLRGELTLGQLIAF 263
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
502-707 |
1.38e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 121.38 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 502 HIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDY-YQIRRRIGTVLQ 580
Cdd:TIGR04520 5 NVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlWEIRKKVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 581 E-DHLFRGSI-ADNIIFFSEDRN--HERMIQCARLALIDsdimtmpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGF 656
Cdd:TIGR04520 85 NpDNQFVGATvEDDVAFGLENLGvpREEMRKRVDEALKL-------VGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 657 LLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNkeegITVISITHDMEEAVLADRVIVMNKG 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
511-707 |
5.91e-30 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 116.34 E-value: 5.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPhTHPDYYQIRRRIGTVLQEDHLFRG-SI 589
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-IKKEPEEVKRRIGYLPEEPSLYENlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFfsedrnhermiqcarlalidsdimtmPMGyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVE 669
Cdd:cd03230 91 RENLKL--------------------------SGG---------------MKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 749181994 670 SEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03230 130 SRREFWELLRELKkegKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
498-707 |
1.41e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHkgSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPdyyqiRRRIGT 577
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQedhlfRGSIADNI-----------------IFFSEDRNHERMIQCA--RL---ALIDSDIMTMPMGyqtligetggg 635
Cdd:COG1121 80 VPQ-----RAEVDWDFpitvrdvvlmgrygrrgLFRRPSRADREAVDEAleRVgleDLADRPIGELSGG----------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 636 lsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG1121 144 ----QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRregKTILVVTHDLGAVREyFDRVLLLNRG 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
487-707 |
1.76e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 124.19 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 487 QERVTEDTDLPLTLTH---IAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIhLPNEGTIRTFGIPH 563
Cdd:PRK11174 337 QGEKELASNDPVTIEAedlEILSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIEL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 564 THPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQR 643
Cdd:PRK11174 414 RELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 644 ILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK11174 494 LALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
499-707 |
4.96e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 114.07 E-value: 4.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 499 TLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTV 578
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 579 LQedhlfrgsiadniiffsedrnherMIQCARLA-LIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGFL 657
Cdd:cd03214 79 PQ------------------------ALELLGLAhLADRPFNELSGG---------------ERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLArergKTVVMVLHDLNLAARyADRVILLKDG 174
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
504-707 |
7.65e-29 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 121.74 E-value: 7.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 504 AFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDH 583
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 LFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 664 SHLDVESEIQISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWgeGRTVIISAHRLSALTEASEILVMQHG 525
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
510-704 |
8.99e-29 |
|
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: 114.17 E-value: 8.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHThpdyyQIRRRIGTVLQE---DHLFR 586
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVPQRrsiDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 GSIADNI---------IFFSEDRNHERMIQCA-----RLALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYK 652
Cdd:cd03235 85 ISVRDVVlmglyghkgLFRRLSKADKAKVDEAlervgLSELADRQIGELSGG---------------QQQRVLLARALVQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 653 KPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETI-ASADRVLYL 704
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRregMTILVVTHDLGLVlEYFDRVLLL 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
511-707 |
4.48e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.85 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHpDYYQIRRRIGTVLQEDHLFRG-SI 589
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYPDlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFF------SEDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLL 659
Cdd:COG1131 91 RENLRFFarlyglPRKEARERIDELLELfgltDAADRKVGTLSGG---------------MKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 660 DEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAaegKTVLLSTHYLEEAERlCDRVAIIDKG 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
498-707 |
6.45e-28 |
|
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: 118.47 E-value: 6.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPN---EGTIRTFGIPHTHPDYYQIRRR 574
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 575 IGTVLQE--DHLFRGSIADNIIFFSEDRN--HERMIQCARLALIDsdimtmpMGYQTLIGETGGGLSGGQKQRILLARAL 650
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEALENLGlsRAEARARVLELLEA-------VGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQrergTTVLLITHDLGVVAEiADRVVVMDDG 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
498-707 |
6.70e-28 |
|
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: 111.81 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFS-HKGSNK-PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI---- 571
Cdd:cd03255 1 IELKNLSKTyGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 572 RRRIGTVLQEDHLFRG-SIADNII---FFSEDRNHERMIQCARL-------ALIDSDIMTMPMGyqtligetggglsggQ 640
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVElplLLAGVPKKERRERAEELlervglgDRLNHYPSELSGG---------------Q 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNkeagTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
498-705 |
1.23e-27 |
|
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: 111.41 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHI--AFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPdyyqiRRRI 575
Cdd:cd03293 1 LEVRNVskTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLF--RgSIADNIIFFSEDRNHERMIQCAR-LALID---------------SDIMtmpmgyqtligetgggls 637
Cdd:cd03293 76 GYVFQQDALLpwL-TVLDNVALGLELQGVPKAEARERaEELLElvglsgfenayphqlSGGM------------------ 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 638 ggqKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHR-PETIASADRVLYLT 705
Cdd:cd03293 137 ---RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHDiDEAVFLADRVVVLS 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
498-707 |
1.47e-27 |
|
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: 111.87 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKgsNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYyQIRRRIGT 577
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLF-RGSIADNIIFFSE------DRNHER---MIQCARL-ALIDSDIMTMPMGyqtligetggglsggQKQRILL 646
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYFAElyglfdEELKKRieeLIELLGLeEFLDRRVGELSTG---------------MKKKVAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 647 ARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP---VLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEgktVLFSSHIMQEVEAlCDRVVILHKG 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
498-707 |
1.93e-27 |
|
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: 109.20 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYY--QIRRRI 575
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLFRG-SIADNIIFfsedrnhermiqcarlALidsdimtmpmgyqtligetggglSGGQKQRILLARALYKKP 654
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIAL----------------GL-----------------------SGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRP-ETIASADRVLYLTDG 707
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQaqlgITVVLVTHDLdEAARLADRVVVLRDG 177
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
513-707 |
3.43e-27 |
|
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: 108.28 E-value: 3.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ-IRRRIGTVLQedhlfrgsiad 591
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ----------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 niiffsedrnhermiqcarlalidsdimtMPMGyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESE 671
Cdd:cd03216 83 -----------------------------LSVG---------------ERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 749181994 672 IQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03216 119 ERLFKVIRRLRaqgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
502-707 |
4.15e-27 |
|
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: 110.66 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 502 HIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQe 581
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQ- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 D--------HLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIMTMPM-----GyqtligetggglsggQKQRILLAR 648
Cdd:COG1124 87 DpyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPhqlsgG---------------QRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 649 ALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP----VLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErgltYLFVSHDLAVVAHlCDRVAVMQNG 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
498-707 |
5.12e-27 |
|
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: 110.52 E-value: 5.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHL-FRGSIADNII--------FFS----EDRNH-ERMIQCARLA-LIDSDIMTMPMGyqtligetggglsggQKQ 642
Cdd:COG1120 80 VPQEPPApFGLTVRELVAlgryphlgLFGrpsaEDREAvEEALERTGLEhLADRPVDELSGG---------------ERQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 643 RILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP----VLLIAHRPeTIAS--ADRVLYLTDG 707
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgrtVVMVLHDL-NLAAryADRLVLLKDG 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
499-707 |
5.28e-27 |
|
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: 108.88 E-value: 5.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 499 TLTHIAFSHKGSNKpILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtFGIPHTHpdYYQIRRRIGTV 578
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL-LNGKPIK--AKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 579 LQE--DHLFRGSIADNIIFFSEDRNHERMIQCARLALIDSDIM------TMPMGyqtligetggglsggQKQRILLARAL 650
Cdd:cd03226 77 MQDvdYQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALkerhplSLSGG---------------QKQRLAIAAAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLRQL---KVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03226 142 LSGKDLLIFDEPTSGLDYKNMERVGELIRELaaqGKAVIVITHDYEFLAKvCDRVLLLANG 202
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
170-437 |
7.92e-27 |
|
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: 110.43 E-value: 7.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSLEILTLGSPLLNQLVIDEVLVAADRS--LLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHH 247
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 248 LVRLPLAWFDARSRGSVNARF-DAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYP 326
Cdd:pfam00664 84 ILRQPMSFFDTNSVGELLSRLtNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 327 SLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIIL 406
Cdd:pfam00664 164 ILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALAL 243
|
250 260 270
....*....|....*....|....*....|.
gi 749181994 407 WKGAGEVLNGTFTVGMLVAYLSYQMRFSSSI 437
Cdd:pfam00664 244 WFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
514-707 |
8.07e-27 |
|
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: 109.19 E-value: 8.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLI-----LGIHLPNEGTIRTFG--IPHTHPDYYQIRRRIGTVLQEDHLFR 586
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGkdIYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 GSIADNIIF-------FSEDRNHERMIQCARLALIDSDIMTMPMGYQtligetgggLSGGQKQRILLARALYKKPGFLLL 659
Cdd:cd03260 95 GSIYDNVAYglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 660 DEATSHLDVESEIQISQTLRQLK--VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKkeYTIVIVTHNMQQAARvADRTAFLLNG 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
506-707 |
1.14e-26 |
|
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: 107.94 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 506 SHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrtfgiphthpdyyQIRRRIGTVLQEDHLF 585
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV-------------SVPGSIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RGSIADNIIFFSEdRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSH 665
Cdd:cd03250 79 NGTIRENILFGKP-FDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 666 LDVESEIQISQ-----TLRQLKVpVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03250 158 VDAHVGRHIFEncilgLLLNNKT-RILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
513-707 |
1.44e-26 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 107.88 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADN 592
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 IIFFSEdrnhermiqcarlaLIDSDIMTMpmgyqTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEI 672
Cdd:cd03369 102 LDPFDE--------------YSDEEIYGA-----LRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 749181994 673 QISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03369 163 LIQKTIREEftNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
498-707 |
2.07e-26 |
|
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: 107.61 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIafSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYqiRRRIGT 577
Cdd:cd03259 1 LELKGL--SKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLF-RGSIADNIIF------FSEDRNHERMIQCARLALIDSDIMTMPM----GyqtligetggglsggQKQRILL 646
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFglklrgVPKAEIRARVRELLELVGLEGLLNRYPHelsgG---------------QQQRVAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 647 ARALYKKPGFLLLDEATSHLDVESEIQ----ISQTLRQLKVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREElreeLKELQRELGITTIYVTHdQEEALALADRIAVMNEG 207
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
498-710 |
6.25e-26 |
|
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: 105.09 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrTFGIPHTHPDYYQIRRRIGT 577
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-TLDGVPVSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNI-IFFSedrnhermiqcarlalidsdimtmpmgyqtligetggglsGGQKQRILLARALYKKPGF 656
Cdd:cd03247 80 LNQRPYLFDTTLRNNLgRRFS----------------------------------------GGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 657 LLLDEATSHLDVESEIQI-SQTLRQLK-VPVLLIAHRPETIASADRVLYLTDGYFT 710
Cdd:cd03247 120 VLLDEPTVGLDPITERQLlSLIFEVLKdKTLIWITHHLTGIEHMDKILFLENGKII 175
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
498-707 |
7.10e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 106.28 E-value: 7.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHK-GSNK-PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI---- 571
Cdd:COG1136 5 LELRNLTKSYGtGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 572 RRRIGTVLQEDHLFRG-SIADNIIF------FSEDRNHERMIQ-CARLALidSDIMT-MPM----Gyqtligetggglsg 638
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllagVSRKERRERARElLERVGL--GDRLDhRPSqlsgG-------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 639 gQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:COG1136 149 -QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrelGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
511-707 |
1.15e-25 |
|
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: 106.22 E-value: 1.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPD---YYQIRRRIGTVLQEDHLFRG 587
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 -SIADNIIF-------FSEDRNHERMIQCARLALIDSDIMTMP------MgyqtligetggglsggQKqRILLARALYKK 653
Cdd:COG1127 97 lTVFENVAFplrehtdLSEAEIRELVLEKLELVGLPGAADKMPselsggM----------------RK-RVALARALALD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 654 PGFLLLDEATSHLDVESEIQISQTLR----QLKVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRelrdELGLTSVVVTHDlDSAFAIADRVAVLADG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
498-707 |
1.76e-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: 111.15 E-value: 1.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNK---PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP---HTHPDYYQI 571
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 572 RRRIGTVLQ--EDHLF-RGSIADNIIF-------FSEDRNHERMIQCARL-----ALIDSDIMTMPMGyqtligetgggl 636
Cdd:COG1123 341 RRRVQMVFQdpYSSLNpRMTVGDIIAEplrlhglLSRAERRERVAELLERvglppDLADRYPHELSGG------------ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 637 sggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG1123 409 ---QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHDLAVVRYiADRVAVMYDG 481
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
498-707 |
2.40e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.94 E-value: 2.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHI--AFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDyyqirRRI 575
Cdd:COG1116 8 LELRGVskRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLF--RgSIADNIIF------FSEDRNHERmiqcAR--LALID------------SdimtmpMGyqtligetg 633
Cdd:COG1116 83 GVVFQEPALLpwL-TVLDNVALglelrgVPKAERRER----ARelLELVGlagfedayphqlS------GG--------- 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 634 gglsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:COG1116 143 ------MRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqetGKTVLFVTHdVDEAVFLADRVVVLSAR 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
515-707 |
3.15e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.11 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRR-IGTVLQEDHLFRG-SIADN 592
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 IIFFSEDR-----NHERMIQCAR--LALIDSDI------MTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLL 659
Cdd:COG1129 100 IFLGREPRrggliDWRAMRRRARelLARLGLDIdpdtpvGDLSVA---------------QQQLVEIARALSRDARVLIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 660 DEATSHLDvESEIQI-SQTLRQLK---VPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:COG1129 165 DEPTASLT-EREVERlFRIIRRLKaqgVAIIYISHRlDEVFEIADRVTVLRDG 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
511-707 |
3.22e-25 |
|
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: 104.89 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH---PDYYQIRRRIGTVLQEDHLFRG 587
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRRRMGMLFQSGALFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 -SIADNIIF-------FSEDRNHERMIQCARLALIDSDIMTMP------MgyqtligetggglsggqKQRILLARALYKK 653
Cdd:cd03261 92 lTVFENVAFplrehtrLSEEEIREIVLEKLEAVGLRGAEDLYPaelsggM-----------------KKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 654 PGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSLKkelgLTSIMVTHDlDTAFAIADRIAVLYDG 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
498-707 |
6.44e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 105.27 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLP---NEGTIRTFGIPHTHPDYYQIRRR 574
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 575 IGTVLQE-DHLFRG-SIADNIIFFSEDRN--HERMIQCARLALIDsdimtmpMGYQTLIGETGGGLSGGQKQRILLARAL 650
Cdd:PRK13640 86 VGIVFQNpDNQFVGaTVGDDVAFGLENRAvpRPEMIKIVRDVLAD-------VGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKkknnLTVISITHDIDEANMADQVLVLDDG 219
|
|
| Peptidase_C39F |
cd02425 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
12-134 |
2.26e-24 |
|
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: 98.88 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 12 LPLIRQTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLE-PEDLKSLSLPCIL 90
Cdd:cd02425 1 VKPILQNNQTECGLACYAMILNYFGYKVSLNELREKYELGRDGLSLSYLKQLLEEYGFKCKVYKISfKKNLYPLKLPVII 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 749181994 91 HWNMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVAL 134
Cdd:cd02425 81 FWNNNHFVVLEKIKKNKVTIVDPAIGRIKISIDEFLENFSGYIL 124
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
525-707 |
6.41e-24 |
|
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: 100.45 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 525 GEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP--------HTHPDyyqiRRRIGTVLQEDHLF-RGSIADNIIF 595
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkiNLPPQ----QRKIGLVFQQYALFpHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 596 -FSEDRNHERMIQCARlalidsdiMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQI 674
Cdd:cd03297 99 gLKRKRNREDRISVDE--------LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 749181994 675 SQTLRQ----LKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03297 171 LPELKQikknLNIPVIFVTHDLSEAEYlADRIVVMEDG 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
244-707 |
7.98e-24 |
|
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: 107.72 E-value: 7.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 244 VFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTtQVLEGILDVLL-VVTALCMMLLYSPEMTLIAVLAAVIYGVMR 321
Cdd:TIGR00957 1044 LLHNKLRSPMSFFERTPSGNLVNRFSKeLDTVDSMIP-PVIKMFMGSLFnVIGALIVILLATPIAAVIIPPLGLLYFFVQ 1122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 322 TLWYPSLRQSAEdaWDAGARESGY--FLETLSGILSLRingvTTHREAAWLNLNVTRRNTQLRQsrllmYYD--IAHTLT 397
Cdd:TIGR00957 1123 RFYVASSRQLKR--LESVSRSPVYshFNETLLGVSVIR----AFEEQERFIHQSDLKVDENQKA-----YYPsiVANRWL 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 398 G----SVVSAIILWKGAGEVLN-GTFTVGMLVAYLSYQMRFSSSISSLTdkffawRMLD------VYNERLADIVLTPTE 466
Cdd:TIGR00957 1192 AvrleCVGNCIVLFAALFAVISrHSLSAGLVGLSVSYSLQVTFYLNWLV------RMSSemetniVAVERLKEYSETEKE 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 467 GNQQqtAQENNSTSTTPSI-------FQERVTEDTDLpltlthiafshkgsnkpILRGVSLTLHTGEVVAITGKSGCGKS 539
Cdd:TIGR00957 1266 APWQ--IQETAPPSGWPPRgrvefrnYCLRYREDLDL-----------------VLRHINVTIHGGEKVGIVGRTGAGKS 1326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 540 TLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEdRNHERMIQCARLALIDSDIM 619
Cdd:TIGR00957 1327 SLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQ-YSDEEVWWALELAHLKTFVS 1405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 620 TMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLR-QLK-VPVLLIAHRPETIAS 697
Cdd:TIGR00957 1406 ALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFEdCTVLTIAHRLNTIMD 1485
|
490
....*....|
gi 749181994 698 ADRVLYLTDG 707
Cdd:TIGR00957 1486 YTRVIVLDKG 1495
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
505-707 |
1.91e-23 |
|
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: 99.58 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT---HPDYYQIRRRIGTVLQE 581
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLF-RGSIADNIIFFSEDRNHERMIQCAR----LALI------DSDIMTMPMGyqtligetggglsggQKQRILLARAL 650
Cdd:cd03258 91 FNLLsSRTVFENVALPLEIAGVPKAEIEERvlelLELVgledkaDAYPAQLSGG---------------QKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLRQ----LKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDinreLGLTIVLITHEMEVVKRiCDRVAVMEKG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
511-707 |
2.01e-23 |
|
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: 100.16 E-value: 2.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEG-TIRTFGIPHTHPDYYQIRRRIGTV---LQEDHLFR 586
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLVspaLQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 GSIADNII--FFS--------EDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYK 652
Cdd:COG1119 95 ETVLDVVLsgFFDsiglyrepTDEQRERARELLELlglaHLADRPFGTLSQG---------------EQRRVLIARALVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 653 KPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIASA-DRVLYLTDG 707
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTHHVEEIPPGiTHVLLLKDG 219
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
500-707 |
2.88e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.07 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 500 LTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVL 579
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 580 QE-DHLFRGSIA-DNIIFFSEDRN--HERMiqcarLALIDSdiMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPG 655
Cdd:PRK13632 90 QNpDNQFIGATVeDDIAFGLENKKvpPKKM-----KDIIDD--LAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 656 FLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHDMDEAILADKVIVFSEG 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
509-715 |
3.79e-23 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.59 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI---RRRIGTVLQeDH-- 583
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylRRRIGVVFQ-DFrl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 LFRGSIADNIIF------FSEDRNHERmiqcARLAL----IDSDIMTMPM----GyqtligetggglsggQKQRILLARA 649
Cdd:COG2884 91 LPDRTVYENVALplrvtgKSRKEIRRR----VREVLdlvgLSDKAKALPHelsgG---------------EQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 650 LYKKPGFLLLDEATSHLDVES--EI-QISQTLRQLKVPVLLIAHRPETIASAD-RVLYLTDGYFTDLTHQ 715
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETswEImELLEEINRRGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEAR 221
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
498-705 |
8.60e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 97.48 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT--HPDYYqiRRRI 575
Cdd:PRK10247 8 LQLQNVGYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIY--RQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLFRGSIADNIIFFSEDRNhermIQCARLALIDsDIMTMPMGyQTLIGETGGGLSGGQKQRILLARALYKKPG 655
Cdd:PRK10247 84 SYCAQTPTLFGDTVYDNLIFPWQIRN----QQPDPAIFLD-DLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 656 FLLLDEATSHLDVESEIQ----ISQTLRQLKVPVLLIAHRPETIASADRVLYLT 705
Cdd:PRK10247 158 VLLLDEITSALDESNKHNvneiIHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
500-707 |
9.77e-23 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 98.34 E-value: 9.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 500 LTHIAFSH----KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ---IR 572
Cdd:TIGR02769 8 VTHTYRTGglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 573 RRIGTVLQEDH-------LFRGSIAD---NIIFFSEDRNHERMIQCARLALIDSDIMtmpmgyqtliGETGGGLSGGQKQ 642
Cdd:TIGR02769 88 RDVQLVFQDSPsavnprmTVRQIIGEplrHLTSLDESEQKARIAELLDMVGLRSEDA----------DKLPRQLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 643 RILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqafgTAYLFITHDLRLVQSfCQRVAVMDKG 227
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
165-442 |
1.03e-22 |
|
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: 99.09 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 165 AAMSRIITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARV 244
Cdd:cd18569 2 SALLFVVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 245 FHHLVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMrtLW 324
Cdd:cd18569 82 FWHVLRLPVEFFSQRYAGDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLV--LR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 325 YPSLRQsaEDAWDAGARESGYFLET----LSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSV 400
Cdd:cd18569 160 LVSRKR--VDLNRRLLQDSGKLTGTtmsgLQMIETLKASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSAL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 749181994 401 VSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTD 442
Cdd:cd18569 238 TNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVG 279
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
498-704 |
2.91e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPN---EGTIRTFGIPHTH-PDYyqiRR 573
Cdd:COG4136 2 LSLENLTITLGG--RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAlPAE---QR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 574 RIGTVLQEDHLF-RGSIADNIIF-------FSEDRNH-ERMIQCARLA-LIDSDIMTMPMGyqtligetggglsggQKQR 643
Cdd:COG4136 77 RIGILFQDDLLFpHLSVGENLAFalpptigRAQRRARvEQALEEAGLAgFADRDPATLSGG---------------QRAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 644 ILLARALYKKPGFLLLDEATSHLDVESEIQISQ----TLRQLKVPVLLIAHRPETIASADRVLYL 704
Cdd:COG4136 142 VALLRALLAEPRALLLDEPFSKLDAALRAQFREfvfeQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
|
|
| Peptidase_C39D |
cd02420 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
13-136 |
3.03e-22 |
|
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: 92.49 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 13 PLIRQTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCILHW 92
Cdd:cd02420 2 PTVLQMEATECGAASLAIILAYYGRYVPLSELRIACGVSRDGSNASNLLKAAREYGLTAKGYKKDLEALREVSLPAIVFW 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 749181994 93 NMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALEL 136
Cdd:cd02420 82 NFNHFLVVEGFDKRKVFLNDPATGRRTVSLEEFDQSFTGVVLTM 125
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
498-707 |
4.29e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.01 E-value: 4.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKgsNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHThpDYYQIRRRIGT 577
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLF-RGSIADNIIF------FSEDRNHERMIQCARLALIDsdimtmpmgyqTLIGETGGGLSGGQKQRILLARAL 650
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFglklrkVPKDEIDERVREVAELLQIE-----------HLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 651 YKKPGFLLLDEATSHLD----VESEIQISQTLRQLKVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:cd03301 146 VREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDG 207
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
416-707 |
4.53e-22 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 100.95 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 416 GTFTVGMLVAYLSYQMRFSSSISSLTDKFFAWRMLDVYNERLADIVLTPtegnqQQTAQENNSTSTTPSIfqervtedtd 495
Cdd:PRK10790 277 GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGP-----RQQYGNDDRPLQSGRI---------- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 496 lplTLTHIAFSHKgSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRI 575
Cdd:PRK10790 342 ---DIDNVSFAYR-DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLFRGSIADNIIF---FSEDRNHE--RMIQCARLAlidsdiMTMPMGYQTLIGETGGGLSGGQKQRILLARAL 650
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLgrdISEEQVWQalETVQLAELA------RSLPDGLYTPLGEQGNNLSVGQKQLLALARVL 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAHRLSTIVEADTILVLHRG 550
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
498-701 |
5.26e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.25 E-value: 5.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH--PDyyqiRRRI 575
Cdd:COG3842 6 LELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPE----KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQED----HLfrgSIADNIIF------FSEDRNHER------MIQCARLAliDSDIMTMPMGyqtligetggglsgg 639
Cdd:COG3842 80 GMVFQDYalfpHL---TVAENVAFglrmrgVPKAEIRARvaelleLVGLEGLA--DRYPHQLSGG--------------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 640 QKQRILLARALYKKPGFLLLDEATSHLDVE--SEIQ--ISQTLRQLKVPVLLIAHRPE---TIasADRV 701
Cdd:COG3842 140 QQQRVALARALAPEPRVLLLDEPLSALDAKlrEEMReeLRRLQRELGITFIYVTHDQEealAL--ADRI 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
509-707 |
1.96e-21 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 93.79 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT---HPDYYQIRRRIGTVLQEDHLF 585
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkGKALRQLRRQIGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 -RGSIADNII------------FFSedRNHERMIQCARLALIDSDIMTmpmgyqtLIGETGGGLSGGQKQRILLARALYK 652
Cdd:cd03256 91 eRLSVLENVLsgrlgrrstwrsLFG--LFPKEEKQRALAALERVGLLD-------KAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 653 KPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINreegITVIVSLHQVDLAREyADRIVGLKDG 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
507-707 |
2.72e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.41 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 507 HKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQE-DHLF 585
Cdd:PRK13650 15 KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RG-SIADNIIFFSEDRN--HERMIQCARLALidsDIMTMpmgyQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:PRK13650 95 VGaTVEDDVAFGLENKGipHEEMKERVNEAL---ELVGM----QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 663 TSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRddyqMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
498-707 |
3.38e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.97 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIIFFSEDRNHERMIQCARL----ALIDSDimtmpMGYQTLIGETGGGLSGGQKQRILLARALYKK 653
Cdd:PRK11160 419 VSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQvgleKLLEDD-----KGLNAWLGEGGRQLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 654 PGFLLLDEATSHLDVESEIQISQTLRQL---KVpVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEHaqnKT-VLMITHRLTGLEQFDRICVMDNG 549
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
498-706 |
4.26e-21 |
|
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: 92.16 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHkgSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPhTHPDYYQIRRRIGT 577
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-IRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRG-SIADNIIFFSE-------DRNHERMIQCARLA-LIDSDIMTMPMGyqtligetggglsggQKQRILLAR 648
Cdd:COG4133 80 LGHADGLKPElTVRENLRFWAAlyglradREAIDEALEAVGLAgLADLPVRQLSAG---------------QKRRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 649 ALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAsADRVLYLTD 706
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA-AARVLDLGD 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
511-708 |
9.47e-21 |
|
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: 91.05 E-value: 9.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG--IPHTHPDYYQIRRRIGTVLQEDHLF-RG 587
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVGMVFQQFNLFpHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIF-------FSEDRNHERMIQ-CARLAL---IDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGF 656
Cdd:cd03262 92 TVLENITLapikvkgMSKAEAEERALElLEKVGLadkADAYPAQLSGG---------------QQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 657 LLLDEATSHLDVESEIQISQTLRQL---KVPVLLIAH-----RpetiASADRVLYLTDGY 708
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHemgfaR----EVADRVIFMDDGR 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
514-706 |
9.74e-21 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 97.79 E-value: 9.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrTFGIPHTHPD--YYQIRRRIGTVLQEDHLFRGSIAD 591
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI-IINDSHNLKDinLKWWRSKIGVVSQDPLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIF--------------FSED----------RNHERMIQCARLALI--------------------DSDIM-------- 619
Cdd:PTZ00265 479 NIKYslyslkdlealsnyYNEDgndsqenknkRNSCRAKCAGDLNDMsnttdsneliemrknyqtikDSEVVdvskkvli 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 620 -----TMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP----VLLIAH 690
Cdd:PTZ00265 559 hdfvsALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAH 638
|
250
....*....|....*.
gi 749181994 691 RPETIASADRVLYLTD 706
Cdd:PTZ00265 639 RLSTIRYANTIFVLSN 654
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
170-441 |
1.17e-20 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 92.92 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTqmllslacQWASITLSVNFnMQWTA------- 242
Cdd:cd18545 5 ALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLV--------NWVASRLRIYL-MAKVGqrilydl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 --RVFHHLVRLPLAWFDARSRGSVNARF--DaIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYG 318
Cdd:cd18545 76 rqDLFSHLQKLSFSFFDSRPVGKILSRVinD-VNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 319 VMRTLWYPSLRQSAEDAWDAGARESGYFLETLSGIlslrinGVT--THREAA----WLNLNVTRRNTQLRQSRLLMYYDI 392
Cdd:cd18545 155 LVVFLLRRRARKAWQRVRKKISNLNAYLHESISGI------RVIqsFAREDEneeiFDELNRENRKANMRAVRLNALFWP 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 749181994 393 AHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18545 229 LVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLS 277
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
515-707 |
2.49e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.90 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI----RTFGIpHTHPdyyQiRRRIGTVLQEDHLFRG-SI 589
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngRDLFT-NLPP---R-ERRVGFVFQHYALFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFF------SEDRNHER------MIQCARLAliDSdimtMPM----GyqtligetggglsggQKQRILLARALYKK 653
Cdd:COG1118 93 AENIAFGlrvrppSKAEIRARveelleLVQLEGLA--DR----YPSqlsgG---------------QRQRVALARALAVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 654 PGFLLLDEATSHLDV----ESEIQISQTLRQLKVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:COG1118 152 PEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVTHdQEEALELADRVVVMNQG 210
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
179-441 |
2.87e-20 |
|
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: 91.78 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 179 ILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMllslACQWASITLSvnfnmQWTA---------RVFHHLV 249
Cdd:cd18546 13 AASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGW----VAQRAQTRLT-----GRTGerllydlrlRVFAHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 250 RLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMrTLWYpsl 328
Cdd:cd18546 84 RLSLDFHERETSGRIMTRMTSdIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALA-TRWF--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 329 RQSAEDAWDAgARES-----GYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSA 403
Cdd:cd18546 160 RRRSSRAYRR-ARERiaavnADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATA 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 749181994 404 IILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18546 239 AVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLS 276
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
519-707 |
4.96e-20 |
|
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: 89.09 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 519 SLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDyyQIRRRIGTVLQEDHLFRG-SIADNIIFFS 597
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP--PADRPVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 598 EDRNHERMIQCARLALIDSDimtmpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD--VESEIQ-- 673
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALAR-----VGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDpaLRAEMLdl 170
|
170 180 190
....*....|....*....|....*....|....*
gi 749181994 674 ISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03298 171 VLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
511-707 |
5.93e-20 |
|
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: 89.60 E-value: 5.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYyqiRRRIGTVLQEDHLF-RGS 588
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPH---KRPVNTVFQNYALFpHLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIF------FSED---RNHERMIQCARL-ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGFLL 658
Cdd:cd03300 89 VFENIAFglrlkkLPKAeikERVAEALDLVQLeGYANRKPSQLSGG---------------QQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 659 LDEATSHLDV----ESEIQISQTLRQLKVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:cd03300 154 LDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHdQEEALTMSDRIAVMNKG 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
515-707 |
7.71e-20 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 89.32 E-value: 7.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG--IPHTHPDyyqiRRRIGTVLQEDHLF-RGSIAD 591
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkdITNLPPE----KRDISYVPQNYALFpHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIF------FSEDRNHERMIQCARLA----LIDSDIMTMPMGYQtligetggglsggqkQRILLARALYKKPGFLLLDE 661
Cdd:cd03299 91 NIAYglkkrkVDKKEIERKVLEIAEMLgidhLLNRKPETLSGGEQ---------------QRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 662 ATSHLDVESEIQISQTL----RQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03299 156 PFSALDVRTKEKLREELkkirKEFGVTVLHVTHDFEEAWAlADKVAIMLNG 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
513-707 |
9.36e-20 |
|
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: 88.94 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrTFG---IPHTHPDyyqiRRRIGTVLQEDHLFRG-S 588
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTI-LFGgedATDVPVQ----ERNVGFVFQHYALFRHmT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIFFSEDRNHERMIQCARLALIDSDIMTMpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDV 668
Cdd:cd03296 91 VFDNVAFGLRVKPRSERPPEAEIRAKVHELLKL-VQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 749181994 669 ESEIQISQTLRQLK----VPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:cd03296 170 KVRKELRRWLRRLHdelhVTTVFVTHdQEEALEVADRVVVMNKG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
501-690 |
1.30e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 89.36 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 501 THIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI---RRRIGT 577
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafRRDIQM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQED-------HLFRGSIAD---NIIFFSEDRNHERMIQCARLA-LIDSDIMTMPmgyqtligetgGGLSGGQKQRILL 646
Cdd:PRK10419 94 VFQDSisavnprKTVREIIREplrHLLSLDKAERLARASEMLRAVdLDDSVLDKRP-----------PQLSGGQLQRVCL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 749181994 647 ARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAH 690
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQqqfgTACLFITH 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
518-707 |
1.32e-19 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 90.94 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI------------RTFGIPHthpdyyqiRRRIGTVLQEDHLF 585
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkGIFLPPE--------KRRIGYVFQEARLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 -RGSIADNIIF-FSEDRNHERMIQCARLalidsdimTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:TIGR02142 88 pHLSVRGNLRYgMKRARPSERRISFERV--------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 664 SHLDVESEIQISQTLRQL----KVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLhaefGIPILYVSHSLQEVLRlADRVVVLEDG 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
498-707 |
1.51e-19 |
|
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: 88.51 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLF-RGSIADNI------IFFSEDRNHERMIQCarLALIDSDIMTMPMGYQtligetgGGLSGGQKQRILLARAL 650
Cdd:cd03295 80 VIQQIGLFpHMTVEENIalvpklLKWPKEKIRERADEL--LALVGLDPAEFADRYP-------HELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHDiDEAFRLADRIAIMKNG 212
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
511-702 |
1.71e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 93.94 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIH-LPNEGTIrTFGIPHT------------------------- 564
Cdd:PTZ00265 1180 NVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdLKNDHHI-VFKNEHTndmtneqdyqgdeeqnvgmknvnef 1258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 565 -------HPDYYQIRRRIGTVL----------------------QEDHLFRGSIADNIIFFSEDRNHERMIQCARLALID 615
Cdd:PTZ00265 1259 sltkeggSGEDSTVFKNSGKILldgvdicdynlkdlrnlfsivsQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAID 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 616 SDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHR 691
Cdd:PTZ00265 1339 EFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAHR 1418
|
250
....*....|.
gi 749181994 692 PETIASADRVL 702
Cdd:PTZ00265 1419 IASIKRSDKIV 1429
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
498-707 |
1.89e-19 |
|
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: 87.98 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIafSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYYQIRRRIG 576
Cdd:cd03218 1 LRAENL--SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQEDHLFRG-SIADNIIFFSEDRNHERMIQCARL-ALIDSdimtmpMGYQTLIGETGGGLSGGQKQRILLARALYKKP 654
Cdd:cd03218 79 YLPQEASIFRKlTVEENILAVLEIRGLSKKEREEKLeELLEE------FHITHLRKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 655 GFLLLDEATSHLD--VESEIQ-ISQTLRQLKVPVLLIAH--RpETIASADRVLYLTDG 707
Cdd:cd03218 153 KFLLLDEPFAGVDpiAVQDIQkIIKILKDRGIGVLITDHnvR-ETLSITDRAYIIYEG 209
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
498-707 |
2.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSH-KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIG 576
Cdd:PRK13642 5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQE-DHLFRG-SIADNIIFFSEDRN--HERMIQCARLALIDSDIMTmpmgYQTligETGGGLSGGQKQRILLARALYK 652
Cdd:PRK13642 85 MVFQNpDNQFVGaTVEDDVAFGMENQGipREEMIKRVDEALLAVNMLD----FKT---REPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 653 KPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKekyqLTVLSITHDLDEAASSDRILVMKAG 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
510-707 |
3.23e-19 |
|
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: 85.95 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ-IRRRIGTVLqEDHLFRG- 587
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVP-EDRKREGl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 ----SIADNIIffsedrnhermiqcarLALIDSDimtmpmGYQtligetggglsggqkQRILLARALYKKPGFLLLDEAT 663
Cdd:cd03215 90 vldlSVAENIA----------------LSSLLSG------GNQ---------------QKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 749181994 664 SHLDVESEIQISQTLRQLK---VPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELAdagKAVLLISSElDELLGLCDRILVMYEG 180
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
498-707 |
3.81e-19 |
|
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: 84.42 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrtfgipHTHPDYyqirrRIGT 577
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------TWGSTV-----KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQedhlfrgsiadniifFSedrnhermiqcarlalidsdimtmpMGYQTligetggglsggqkqRILLARALYKKPGFL 657
Cdd:cd03221 68 FEQ---------------LS-------------------------GGEKM---------------RLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
498-707 |
4.44e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.88 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGT 577
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQE-DHLFRGSIADNIIFFSEDRN---HERMIQCARLALIDSDiMTMPMGY--QTLigetggglSGGQKQRILLARALY 651
Cdd:PRK13648 88 VFQNpDNQFVGSIVKYDVAFGLENHavpYDEMHRRVSEALKQVD-MLERADYepNAL--------SGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 652 KKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKsehnITIISITHDLSEAMEADHVIVMNKG 218
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
170-425 |
4.78e-19 |
|
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: 88.41 E-value: 4.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLV 249
Cdd:cd18566 7 VLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 250 RLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLR 329
Cdd:cd18566 87 SLPLSFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 330 QSAEDAWDAGARESGYFLETLSGILSLRINGVtthrEAAWLnlnvtRR------NTQLRQSRLLMYYDIAHTLTGS---V 400
Cdd:cd18566 167 RALKERSRADERRQNFLIETLTGIHTIKAMAM----EPQML-----RRyerlqaNAAYAGFKVAKINAVAQTLGQLfsqV 237
|
250 260
....*....|....*....|....*
gi 749181994 401 VSAIILWKGAGEVLNGTFTVGMLVA 425
Cdd:cd18566 238 SMVAVVAFGALLVINGDLTVGALIA 262
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
509-707 |
4.79e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 86.31 E-value: 4.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI---RRRIGTVLQEDHLF 585
Cdd:cd03292 11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKIGVVFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RG-SIADNIIFFSEDRNHE-RMIQ---CARLALID--SDIMTMPMGyqtligetgggLSGGQKQRILLARALYKKPGFLL 658
Cdd:cd03292 91 PDrNVYENVAFALEVTGVPpREIRkrvPAALELVGlsHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 659 LDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTtRHRVIALERG 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
513-709 |
5.81e-19 |
|
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: 87.60 E-value: 5.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGiphthpdyyqirrRIGTVLQEDHLFRGSIADN 592
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 IIF---FSEDRnHERMIQCARLaliDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVE 669
Cdd:cd03291 118 IIFgvsYDEYR-YKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 670 SEIQISQT----LRQLKVPVlLIAHRPETIASADRVLYLTDG--YF 709
Cdd:cd03291 194 TEKEIFEScvckLMANKTRI-LVTSKMEHLKKADKILILHEGssYF 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
511-707 |
6.91e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.24 E-value: 6.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH--PDyyqiRRRIGTVLQEDHLF-RG 587
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpAE----NRHVNTVFQSYALFpHM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIF--------FSE--DRNHE--RMIQCARLAliDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPG 655
Cdd:PRK09452 102 TVFENVAFglrmqktpAAEitPRVMEalRMVQLEEFA--QRKPHQLSGG---------------QQQRVAIARAVVNKPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 656 FLLLDEATSHLD----VESEIQISQTLRQLKVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:PRK09452 165 VLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDG 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
509-707 |
8.39e-19 |
|
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: 85.85 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRR----IGTVLQEDHL 584
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 FRGSIADNIIFFSEdRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATS 664
Cdd:cd03290 91 LNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 749181994 665 HLDVESEIQISQT-----LRQLKVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03290 170 ALDIHLSDHLMQEgilkfLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
498-707 |
1.13e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.21 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHkgSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtFG---IPHTHPDyyqiRRR 574
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL-IGgrdVTDLPPK----DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 575 IGTVLQE----DHLfrgSIADNIIF------FSEDRNHERMIQCARL----ALIDSdimtMPM----Gyqtligetgggl 636
Cdd:COG3839 77 IAMVFQSyalyPHM---TVYENIAFplklrkVPKAEIDRRVREAAELlgleDLLDR----KPKqlsgG------------ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 637 sggQKQRILLARALYKKPGFLLLDEATSHLD----VESEIQISQTLRQLKVPVLLIAHRP-ETIASADRVLYLTDG 707
Cdd:COG3839 138 ---QRQRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQvEAMTLADRIAVMNDG 210
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
474-707 |
1.62e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.87 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 474 QENNSTSTTPSIFQERVTEDTDLPLTLTHIAFSHkGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNE 553
Cdd:COG4178 339 EEALEAADALPEAASRIETSEDGALALEDLTLRT-PDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 554 GTIRtfgiphthpdyyqiRRRIGTVL---QEDHLFRGSIADNIIF------FSEDRNHERMIQC------ARLALIDSDI 618
Cdd:COG4178 418 GRIA--------------RPAGARVLflpQRPYLPLGTLREALLYpataeaFSDAELREALEAVglghlaERLDEEADWD 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 619 MTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETIA 696
Cdd:COG4178 484 QVLSLG---------------EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGHRSTLAA 548
|
250
....*....|.
gi 749181994 697 SADRVLYLTDG 707
Cdd:COG4178 549 FHDRVLELTGD 559
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
498-690 |
2.04e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.68 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSN--KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDyyqIRRri 575
Cdd:COG4525 4 LTVRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG---ADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLFRG-SIADNIIF----FSEDRNHERMIQCARLALIdsdimtmpmGYQTLIGETGGGLSGGQKQRILLARAL 650
Cdd:COG4525 79 GVVFQKDALLPWlNVLDNVAFglrlRGVPKAERRARAEELLALV---------GLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLrqLKV------PVLLIAH 690
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELL--LDVwqrtgkGVFLITH 193
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
511-669 |
2.07e-18 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 85.05 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHP--DYYQIRRRIGTVLQEDHLF-RG 587
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkDINKLRRKVGMVFQQFNLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIF-------FSEDRNHER-MIQCARLALIDSdIMTMPM----GyqtligetggglsggQKQRILLARALYKKPG 655
Cdd:COG1126 93 TVLENVTLapikvkkMSKAEAEERaMELLERVGLADK-ADAYPAqlsgG---------------QQQRVAIARALAMEPK 156
|
170
....*....|....
gi 749181994 656 FLLLDEATSHLDVE 669
Cdd:COG1126 157 VMLFDEPTSALDPE 170
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
470-707 |
2.71e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 90.04 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 470 QQTAQENNSTSTTpsifqERVTEDTDLPLTLTHI--------AFSHKGSNK-------------PILRGVSLTLHTGEVV 528
Cdd:PLN03232 1191 RQASKAENSLNSV-----ERVGNYIDLPSEATAIiennrpvsGWPSRGSIKfedvhlryrpglpPVLHGLSFFVSPSEKV 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 529 AITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFSEdRNHERMIQC 608
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSE-HNDADLWEA 1344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 609 ARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQ--LKVPVL 686
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTML 1424
|
250 260
....*....|....*....|.
gi 749181994 687 LIAHRPETIASADRVLYLTDG 707
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSG 1445
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
515-701 |
3.92e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.16 E-value: 3.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ-IRRRIGTVLQEDHLFRG-SIADN 592
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVPNlTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 IIFFSEDRNH--------ERMIQ--CARLAL-IDSD--IMTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLL 659
Cdd:COG3845 101 IVLGLEPTKGgrldrkaaRARIRelSERYGLdVDPDakVEDLSVG---------------EQQRVEILKALYRGARILIL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 660 DEATSHL-DVESEiQISQTLRQLK---VPVLLIAHR-PETIASADRV 701
Cdd:COG3845 166 DEPTAVLtPQEAD-ELFEILRRLAaegKSIIFITHKlREVMAIADRV 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
513-709 |
4.50e-18 |
|
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: 89.20 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGiphthpdyyqirrRIGTVLQEDHLFRGSIADN 592
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 IIF---FSEDRNHERMIQCArlalIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVE 669
Cdd:TIGR01271 507 IIFglsYDEYRYTSVIKACQ----LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 670 SEIQISQT-LRQLKV--PVLLIAHRPETIASADRVLYLTDG--YF 709
Cdd:TIGR01271 583 TEKEIFEScLCKLMSnkTRILVTSKLEHLKKADKILLLHEGvcYF 627
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
498-707 |
5.46e-18 |
|
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: 83.19 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHI--AFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIpHTHPDYYQIRRRI 575
Cdd:cd03266 2 ITADALtkRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF-DVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLF-RGSIADNIIFFSEDRNHERMIQCARLalidsDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKP 654
Cdd:cd03266 81 GFVSDSTGLYdRLTARENLEYFAGLYGLKGDELTARL-----EELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQLKVP---VLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALgkcILFSTHIMQEVERlCDRVVVLHRG 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
513-704 |
6.89e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 6.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGiphthpdyyqiRRRIGTVLQedhlfRGSIADN 592
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ-----RSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 ----------IIFFSEDRNHERMIQCARLALIDSdimTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:NF040873 70 lpltvrdlvaMGRWARRGLWRRLTRDDRAAVDDA---LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 663 TSHLDVESEIQISQTLRQL---KVPVLLIAHRPETIASADRVLYL 704
Cdd:NF040873 147 TTGLDAESRERIIALLAEEharGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
171-444 |
7.38e-18 |
|
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: 84.75 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 171 ITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLslACQWASitlsvNFNMQWTA-------- 242
Cdd:cd18544 5 LLLLLLATALELLGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSF--LLQYLQ-----TYLLQKLGqriiydlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 -RVFHHLVRLPLAWFDARSRGSVNARF--DaIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAA-VIYG 318
Cdd:cd18544 78 rDLFSHIQRLPLSFFDRTPVGRLVTRVtnD-TEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLpLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 319 VMRtlWYpslRQSAEDAWDAgARESgyfLETLSGILSLRINGVTT----HREAAWLN----LNVTRRNTQLRQSRL-LMY 389
Cdd:cd18544 157 ATY--LF---RKKSRKAYRE-VREK---LSRLNAFLQESISGMSViqlfNREKREFEefdeINQEYRKANLKSIKLfALF 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 390 YDIAHTLtGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKF 444
Cdd:cd18544 228 RPLVELL-SSLALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKF 281
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
498-693 |
7.39e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 83.98 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQirrriGT 577
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFR-GSIADNIIFFSE----DRNHERMIQCARLALIDSDIMTMPMGYQtligetgggLSGGQKQRILLARALYK 652
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVAFGLQlagvEKMQRLEIAHQMLKKVGLEGAEKRYIWQ---------LSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 653 KPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPE 693
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKLwqetGKQVLLITHDIE 190
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
174-440 |
7.62e-18 |
|
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: 84.49 E-value: 7.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 174 ALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLVRLPL 253
Cdd:cd18783 11 SLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 254 AWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLRQSAE 333
Cdd:cd18783 91 DFFERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 334 DAWDAGARESGYFLETLSGI---LSLRINGVtthREAAWLNLNVTRRNTQLRQSRLLMyydIAHTLTG---SVVSAIILW 407
Cdd:cd18783 171 ALYRAEGERQAFLVETVHGIrtvKSLALEPR---QRREWDERVARAIRARFAVGRLSN---WPQTLTGpleKLMTVGVIW 244
|
250 260 270
....*....|....*....|....*....|...
gi 749181994 408 KGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSL 440
Cdd:cd18783 245 VGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQL 277
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
514-707 |
8.21e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG--IPHTHPDyyqiRRRIGTVLQEDHLFRG-SIA 590
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdVSRLHAR----DRKVGFVFQHYALFRHmTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIF-FSEDRNHERmiqcARLALIDSDIMTMPMGYQT--LIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD 667
Cdd:PRK10851 93 DNIAFgLTVLPRRER----PNAAAIKAKVTQLLEMVQLahLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 668 VESEIQISQTLRQL----KVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:PRK10851 169 AQVRKELRRWLRQLheelKFTSVFVTHdQEEAMEVADRVVVMSQG 213
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
497-723 |
1.04e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.57 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 497 PLTLTHIafSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHThpdyyQIRRRIG 576
Cdd:PRK11247 12 PLLLNAV--SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA-----EAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQEDHLFR-GSIADNIIFFSedRNHERmiQCARLALidsdimtMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPG 655
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGL--KGQWR--DAALQAL-------AAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 656 FLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHR-PETIASADRVLYLTDGYF-----TDLTHQYRNGSEYL 723
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIeslwQQHGFTVLLVTHDvSEAVAMADRVLLIEEGKIgldltVDLPRPRRRGSARL 231
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-441 |
2.22e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 83.30 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 179 ILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQW--ASITLSVNFNMQwtARVFHHLVRLPLAWF 256
Cdd:cd18550 13 LLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYlsARIGQGVMYDLR--VQLYAHLQRMSLAFF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 257 DARSRGSVNARF--DaIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMrTLWYPSLRQS-AE 333
Cdd:cd18550 91 TRTRTGEIQSRLnnD-VGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLP-TRRVGRRRRKlTR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 334 DAWDAGARESGYFLETLS--GILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILWKGAG 411
Cdd:cd18550 169 EQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGL 248
|
250 260 270
....*....|....*....|....*....|
gi 749181994 412 EVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18550 249 LVIGGGLTIGTLVAFTALLGRLYGPLTQLL 278
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
512-707 |
2.39e-17 |
|
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: 81.17 E-value: 2.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGiphtHPDYYQIRRRIGTVLQEDHLFRG-SIA 590
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRIGYLPEERGLYPKmKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIFFSEDRN-------HERMIQCARLALID---SDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLLD 660
Cdd:cd03269 89 DQLVYLAQLKGlkkeearRRIDEWLERLELSEyanKRVEELSKG---------------NQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 661 EATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETI-ASADRVLYLTDG 707
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELAragKTVILSTHQMELVeELCDRVLLLNKG 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
512-690 |
2.61e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrtfgipHTHPDYyqirrRIGTVLQEDHLFRG-SIA 590
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------SIPKGL-----RIGYLPQEPPLDDDlTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNII-------------------FFSEDRNHERMIQC---------------ARLAL----IDSDIMTMPM-----Gyqt 627
Cdd:COG0488 80 DTVLdgdaelraleaeleeleakLAEPDEDLERLAELqeefealggweaearAEEILsglgFPEEDLDRPVselsgG--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 628 ligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAH 690
Cdd:COG0488 157 ------------WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSH 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
495-723 |
2.96e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.50 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 495 DLPLTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtFGiPHTHPDYY-QIRR 573
Cdd:COG0488 313 KKVLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LG-ETVKIGYFdQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 574 RI---GTVLqeDHLFRGSIADNIIF---------FSEDRNHERmiqCARLalidSdimtmpMGyqtligetggglsggQK 641
Cdd:COG0488 389 ELdpdKTVL--DELRDGAPGGTEQEvrgylgrflFSGDDAFKP---VGVL----S------GG---------------EK 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 642 QRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDGYFTDLTHQYrngS 720
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRvATRILEFEDGGVREYPGGY---D 515
|
...
gi 749181994 721 EYL 723
Cdd:COG0488 516 DYL 518
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
500-707 |
3.36e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 3.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 500 LTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHP--DYYQIRRRIGT 577
Cdd:PRK13637 8 LTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvKLSDIRKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQ--EDHLFRGSIADNIIF------FSEDRNHERMIQCARLALIDsdimtmpmgYQTLIGETGGGLSGGQKQRILLARA 649
Cdd:PRK13637 88 VFQypEYQLFEETIEKDIAFgpinlgLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 650 LYKKPGFLLLDEATSHLDVES--EI--QISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGrdEIlnKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKG 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
495-707 |
3.45e-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: 80.29 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 495 DLPLTLTHIAFSHKgsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILG--IHLPNEGTIRTFGIPhTHPDyyQIR 572
Cdd:cd03213 8 NLTVTVKSSPSKSG---KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRP-LDKR--SFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 573 RRIGTVLQEDHLFRGSIADNIIFFSedrnhermiqcARLALIDSDimtmpmgyqtligetggglsggQKQRILLARALYK 652
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFA-----------AKLRGLSGG----------------------ERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 653 KPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRP--ETIASADRVLYLTDG 707
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLAdtgRTIICSIHQPssEIFELFDKLLLLSQG 188
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
170-441 |
4.04e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 82.56 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSL--EILTLGSPLLNQLVIDEVLV----AADRSLLTVVIVALLLLSLTQMllslACQWASITLSVNFNMQWTA- 242
Cdd:cd18563 2 ILGFLLMLlgTALGLVPPYLTKILIDDVLIqlgpGGNTSLLLLLVLGLAGAYVLSA----LLGILRGRLLARLGERITAd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 ---RVFHHLVRLPLAWFDARSRGSVNAR--FDAiDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAA--V 315
Cdd:cd18563 78 lrrDLYEHLQRLSLSFFDKRQTGSLMSRvtSDT-DRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVplV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 316 IYGV------MRTLWYpslRQsaedaWDAGARESGYFLETLSGIlslRIngVTT----HREAAWLNlnvtRRNTQLRQSR 385
Cdd:cd18563 157 VWGSyffwkkIRRLFH---RQ-----WRRWSRLNSVLNDTLPGI---RV--VKAfgqeKREIKRFD----EANQELLDAN 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 386 L------LMYYDIAHTLTgSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18563 220 IraeklwATFFPLLTFLT-SLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLS 280
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
505-707 |
4.13e-17 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 83.20 E-value: 4.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT---HPDYYQIRRRIGTVLQE 581
Cdd:COG1135 11 FPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalsERELRAARRKIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLFRG-SIADNIIF------FSEDRNHERmiqcAR--LALID------------SDimtmpmGyqtligetggglsggQ 640
Cdd:COG1135 91 FNLLSSrTVAENVALpleiagVPKAEIRKR----VAelLELVGlsdkadaypsqlSG------G---------------Q 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLkdinRELGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
518-707 |
5.33e-17 |
|
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: 83.23 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR---------TFGI---PHthpdyyqiRRRIGTVLQEDHLF 585
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsARGIflpPH--------RRRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 -----RGSIADNIIFFSEDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGF 656
Cdd:COG4148 90 phlsvRGNLLYGRKRAPRAERRISFDEVVELlgigHLLDRRPATLSGG---------------ERQRVAIGRALLSSPRL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 657 LLLDEATSHLDVES--EIQ--ISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG4148 155 LLMDEPLAALDLARkaEILpyLERLRDELDIPILYVSHSLDEVARlADHVVLLEQG 210
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
243-442 |
5.96e-17 |
|
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: 81.76 E-value: 5.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLI-------AVLAA 314
Cdd:cd18576 74 DLYRHLQRLPLSFFHERRVGELTSRLSNdVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLmlatvpvVVLVA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 315 VIYGvmrtlwyPSLRQSAEDAWDAGARESGYFLETLSGILSLRingvTTHREAawlnLNVTRRNTQLRQS-RLLMYYDIA 393
Cdd:cd18576 154 VLFG-------RRIRKLSKKVQDELAEANTIVEETLQGIRVVK----AFTRED----YEIERYRKALERVvKLALKRARI 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 394 HTLTGSVVS-------AIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTD 442
Cdd:cd18576 219 RALFSSFIIfllfgaiVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLAD 274
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
502-704 |
6.44e-17 |
|
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: 82.41 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 502 HIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPN---EGTIRTFGIPHTH---PDYYQIR-RR 574
Cdd:COG0444 8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKlseKELRKIRgRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 575 IGTVLQE-----DHLFR-G-SIADNIIFF---SEDRNHERMIQCARLALIDSDIMTMPM-------Gyqtligetgggls 637
Cdd:COG0444 88 IQMIFQDpmtslNPVMTvGdQIAEPLRIHgglSKAEARERAIELLERVGLPDPERRLDRyphelsgG------------- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 638 ggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADR--VLYL 704
Cdd:COG0444 155 --MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQrelgLAILFITHDLGVVAEiADRvaVMYA 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
507-707 |
9.28e-17 |
|
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: 79.86 E-value: 9.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 507 HKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPhTHPDYYQIRRRIGTVLQEDHLFR 586
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS-IRTDRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 G-SIADNIIFFS---------EDRNHERMIQCARL-ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPG 655
Cdd:cd03263 89 ElTVREHLRFYArlkglpkseIKEEVELLLRVLGLtDKANKRARTLSGG---------------MKRKLSLAIALIGGPS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 656 FLLLDEATSHLDVESEIQISQTLRQLKV--PVLLIAHRPETI-ASADRVLYLTDG 707
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAeALCDRIAIMSDG 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
511-682 |
1.07e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.47 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVK-------LILGIHLpnEGTIRTFGIPHTHPDY--YQIRRRIGTVLQE 581
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGEDIYDPDVdvVELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLFRGSIADNIIF-------FSEDRNHERMIQCARLALI--------DSDIMTMPMGyqtligetggglsggQKQRILL 646
Cdd:COG1117 101 PNPFPKSIYDNVAYglrlhgiKSKSELDEIVEESLRKAALwdevkdrlKKSALGLSGG---------------QQQRLCI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 749181994 647 ARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK 682
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELK 201
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
515-704 |
1.11e-16 |
|
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: 79.79 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRR-IGTVLQEDHLFRG-SIADN 592
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 I-----------IFFSEDRNHERMIQCARLALID----SDIMTMPMGyqTLigetggglSGGQKQRILLARALYKKPGFL 657
Cdd:cd03219 96 VmvaaqartgsgLLLARARREEREARERAEELLErvglADLADRPAG--EL--------SYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYL 704
Cdd:cd03219 166 LLDEPAAGLNPEETEELAELIRELRergITVLLVEHDMDVVMSlADRVTVL 216
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
170-441 |
1.70e-16 |
|
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: 80.91 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSL--EILTLGSPLLNQLVIDEVLVAADRS-------------LLTVVIVALLllsltqmllslACQW------A 228
Cdd:cd18547 2 ILVIILAIisTLLSVLGPYLLGKAIDLIIEGLGGGggvdfsgllrillLLLGLYLLSA-----------LFSYlqnrlmA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 229 SITLSVNFNMQwtARVFHHLVRLPLAWFDARSRGSVNARF--DaIDTIQQALT---TQVLEGILdvlLVVTALCMMLLYS 303
Cdd:cd18547 71 RVSQRTVYDLR--KDLFEKLQRLPLSYFDTHSHGDIMSRVtnD-VDNISQALSqslTQLISSIL---TIVGTLIMMLYIS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 304 PEMTLIAVL-AAVIYGVMRTLwypsLRQSAE---DAWDAGARESGYFLETLSGILSLRINGvttHREAAwlNLNVTRRNT 379
Cdd:cd18547 145 PLLTLIVLVtVPLSLLVTKFI----AKRSQKyfrKQQKALGELNGYIEEMISGQKVVKAFN---REEEA--IEEFDEINE 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 380 QLRQSrllmyYDIAHTLTGS-------------VVSAIIlwkGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18547 216 ELYKA-----SFKAQFYSGLlmpimnfinnlgyVLVAVV---GGLLVINGALTVGVIQAFLQYSRQFSQPINQIS 282
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
513-707 |
1.71e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 84.40 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI-------RTFGIphthpdyYQIRRRIGTVLQEDHLF 585
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIlidgcdiSKFGL-------MDLRKVLGIIPQAPVLF 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RGSIADNIIFFSEDRNHERMIQCARLALIDSdIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSH 665
Cdd:PLN03130 1326 SGTVRFNLDPFNEHNDADLWESLERAHLKDV-IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 749181994 666 LDVESEIQISQTLRQ--LKVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PLN03130 1405 VDVRTDALIQKTIREefKSCTMLIIAHRLNTIIDCDRILVLDAG 1448
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
510-706 |
2.00e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 77.19 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrtfGIPhthpdyyqirrrigtvLQEDHLF---- 585
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMP----------------EGEDLLFlpqr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 ----RGSIADNIIF-----FSEDrnhermiqcarlalidsdimtmpmgyqtligetggglsggQKQRILLARALYKKPGF 656
Cdd:cd03223 73 pylpLGTLREQLIYpwddvLSGG----------------------------------------EQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 749181994 657 LLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHRPETIASADRVLYLTD 706
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
243-695 |
2.52e-16 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 83.81 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMR 321
Cdd:TIGR01271 963 QMLHSVLQAPMAVLNTMKAGRILNRFTKdMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLR 1042
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 322 TLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHRE-----------AAWLNLNVTRRNTQLRQSRLLMYY 390
Cdd:TIGR01271 1043 AYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFEtlfhkalnlhtANWFLYLSTLRWFQMRIDIIFVFF 1122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 391 DIAHTLtgsvVSAIILWKGAGEVlNGTFTVGMLVAYlSYQMRFSSSISslTDKFfawrMLDVynERLADIVLTPTEGNQQ 470
Cdd:TIGR01271 1123 FIAVTF----IAIGTNQDGEGEV-GIILTLAMNILS-TLQWAVNSSID--VDGL----MRSV--SRVFKFIDLPQEEPRP 1188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 471 QTAQENNSTSTTPSIFQERVTED--TDLPLTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGI 548
Cdd:TIGR01271 1189 SGGGGKYQLSTVLVIENPHAQKCwpSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL 1268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 549 hLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNIIFFsEDRNHERMIQCARLALIDSDIMTMPMGYQTL 628
Cdd:TIGR01271 1269 -LSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPY-EQWSDEEIWKVAEEVGLKSVIEQFPDKLDFV 1346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 629 IGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETI 695
Cdd:TIGR01271 1347 LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEHRVEAL 1415
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
497-711 |
3.02e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 81.43 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 497 PLTLTHIAFSHKGSnkPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIG 576
Cdd:PRK09536 3 MIDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQED------------------HLFRGSIADNiiffSEDRNHER-MIQCARLALIDSDIMTMPMGyqtligetgggls 637
Cdd:PRK09536 81 SVPQDTslsfefdvrqvvemgrtpHRSRFDTWTE----TDRAAVERaMERTGVAQFADRPVTSLSGG------------- 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 638 ggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIaHRPETIAS-ADRVLYLTDGYFTD 711
Cdd:PRK09536 144 --ERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLvddgKTAVAAI-HDLDLAARyCDELVLLADGRVRA 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
487-717 |
3.20e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 487 QERVTEDTDLpLTLTHIAFSHKGSnkPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH- 565
Cdd:PRK15439 2 QTSDTTAPPL-LCARSISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 566 -PDYYQiRRRIGTVLQEDHLFRG-SIADNIIFF--SEDRNHERMIQcaRLALIDSDI-MTMPMGyqTLigetggglSGGQ 640
Cdd:PRK15439 79 tPAKAH-QLGIYLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQ--LLAALGCQLdLDSSAG--SL--------EVAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLD-VESEIQISQ--TLRQLKVPVLLIAHR-PETIASADRVLYLTDGY--FTDLTH 714
Cdd:PRK15439 146 RQIVEILRGLMRDSRILILDEPTASLTpAETERLFSRirELLAQGVGIVFISHKlPEIRQLADRISVMRDGTiaLSGKTA 225
|
...
gi 749181994 715 QYR 717
Cdd:PRK15439 226 DLS 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
518-709 |
4.61e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 80.65 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQirRRIGTVLQEDHLF-RGSIADNIIF- 595
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ--RPINMMFQSYALFpHMTVEQNIAFg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 596 FSEDRNHERMIQcARLAlidsDIMTMpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVE----SE 671
Cdd:PRK11607 116 LKQDKLPKAEIA-SRVN----EMLGL-VHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQ 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 749181994 672 IQISQTLRQLKVPVLLIAH-RPETIASADRVLYLTDGYF 709
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
510-707 |
5.10e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.28 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLI--LGIHLPN---EGTIRTFG--IPHTHPDYYQIRRRIGTVLQED 582
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGhnIYSPRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 583 HLFRGSIADNIIF---FSEDRNHERMIQCARLALIDSDIMTMpmgYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLL 659
Cdd:PRK14239 96 NPFPMSIYENVVYglrLKGIKDKQVLDEAVEKSLKGASIWDE---VKDRLHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 660 DEATSHLDVESEIQISQTLRQLKVP-VLLIAHRPETIAS--ADRVLYLTDG 707
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDyTMLLVTRSMQQASriSDRTGFFLDG 223
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
510-707 |
6.21e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKL------ILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDH 583
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 LF-RGSIADNIIF------FSEDRNHERMIQ-CARLALIDSDImtmpmgyQTLIGETGGGLSGGQKQRILLARALYKKPG 655
Cdd:PRK14246 101 PFpHLSIYDNIAYplkshgIKEKREIKKIVEeCLRKVGLWKEV-------YDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 656 FLLLDEATSHLDVESEIQISQTLRQLK--VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKneIAIVIVSHNPQQVARvADYVAFLYNG 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
515-710 |
6.37e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI---RRRIGTVLQEDHLFRG-SIA 590
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQIGMIFQDHHLLMDrTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DN-----IIFFSEDRNHERMIQCA--RLALIDSdIMTMPMgyqtligetggGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:PRK10908 98 DNvaiplIIAGASGDDIRRRVSAAldKVGLLDK-AKNFPI-----------QLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 664 SHLD---VESEIQISQTLRQLKVPVLLIAHRPETIASAD-RVLYLTDGYFT 710
Cdd:PRK10908 166 GNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
515-707 |
6.40e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 77.51 E-value: 6.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIrrrigTVLQEDHLFRGSIADNII 594
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 595 FFSEDRNHERMIQCARLALIDSDIMTmpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQI 674
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIVEEHIAL--VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 749181994 675 SQTLRQL----KVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:TIGR01184 154 QEELMQIweehRVTVLMVTHDvDEALLLSDRVVMLTNG 191
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
512-711 |
7.44e-16 |
|
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: 78.03 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIAD 591
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIffSEDR-NHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVES 670
Cdd:cd03288 114 NLD--PECKcTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 749181994 671 EiQISQTLRQLKVP---VLLIAHRPETIASADRVLYLTDGYFTD 711
Cdd:cd03288 192 E-NILQKVVMTAFAdrtVVTIAHRVSTILDADLVLVLSRGILVE 234
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
17-134 |
7.62e-16 |
|
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: 74.34 E-value: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 17 QTESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCILHWNMNH 96
Cdd:cd02259 1 GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLPALLLWKQGH 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 749181994 97 FVVLHKVRRSRLVIHDP-DKGKITLSLQDAGKHFTGVAL 134
Cdd:cd02259 81 FVILYGADKGQVLIADPlEEGPVTLSESELEERWTGHWV 119
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
179-429 |
1.07e-15 |
|
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: 78.24 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 179 ILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVN--FNMQwtARVFHHLVRLPLAWF 256
Cdd:cd18542 13 ALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKvaYDLR--NDLYDHLQRLSFSFH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 257 DARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLRQSAEDA 335
Cdd:cd18542 91 DKARTGDLMSRCTSdVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 336 WDAGAResgyfletLSGILSLRINGVTT----HREAA----WLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILW 407
Cdd:cd18542 171 REQEGE--------LNTVLQENLTGVRVvkafAREDYeiekFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLW 242
|
250 260
....*....|....*....|..
gi 749181994 408 KGAGEVLNGTFTVGMLVAYLSY 429
Cdd:cd18542 243 VGGYLVINGEITLGELVAFISY 264
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
511-707 |
1.29e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP-HTHPDYYQIRRRigTVL-QEDHL---F 585
Cdd:COG4559 13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPlAAWSPWELARRR--AVLpQHSSLafpF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 R-------GSIAdniiFFSEDRNHERMIQCArLALIDsdimTMPMG---YQTLigetggglSGGQKQRILLARAL----- 650
Cdd:COG4559 91 TveevvalGRAP----HGSSAAQDRQIVREA-LALVG----LAHLAgrsYQTL--------SGGEQQRVQLARVLaqlwe 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 651 --YKKPGFLLLDEATSHLDVESEIQISQTLRQL---KVPVLLIAHRPEtIAS--ADRVLYLTDG 707
Cdd:COG4559 154 pvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLarrGGGVVAVLHDLN-LAAqyADRILLLHQG 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
513-707 |
2.23e-15 |
|
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: 75.93 E-value: 2.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYYQIRRRIGTVLQEDHLFRG-SIA 590
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHERARAGIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNI---IFFSEDRNHERMIQ------------CARLAlidsdiMTMPMGyqtligetggglsggQKQRILLARALYKKPG 655
Cdd:cd03224 94 ENLllgAYARRRAKRKARLErvyelfprlkerRKQLA------GTLSGG---------------EQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 656 FLLLDEATSHLD---VESEIQISQTLRQLKVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:cd03224 153 LLLLDEPSEGLApkiVEEIFEAIRELRDEGVTILLVEQNaRFALEIADRAYVLERG 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
508-707 |
2.29e-15 |
|
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: 75.77 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 508 KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGiHLPN----EGTIRTFGIPhthPDYYQIRRRIGTVLQEDH 583
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGggttSGQILFNGQP---RKPDQFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 LFRG-SIADNIIFFSEDRNHERMIQcARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:cd03234 92 LLPGlTVRETLTYTAILRLPRKSSD-AIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 749181994 663 TSHLDVESEIQISQTLRQLKVP---VLLIAH--RPETIASADRVLYLTDG 707
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRnriVILTIHqpRSDLFRLFDRILLLSSG 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
505-707 |
6.38e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 76.76 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT---HPDYYQIRRRIGTVLQe 581
Cdd:PRK11153 11 FPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalsEKELRKARRQIGMIFQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 dH---LFRGSIADNIIFFSE-DRNHERMIQcAR----LALID-SDIM-TMPM----GyqtligetggglsggQKQRILLA 647
Cdd:PRK11153 90 -HfnlLSSRTVFDNVALPLElAGTPKAEIK-ARvtelLELVGlSDKAdRYPAqlsgG---------------QKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 648 RALYKKPGFLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK11153 153 RALASNPKVLLCDEATSALDPATTRSILELLkdinRELGLTIVLITHEMDVVKRiCDRVAVIDAG 217
|
|
| C39G |
COG3271 |
Predicted double-glycine leader peptidase, C39-like (CLD) domain [Intracellular trafficking, ... |
1-134 |
8.65e-15 |
|
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: 73.10 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 1 MELMNWTGKKRLPLIRQTESAECGLACLA-MMACWHGLQTDLTTLRER----FSISTQGMTLQRLIECAAGIQLSSRAVR 75
Cdd:COG3271 32 VPVKSLKELRFRNVVRQQYDYSCGAAALAtLLNYHYGRPVSEAEVLEGmlthGDQRRRGFSLLDMKRYLEALGLRADGYR 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 76 LEPEDLKSLSLPCILHWNM---NHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVAL 134
Cdd:COG3271 112 LTLDDLAQLGIPAIVLINLggyKHFVVVKGVDDGRVLLADPALGNRSLSREEFEKMWDGNVL 173
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
179-427 |
9.55e-15 |
|
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: 75.54 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 179 ILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALlllsltqmllslacqwasITLSV---------NFNMQWTA------- 242
Cdd:cd18552 13 ATTAALAWLLKPLLDDIFVEKDLEALLLVPLAI------------------IGLFLlrglasylqTYLMAYVGqrvvrdl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 --RVFHHLVRLPLAWFDARSRGSVNARF--DaIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAA-VIY 317
Cdd:cd18552 75 rnDLFDKLLRLPLSFFDRNSSGDLISRItnD-VNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLpLAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 318 GVMRTLwYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRllmYYDIAHTLT 397
Cdd:cd18552 154 LPIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIAR---ARALSSPLM 229
|
250 260 270
....*....|....*....|....*....|...
gi 749181994 398 ---GSVVSAIILWKGAGEVLNGTFTVGMLVAYL 427
Cdd:cd18552 230 ellGAIAIALVLWYGGYQVISGELTPGEFISFI 262
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
517-690 |
9.93e-15 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 75.92 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 517 GVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHP---DYYQIRRRIGTVLQEDHlfrGS----- 588
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLsgrELRPLRRRMQMVFQDPY---ASlnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 -IADnIIffSED-RNHERMIQCARLALIDsDIMTM-----------PM----GyqtligetggglsggQKQRILLARALY 651
Cdd:COG4608 113 tVGD-II--AEPlRIHGLASKAERRERVA-ELLELvglrpehadryPHefsgG---------------QRQRIGIARALA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 652 KKPGFLLLDEATSHLDVeSeIQiSQTL-------RQLKVPVLLIAH 690
Cdd:COG4608 174 LNPKLIVCDEPVSALDV-S-IQ-AQVLnlledlqDELGLTYLFISH 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
511-707 |
1.43e-14 |
|
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: 73.02 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPdyYQIRRRIGTVLQE----DHLfr 586
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGALIEApgfyPNL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 gSIADNIIFFS-----EDRNHERMIQCARLALIDSD-IMTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLLD 660
Cdd:cd03268 88 -TARENLRLLArllgiRKKRIDEVLDVVGLKDSAKKkVKGFSLG---------------MKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 661 EATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKvADRIGIINKG 202
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
511-681 |
1.48e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPhtHPDYYQI-RRRIGTVLQEDHLFRG-S 588
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP--VPARARLaRARIGVVPQFDNLDLEfT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIFFSED-RNHERMIQCARLALIDSDIMtmpmgyQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD 667
Cdd:PRK13536 131 VRENLLVFGRYfGMSTREIEAVIPSLLEFARL------ESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170
....*....|....
gi 749181994 668 VESEIQISQTLRQL 681
Cdd:PRK13536 205 PHARHLIWERLRSL 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
515-727 |
1.99e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.05 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVK-------LILGIHLpnEGTIRTFG--IPHTHPDYYQIRRRIGTVLQEDHLF 585
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGknLYAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RGSIADNIIFFSE--------DRNHERMIQCArlALIDSDIMTMPMGYQTLigetggglSGGQKQRILLARALYKKPGFL 657
Cdd:PRK14243 104 PKSIYDNIAYGARingykgdmDELVERSLRQA--ALWDEVKDKLKQSGLSL--------SGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLK--VPVLLIAHrpeTIASADRVLYLTDGYFTDLTHQ-YRNGseYLVRMD 727
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKeqYTIIIVTH---NMQQAARVSDMTAFFNVELTEGgGRYG--YLVEFD 241
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
170-440 |
2.03e-14 |
|
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: 74.44 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSL--EILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHH 247
Cdd:cd18543 2 ILALLAALlaTLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 248 LVRLPLAWFDARSRGSVNARfdAIDTIQ--QALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGV----MR 321
Cdd:cd18543 82 LQRLDGAFHDRWQSGQLLSR--ATSDLSlvQRFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLvarrFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 322 TLWYPSLRQSAEDAWD-AGAREsgyflETLSGILSLRINGvtthREAAWLNLNVTR----RNTQLRQSRLLMYYDIAHTL 396
Cdd:cd18543 160 RRYFPASRRAQDQAGDlATVVE-----ESVTGIRVVKAFG----RERRELDRFEAAarrlRATRLRAARLRARFWPLLEA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 749181994 397 TGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSL 440
Cdd:cd18543 231 LPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRML 274
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
505-707 |
2.17e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.00 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNKPiLRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQ--ED 582
Cdd:PRK13647 12 FRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQdpDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 583 HLFRGSIADNIIF------FSEDRNHERmiqcARLALidsDIMTMpmgyQTLIGETGGGLSGGQKQRILLARALYKKPGF 656
Cdd:PRK13647 91 QVFSSTVWDDVAFgpvnmgLDKDEVERR----VEEAL---KAVRM----WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 657 LLLDEATSHLD---VESEIQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13647 160 IVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEG 214
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-701 |
2.72e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKpILRGVSLTLHTGEVVAITGKSGCGKSTLVK-----LILGIHLPNEGTIRTFGIPHTHPDY--YQIRRRIGTVLQE 581
Cdd:PRK14267 15 GSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVdpIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLF-RGSIADNI--------IFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTligetggGLSGGQKQRILLARALYK 652
Cdd:PRK14267 94 PNPFpHLTIYDNVaigvklngLVKSKKELDERVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALAM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 653 KPGFLLLDEATSHLDVESEIQISQTLRQLK--VPVLLIAHRPetiASADRV 701
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKkeYTIVLVTHSP---AQAARV 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
514-707 |
4.96e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 4.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKlILG-IHLPNEGTIRTFG--IPHTHPDYYQIRRR--IGTVLQEDHLFRG- 587
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGcLDKPTSGTYRVAGqdVATLDADALAQLRRehFGFIFQRYHLLSHl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNI----IFFSEDRNH--ERMIQ-CARLALIDSdimtmpMGYQTligetgGGLSGGQKQRILLARALYKKPGFLLLD 660
Cdd:PRK10535 102 TAAQNVevpaVYAGLERKQrlLRAQElLQRLGLEDR------VEYQP------SQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 749181994 661 EATSHLDVESEIQISQTLRQLKV---PVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
243-441 |
5.40e-14 |
|
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: 73.24 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFDAiDT--IQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVM 320
Cdd:cd18551 74 RLWRRLLRLPVSFFDRRRSGDLVSRVTN-DTtlLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 321 RTLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGvTTHREAAwlnlNVTRRNTQLRQS--RLLMYYDIAHTLTG 398
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASN-AEERETK----RGGEAAERLYRAglKAAKIEALIGPLMG 227
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 399 SVVSA---IILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18551 228 LAVQLallVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLS 273
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
505-707 |
5.94e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 71.98 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG-IPHTHPDyyQIRRRIGTVL-QED 582
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRK--KFLRRIGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 583 HLF-----RGSIADN--IIFFSEDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALY 651
Cdd:cd03267 105 QLWwdlpvIDSFYLLaaIYDLPPARFKKRLDELSELldleELLDTPVRQLSLG---------------QRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 652 KKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEAlARRVLVIDKG 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
514-707 |
8.51e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.70 E-value: 8.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR--------TFGIPHTHPDYYQIRRRIGTVLQEDHLF 585
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtARSLSQQKGLIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 -RGSIADNII---FFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIgetggglSGGQKQRILLARALYKKPGFLLLDE 661
Cdd:PRK11264 98 pHRTVLENIIegpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRL-------SGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 662 ATSHLDVESEIQISQTLRQL---KVPVLLIAHRpETIAS--ADRVLYLTDG 707
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQLaqeKRTMVIVTHE-MSFARdvADRAIFMDQG 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
498-704 |
9.63e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.68 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHkgSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtfgiphthpdyYQIRRRIGT 577
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLfrgsiaDNIIFFSEDRnhermIQCARLALIDSDIMTMPMGYQT--LIGETGGGLSGGQKQRILLARALYKKPG 655
Cdd:PRK09544 72 VPQKLYL------DTTLPLTVNR-----FLRLRPGTKKEDILPALKRVQAghLIDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 656 FLLLDEATSHLDVESEIQ----ISQTLRQLKVPVLLIAHRPETI-ASADRVLYL 704
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVAlydlIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
514-707 |
1.02e-13 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.20 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNI 593
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 594 IFFSEDRNHERMiqcARLAL-------------IDSDIMTMPMGYQTligetggglsgGQKQRILLARALYKK-PGFLLL 659
Cdd:PTZ00243 1405 DPFLEASSAEVW---AALELvglrervasesegIDSRVLEGGSNYSV-----------GQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 749181994 660 DEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAfsAYTVITIAHRLHTVAQYDKIIVMDHG 1520
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
243-442 |
1.06e-13 |
|
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: 72.21 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMr 321
Cdd:cd18557 74 DLFSSLLRQEIAFFDKHKTGELTSRLSSdTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIA- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 322 TLWYPS-LRQSAEDAWDAGARESGYFLETLSGILSLRINGvtthREAAwlnlNVTRRNTQLRQS--------RLLMYYDI 392
Cdd:cd18557 153 SKIYGRyIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFS----AEEK----EIRRYSEALDRSyrlarkkaLANALFQG 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 749181994 393 AHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTD 442
Cdd:cd18557 225 ITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSS 274
|
|
| Peptidase_C39E |
cd02424 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
14-135 |
1.18e-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, which contains Colicin V perocessing peptidase.
Pssm-ID: 239104 [Multi-domain] Cd Length: 129 Bit Score: 68.13 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 14 LIRQTESAECGLACLAMMA-CWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLP---CI 89
Cdd:cd02424 3 IIKQTDLNDCGIAVIQMLYnHYYKKKYDLNELKIKANLKKNGLSIYDLENLAKKFGLETESYQGSFLEFLELKNKfiiLL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 749181994 90 LHWNMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVALE 135
Cdd:cd02424 83 KSNGLNHFVIVKKIKKNKFIVLDPKKGKYKITYKEFEKIFNNIIIT 128
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
509-707 |
1.43e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.83 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKPIlRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQirRRIGTVLQEDHLF-RG 587
Cdd:PRK11432 17 GSNTVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFpHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIF--FSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIgetggglSGGQKQRILLARALYKKPGFLLLDEATSH 665
Cdd:PRK11432 94 SLGENVGYglKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 666 LDVESEIQISQTLR----QLKVPVLLIAH-RPETIASADRVLYLTDG 707
Cdd:PRK11432 167 LDANLRRSMREKIRelqqQFNITSLYVTHdQSEAFAVSDTVIVMNKG 213
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
515-707 |
1.48e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 71.73 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH--PDYY--QIRRRIGTVLQ--EDHLFRGS 588
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktKDKYirPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIF----FS------EDRNHERMIQCArlalIDSDIMT-----MPMGyqtligetggglsggQKQRILLARALYKK 653
Cdd:PRK13646 103 VEREIIFgpknFKmnldevKNYAHRLLMDLG----FSRDVMSqspfqMSGG---------------QMRKIAIVSILAMN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 654 PGFLLLDEATSHLDVESEIQISQTLRQLKV----PVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdenkTIILVSHDMNEVARyADEVIVMKEG 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
519-707 |
1.77e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.55 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 519 SLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQirRRIGTVLQEDHLFRG-SIADNIIF-F 596
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSMLFQENNLFPHlTVAQNIGLgL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 597 SEDRN-----HERMIQCARlalidsdimtmPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD---- 667
Cdd:COG3840 97 RPGLKltaeqRAQVEQALE-----------RVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 749181994 668 VESEIQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG3840 166 QEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADG 206
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
243-429 |
2.96e-13 |
|
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: 70.90 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARF--DaIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVL-----AAV 315
Cdd:cd18541 78 DLFAHLLTLSPSFYQKNRTGDLMARAtnD-LNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLplpllALL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 316 IYGVMRTLwypslRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHT 395
Cdd:cd18541 157 VYRLGKKI-----HKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
|
170 180 190
....*....|....*....|....*....|....
gi 749181994 396 LTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSY 429
Cdd:cd18541 232 LLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNSY 265
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
513-707 |
3.96e-13 |
|
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: 69.39 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtfgIPHTHP----------DYYQIRRR-IGTVLQ- 580
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL---VRHDGGwvdlaqasprEILALRRRtIGYVSQf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 581 ---------EDHLFRGSIADNIiffSEDRNHERmiqcARLAL----IDSDIMTMPM-----GyqtligetggglsggQKQ 642
Cdd:COG4778 102 lrviprvsaLDVVAEPLLERGV---DREEARAR----ARELLarlnLPERLWDLPPatfsgG---------------EQQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 643 RILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKargTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
505-683 |
4.19e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.07 E-value: 4.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLI-----LGIHLPNEGTIRTFG--IPHTHPDYYQIRRRIGT 577
Cdd:PRK14258 13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNqnIYERRVNLNRLRRQVSM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIIFFSED---RNHERMIQCARLALIDSDIMTMpmgYQTLIGETGGGLSGGQKQRILLARALYKKP 654
Cdd:PRK14258 93 VHPKPNLFPMSVYDNVAYGVKIvgwRPKLEIDDIVESALKDADLWDE---IKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180
....*....|....*....|....*....
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQLKV 683
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRL 198
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
515-707 |
5.96e-13 |
|
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: 69.59 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT---HPDYYQIRR-RIGTVLQEDHLF-RGSI 589
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsRKELRELRRkKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFFSEDRN------HERMIQCARLALIDSDIMTMPmgyqtligetgGGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:cd03294 120 LENVAFGLEVQGvpraerEERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 664 SHLD--VESEIQ--ISQTLRQLKVPVLLIAHRP-ETIASADRVLYLTDG 707
Cdd:cd03294 189 SALDplIRREMQdeLLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDG 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
511-707 |
6.72e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.42 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHL---FRG 587
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 S------IADNIIFFSEDRNH-ERMIQCARLA-LIDSDimtmpmgYQTLigetggglSGGQKQRILLARAL------YKK 653
Cdd:PRK13548 94 EevvamgRAPHGLSRAEDDALvAAALAQVDLAhLAGRD-------YPQL--------SGGEQQRVQLARVLaqlwepDGP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 654 PGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPE-TIASADRVLYLTDG 707
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHDLNlAARYADRIVLLHQG 217
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
242-429 |
7.36e-13 |
|
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: 69.85 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 242 ARVFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAA-VIYGV 319
Cdd:cd18564 91 RDLFAHLQRLSLSFHDRRRTGDLLSRLTGdVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVApLLLLA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 320 MRTLwYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGS 399
Cdd:cd18564 171 ARRF-SRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVA 249
|
170 180 190
....*....|....*....|....*....|
gi 749181994 400 VVSAIILWKGAGEVLNGTFTVGMLVAYLSY 429
Cdd:cd18564 250 VGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
510-707 |
8.38e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ-IRRRIGTVlQEDHLFRG- 587
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYV-PEDRKGEGl 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 ----SIADNIIFFSEDR-------NHERMIQCARlALIDS-DI----MTMPMGY-----QtligetggglsggqkQRILL 646
Cdd:COG1129 342 vldlSIRENITLASLDRlsrggllDRRRERALAE-EYIKRlRIktpsPEQPVGNlsggnQ---------------QKVVL 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 647 ARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAaegKAVIVISSElPELLGLSDRILVMREG 470
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
513-681 |
9.08e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 68.58 E-value: 9.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHP--DYYQIRRRIGTVLQEDHLFRGSIA 590
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPkvDERLIRQEAGMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 -DNIIFFSedrnhermIQCARLALIDSDIMTMPM----GYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSH 665
Cdd:PRK09493 95 lENVMFGP--------LRVRGASKEEAEKQARELlakvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170
....*....|....*.
gi 749181994 666 LDVESEIQISQTLRQL 681
Cdd:PRK09493 167 LDPELRHEVLKVMQDL 182
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
519-720 |
1.05e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 519 SLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH--PDyyqiRRRIGTVLQEDHLFRG-SIADNI-- 593
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtpPS----RRPVSMLFQENNLFSHlTVAQNIgl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 594 -IFFSEDRNHERMIQCARLAlidsdimtMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD--VES 670
Cdd:PRK10771 95 gLNPGLKLNAAQREKLHAIA--------RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 671 EI--QISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG--YFTDLTHQYRNGS 720
Cdd:PRK10771 167 EMltLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGriAWDGPTDELLSGK 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
511-688 |
1.06e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRR-IGTVlQEDHLFRG-- 587
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYI-PEDRLGRGlv 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 ---SIADNIIFFSEDR---------NHERMIQCARlALIDS-DIMT----MPMGY-----QtligetggglsggqkQRIL 645
Cdd:COG3845 349 pdmSVAENLILGRYRRppfsrggflDRKAIRAFAE-ELIEEfDVRTpgpdTPARSlsggnQ---------------QKVI 412
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 646 LARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLI 688
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdagAAVLLI 458
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
511-707 |
1.15e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 67.55 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGihlpnegtirtfgiphtHPDYYQIRRRIgtvlqedhLFRGsia 590
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-----------------HPKYEVTEGEI--------LFKG--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIFFSEDrnhERmiqcARLALIdsdimtmpMGYQ-----------TLIGETGGGLSGGQKQRILLARALYKKPGFLLL 659
Cdd:cd03217 64 EDITDLPPE---ER----ARLGIF--------LAFQyppeipgvknaDFLRYVNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 660 DEATSHLDVESEIQISQTLRQLKVP---VLLIAHRPETIA--SADRVLYLTDG 707
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEgksVLIITHYQRLLDyiKPDRVHVLYDG 181
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
514-707 |
1.16e-12 |
|
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: 68.23 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI----RRRIGTVLQEDHLFRGSI 589
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 A-DNIIFFSEDRNHERMIQCARLAL--------IDSDIMTMPMGYQtligetggglsggqkQRILLARALYKKPGFLLLD 660
Cdd:COG4181 107 AlENVMLPLELAGRRDARARARALLervglghrLDHYPAQLSGGEQ---------------QRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 749181994 661 EATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELNrergTTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
513-707 |
1.17e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ-IRRRIGTVLQE-DHLFRGSIA 590
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgIRKLVGIVFQNpETQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIFFSEDRNHERMIQCARLAlidsDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVES 670
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRV----DRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 749181994 671 EIQISQTLRQLK---VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13644 172 GIAVLERIKKLHekgKTIVYITHNLEELHDADRIIVMDRG 211
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
517-716 |
1.38e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 69.35 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 517 GVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG---IPHTHPDYYQIRRRIGTVLQeDHLF----RGSI 589
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGkdlLGMKDDEWRAVRSDIQMIFQ-DPLAslnpRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNI-----IFFSE-------DRNHERMiqcARLALIDSDIMTMPMGYQTligetggglsgGQKQRILLARALYKKPGFL 657
Cdd:PRK15079 118 GEIIaeplrTYHPKlsrqevkDRVKAMM---LKVGLLPNLINRYPHEFSG-----------GQCQRIGIARALILEPKLI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVL--YL--------TDGYFTDLTHQY 716
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQremgLSLIFIAHDLAVVKHiSDRVLvmYLghavelgtYDEVYHNPLHPY 257
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
515-707 |
1.48e-12 |
|
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: 70.48 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIhLPNEGTIRTFGIP---HTHPDYYQIRRRIGTVLQEDhlF-----R 586
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDldgLSRRALRPLRRRMQVVFQDP--FgslspR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 GSIADnIIffSE------------DRnHERMIQcarlAL----IDSDIMT-MPM----GyqtligetggglsggQKQRIL 645
Cdd:COG4172 379 MTVGQ-II--AEglrvhgpglsaaER-RARVAE----ALeevgLDPAARHrYPHefsgG---------------QRQRIA 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 646 LARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAH-----RpetiASADRVLYLTDG 707
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqrehGLAYLFISHdlavvR----ALAHRVMVMKDG 502
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
513-691 |
1.49e-12 |
|
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: 67.70 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRR-IGTVLQEDHLFRG-SIA 590
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFPSlTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNII---FFSEDRNHERmiqcARLAlidsDIMTM-PM-------------GYQtligetggglsggqkQRIL-LARALYK 652
Cdd:COG0410 97 ENLLlgaYARRDRAEVR----ADLE----RVYELfPRlkerrrqragtlsGGE---------------QQMLaIGRALMS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 653 KPGFLLLDEATSHLD---VEseiQISQTLRQLK---VPVLL----------IAHR 691
Cdd:COG0410 154 RPKLLLLDEPSLGLApliVE---EIFEIIRRLNregVTILLveqnarfaleIADR 205
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
500-708 |
1.85e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 67.73 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 500 LTHIAFSHkGSNKpILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI----RTFGIpHTHPDYYQI---R 572
Cdd:PRK11124 5 LNGINCFY-GAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagNHFDF-SKTPSDKAIrelR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 573 RRIGTVLQEDHLF-RGSIADNII-------FFSEDRNHERMIQ-CARLALID-SDimTMPMgyqtligetggGLSGGQKQ 642
Cdd:PRK11124 82 RNVGMVFQQYNLWpHLTVQQNLIeapcrvlGLSKDQALARAEKlLERLRLKPyAD--RFPL-----------HLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 643 RILLARALYKKPGFLLLDEATSHLDVESEIQ---ISQTLRQLKVPVLLIAHRPET---IASadRVLYLTDGY 708
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQivsIIRELAETGITQVIVTHEVEVarkTAS--RVVYMENGH 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
484-667 |
2.94e-12 |
|
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: 70.36 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 484 SIFQERVTEDTDLPLTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGtirtfgipH 563
Cdd:TIGR00957 623 SIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--------H 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 564 THpdyyqIRRRIGTVLQEDHLFRGSIADNIIF---FSEDRNHERMIQCARLAlidsDIMTMPMGYQTLIGETGGGLSGGQ 640
Cdd:TIGR00957 695 VH-----MKGSVAYVPQQAWIQNDSLRENILFgkaLNEKYYQQVLEACALLP----DLEILPSGDRTEIGEKGVNLSGGQ 765
|
170 180
....*....|....*....|....*..
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLD 667
Cdd:TIGR00957 766 KQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
515-707 |
3.39e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 67.55 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG---IPHT-HPDYYQIRRRIGTVLQ--EDHLFRGS 588
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhiTPETgNKNLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIF------FSEDRNHERMIQCARLALIDSDIMTmpmgyqtligETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:PRK13641 103 VLKDVEFgpknfgFSEDEAKEKALKWLKKVGLSEDLIS----------KSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 663 TSHLDVESEIQISQTLRQLKVP---VLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEyADDVLVLEHG 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
498-707 |
3.61e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.59 E-value: 3.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYYQIRRRIG 576
Cdd:COG1137 4 LEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQEDHLFRG-SIADNIIFFSEDRN---HERMIQCARL-------ALIDSDIMTMPMGyqtligetggglsggQKQRIL 645
Cdd:COG1137 82 YLPQEASIFRKlTVEDNILAVLELRKlskKEREERLEELleefgitHLRKSKAYSLSGG---------------ERRRVE 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 646 LARALYKKPGFLLLDEATSHLD---VEsEIQ-ISQTLRQLKVPVLLIAH--RpETIASADRVLYLTDG 707
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDpiaVA-DIQkIIRHLKERGIGVLITDHnvR-ETLGICDRAYIISEG 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
511-707 |
3.69e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.83 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDyyqiRRRIGTVLQEdhlfRG--- 587
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEE----RGlyp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 --SIADNIIFF------SEDRNHERMIQ-CARLAL---IDSDIMTMPMGYQtligetggglsggqkQRILLARALYKKPG 655
Cdd:COG4152 85 kmKVGEQLVYLarlkglSKAEAKRRADEwLERLGLgdrANKKVEELSKGNQ---------------QKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 656 FLLLDEATSHLD-VESEIqISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG4152 150 LLILDEPFSGLDpVNVEL-LKDVIRELAakgTTVIFSSHQMELVEElCDRIVIINKG 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
515-707 |
4.50e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.02 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG--IPHTHPDYYQIRRRIGTVLQ--EDHLFRGSIA 590
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQnpDDQLFAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIF------FSEDRNHERMIQCarLALIDSDimtmpmGYQTligETGGGLSGGQKQRILLARALYKKPGFLLLDEATS 664
Cdd:PRK13639 98 EDVAFgplnlgLSKEEVEKRVKEA--LKAVGME------GFEN---KPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 665 HLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNkegITIIISTHDVDLVPVyADKVYVMSDG 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
498-682 |
4.58e-12 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 66.39 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGSnkPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYYQIRRRIG 576
Cdd:TIGR03410 1 LEVSNLNVYYGQS--HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlPPHERARAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQEDHLF-RGSIADNII--FFSEDRNHERmiqcarlalIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKK 653
Cdd:TIGR03410 79 YVPQGREIFpRLTVEENLLtgLAALPRRSRK---------IPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTR 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 749181994 654 PGFLLLDEATshldvesE-IQ------ISQTLRQLK 682
Cdd:TIGR03410 150 PKLLLLDEPT-------EgIQpsiikdIGRVIRRLR 178
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
243-440 |
6.00e-12 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 67.18 E-value: 6.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARF-DAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMr 321
Cdd:cd18778 78 DLYDKLQRLSLRYFDDRQTGDLMSRViNDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALG- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 322 TLWYpSLRqsAEDAWDAGARESG----YFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLT 397
Cdd:cd18778 157 AWLY-SKK--VRPRYRKVREALGelnaLLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFL 233
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 749181994 398 GSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSL 440
Cdd:cd18778 234 TSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSL 276
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
512-707 |
6.50e-12 |
|
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: 65.63 E-value: 6.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrtfgiphthpdyyQIRRRIGTVLQEDHLFRGSIA- 590
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV-------------TVRGRVSSLLGLGGGFNPELTg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 -DNIIF------FSEDRNHERMIQCARLALIDsDIMTMPMG-YQTligetggglsgGQKQRILLARALYKKPGFLLLDEA 662
Cdd:cd03220 102 rENIYLngrllgLSRKEIDEKIDEIIEFSELG-DFIDLPVKtYSS-----------GMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 663 TSHLDVESEIQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLkqgKTVILVSHDPSSIKRlCDRALVLEKG 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
513-707 |
6.92e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.69 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT----HPDYYQIRRRIGTVLQ--EDHLFR 586
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 GSIADNIIFFSED--RNHERMIQCAR--LALIDSDimtmpmgyQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:PRK13649 101 ETVLKDVAFGPQNfgVSQEEAEALARekLALVGIS--------ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 663 TSHLDVESE---IQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13649 173 TAGLDPKGRkelMTLFKKLHQSGMTIVLVTHLMDDVANyADFVYVLEKG 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
498-710 |
9.33e-12 |
|
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: 64.91 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKgsNKPILRGVSLTLHTGeVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT-HPDYyqIRRRIG 576
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLkQPQK--LRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQE----------DHLFRGSIADNIiffsEDRNHERMIQCArLALID-SDIMTMPMGyqtligetggGLSGGQKQRIL 645
Cdd:cd03264 76 YLPQEfgvypnftvrEFLDYIAWLKGI----PSKEVKARVDEV-LELVNlGDRAKKKIG----------SLSGGMRRRVG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 646 LARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL---KVpVLLIAHRPETIAS-ADRVLYLTDGYFT 710
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgedRI-VILSTHIVEDVESlCNQVAVLNKGKLV 208
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
243-444 |
9.39e-12 |
|
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: 66.41 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARF--DAiDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIA-VLAAVIYGV 319
Cdd:cd18572 74 DLFRSLLRQDIAFFDATKTGELTSRLtsDC-QKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAfITVPVIALI 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 320 MRtlWYPSL-RQSAEDAWDAGARESGYFLETLSGILSLRINGvTTHREA--------AWLNLNVtrrntqlRQSRLLMYY 390
Cdd:cd18572 153 TK--VYGRYyRKLSKEIQDALAEANQVAEEALSNIRTVRSFA-TEEREArryeraldKALKLSV-------RQALAYAGY 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 391 DIAHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKF 444
Cdd:cd18572 223 VAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVF 276
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
512-707 |
1.12e-11 |
|
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: 67.91 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGI--HLPNEGTI----------RTFGIPH---------------- 563
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcGYVERPSkvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 564 -------THPDYYQIRRRIGTVLQEDHLFRG--SIADNIIFFSEDRNHERMIQCAR-LALIDsdiMTMpMGYQtlIGETG 633
Cdd:TIGR03269 93 evdfwnlSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIGYEGKEAVGRaVDLIE---MVQ-LSHR--ITHIA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 634 GGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkasGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
499-560 |
1.28e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.28e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 499 TLTHIAFSHKGSNKP---ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG 560
Cdd:COG1134 23 SLKELLLRRRRTRREefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG 87
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
489-726 |
1.38e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.76 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 489 RVTEDT--DLPLTLTHIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPN---EGTIRTFGIPH 563
Cdd:TIGR00955 13 RVAQDGswKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 564 THPdyyQIRRRIGTVlQEDHLFRGSIA--DNIIFFSEDRNHERMIQCARLALIDsDIMTMpMGY----QTLIGETGGGLS 637
Cdd:TIGR00955 93 DAK---EMRAISAYV-QQDDLFIPTLTvrEHLMFQAHLRMPRRVTKKEKRERVD-EVLQA-LGLrkcaNTRIGVPGRVKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 638 GG--QKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIaHRP--ETIASADRVLYLTDG-- 707
Cdd:TIGR00955 167 LSggERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaqkgKTIICTI-HQPssELFELFDKIILMAEGrv 245
|
250 260 270
....*....|....*....|....*....|...
gi 749181994 708 -----------YFTDLTHQ---YRNGSEYLVRM 726
Cdd:TIGR00955 246 aylgspdqavpFFSDLGHPcpeNYNPADFYVQV 278
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
515-707 |
1.51e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 65.64 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP--HTHPDYYQIRRRIGTVLQE-DH-LFRGSIA 590
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPidYSRKGLMKLRESVGMVFQDpDNqLFSASVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIF------FSEDRNHERMiqcaRLALIDSdimtmpmGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATS 664
Cdd:PRK13636 102 QDVSFgavnlkLPEDEVRKRV----DNALKRT-------GIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 749181994 665 HLDVE--SEIQ--ISQTLRQLKVPVLLIAHRPETIA-SADRVLYLTDG 707
Cdd:PRK13636 171 GLDPMgvSEIMklLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEG 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
515-707 |
1.66e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPH---THPDYYQIrrRIGTVLQE---------- 581
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnklDHKLAAQL--GIGIIYQElsvideltvl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 ------DHLFRGSIADNIIFFSEDRnhermiqcarlalIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPG 655
Cdd:PRK09700 99 enlyigRHLTKKVCGVNIIDWREMR-------------VRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 656 FLLLDEATSHL---DVESEIQISQTLRQLKVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:PRK09700 166 VIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| Peptidase_C39G |
cd02423 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
14-134 |
1.91e-11 |
|
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: 61.90 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 14 LIRQTESAECGLACLAMMACWHG-LQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCI--- 89
Cdd:cd02423 3 VVRQSYDFSCGPAALATLLRYYGgINITEQEVLKLMLIRSEGFSMLDLKRYAEALGLKANGYRLNLDKLNALQIPVIvlv 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 749181994 90 LHWNMNHFVVLHKVRRSRLVIHDPDKGKITLSLQDAGKHFTGVAL 134
Cdd:cd02423 83 NNGGYGHFVVIKGIDGDRVLVGDPALGNISMSREEFERIWTGNAL 127
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
508-707 |
1.96e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.49 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 508 KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYYQIRRRIGTVLQE-DHLF 585
Cdd:PRK13633 19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeENLWDIRNKAGMVFQNpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RGSIADNIIFF---------SEDRnhERMIQCARlalidsdimtmPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGF 656
Cdd:PRK13633 99 VATIVEEDVAFgpenlgippEEIR--ERVDESLK-----------KVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 657 LLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNkkygITIILITHYMEEAVEADRIIVMDSG 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
512-703 |
2.64e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.82 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHL--PNEGTIRtfgIPHTHPDyyqirrRIGTVLqeDHLFR-GS 588
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD---VPDNQFG------REASLI--DAIGRkGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIiffsedrnheRMIQCARLalidSDIMTMPMGYQTLigetggglSGGQKQRILLARALYKKPGFLLLDEATSHLDV 668
Cdd:COG2401 112 FKDAV----------ELLNAVGL----SDAVLWLRRFKEL--------STGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 749181994 669 ESEIQISQTL----RQLKVPVLLIAHRPETIA--SADRVLY 703
Cdd:COG2401 170 QTAKRVARNLqklaRRAGITLVVATHHYDVIDdlQPDLLIF 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
515-707 |
2.67e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.11 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtFGIPHTHPDYY------------------------- 569
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE-WIFKDEKNKKKtkekekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 570 QIRRRIGTVLQ--EDHLFRGSIADNIIF----FSEDRNHERMIQCARLALIDSDIMTMPMGYQTLigetggglSGGQKQR 643
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFgpvsMGVSKEEAKKRAAKYIELVGLDESYLQRSPFEL--------SGGQKRR 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 644 ILLARALYKKPGFLLLDEATSHLD---VESEIQISQTLRQLKVPVLLIAHRPETI-ASADRVLYLTDG 707
Cdd:PRK13651 174 VALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKDG 241
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
514-707 |
3.79e-11 |
|
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: 64.49 E-value: 3.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIhLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGSIADNI 593
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 594 IFFsEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQ 673
Cdd:cd03289 98 DPY-GKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 749181994 674 ISQTLRQ--LKVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:cd03289 177 IRKTLKQafADCTVILSEHRIEAMLECQRFLVIEEN 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
505-727 |
4.37e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 64.87 E-value: 4.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNK-PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGI---PHTHP-------------D 567
Cdd:PRK13631 31 FDEKQENElVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigDKKNNhelitnpyskkikN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 568 YYQIRRRIGTVLQ--EDHLFRGSIADNIIF------FSEDRNHERM-IQCARLALIDSDIMTMPMGyqtligetgggLSG 638
Cdd:PRK13631 111 FKELRRRVSMVFQfpEYQLFKDTIEKDIMFgpvalgVKKSEAKKLAkFYLNKMGLDDSYLERSPFG-----------LSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 639 GQKQRILLARALYKKPGFLLLDEATSHLDVESE---IQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDGYFtdLTH 714
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEhemMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKI--LKT 257
|
250
....*....|...
gi 749181994 715 qyrnGSEYLVRMD 727
Cdd:PRK13631 258 ----GTPYEIFTD 266
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
498-709 |
5.27e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.37 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT-HPDYYQIRRRIG 576
Cdd:PRK10895 4 LTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISlLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 577 TVLQEDHLFRG-SIADNIIFF-----------SEDRNHERMIQCARLALIDSdimtmpMGyQTLigetggglSGGQKQRI 644
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMAVlqirddlsaeqREDRANELMEEFHIEHLRDS------MG-QSL--------SGGERRRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 645 LLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK---VPVLLIAHR-PETIASADRVLYLTDGYF 709
Cdd:PRK10895 147 EIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRdsgLGVLITDHNvRETLAVCERAYIVSQGHL 215
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
511-681 |
6.69e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP--HTHPDYYQIRRRIGTVLQ--EDHLFR 586
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLLALRQQVATVFQdpEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 GSIADNIIF------FSEDRNHERMIQCarLALIDSdimtmpmgyQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLD 660
Cdd:PRK13638 93 TDIDSDIAFslrnlgVPEAEITRRVDEA--LTLVDA---------QHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180
....*....|....*....|.
gi 749181994 661 EATSHLDVESEIQISQTLRQL 681
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRI 182
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
512-707 |
8.18e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 8.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTfgiphthpdyyqiRRRIGTVLQEDHLFRGSIAD 591
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-------------ERSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIFFSEDRNhERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESE 671
Cdd:PTZ00243 740 NILFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 749181994 672 IQISQT--LRQL--KVPVlLIAHRPETIASADRVLYLTDG 707
Cdd:PTZ00243 819 ERVVEEcfLGALagKTRV-LATHQVHVVPRADYVVALGDG 857
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
518-708 |
9.18e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.60 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT----HPDYYQIRRRIGTVLQ--EDHLFRGSIAD 591
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskQKEIKPVRKKVGVVFQfpESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIF----FSEDRNHERMIQCARLALIDSDimtmpmgyQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD 667
Cdd:PRK13643 105 DVAFgpqnFGIPKEKAEKIAAEKLEMVGLA--------DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 668 VESEIQIS---QTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDGY 708
Cdd:PRK13643 177 PKARIEMMqlfESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGH 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
511-671 |
9.87e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIG------TVLqedhl 584
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGhrnamkPAL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 frgSIADNIIFFSEDRN-HERMIQCArLALID-SDIMTMPMGYqtligetgggLSGGQKQRILLARAL-YKKPgFLLLDE 661
Cdd:PRK13539 89 ---TVAENLEFWAAFLGgEELDIAAA-LEAVGlAPLAHLPFGY----------LSAGQKRRVALARLLvSNRP-IWILDE 153
|
170
....*....|
gi 749181994 662 ATSHLDVESE 671
Cdd:PRK13539 154 PTAALDAAAV 163
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
515-702 |
9.88e-11 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 62.75 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRR-IGTVLQEDHLFRG-SIADN 592
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLgIARTFQNPRLFPElTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 II----------FFS-----------EDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRILLA 647
Cdd:COG0411 100 VLvaaharlgrgLLAallrlprarreEREARERAEELLERvglaDRADEPAGNLSYG---------------QQRRLEIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 648 RALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVL 702
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdergITILLIEHDMDLVMGlADRIV 224
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
19-131 |
1.11e-10 |
|
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: 59.57 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 19 ESAECGLACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCILHWNMNHFV 98
Cdd:cd02417 3 TKPDSGLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPLPALAWDDDGGHF 82
|
90 100 110
....*....|....*....|....*....|....
gi 749181994 99 VLHKVRRSRLVIHDPDKGK-ITLSLQDAGKHFTG 131
Cdd:cd02417 83 ILAKLDGQKYLIQDPISQRpEVLSREEFEARWSG 116
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
512-681 |
1.15e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 63.29 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG--IPHTHPdyyQIRRRIGTVLQEDHL---Fr 586
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepVPSRAR---HARQRVGVVPQFDNLdpdF- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 gSIADNIIFF------SEDRNHERM---IQCARL-ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGF 656
Cdd:PRK13537 96 -TVRENLLVFgryfglSAAAARALVpplLEFAKLeNKADAKVGELSGG---------------MKRRLTLARALVNDPDV 159
|
170 180
....*....|....*....|....*
gi 749181994 657 LLLDEATSHLDVESEIQISQTLRQL 681
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSL 184
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
515-704 |
1.17e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.45 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDY---------YQI-----------RRR 574
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqkllrqkIQIvfqnpygslnpRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 575 IGTVLQEdhlfrgSIADNIIFFSEDRN---HERMiqcARLALidsdimtMPMGYQtligETGGGLSGGQKQRILLARALY 651
Cdd:PRK11308 111 VGQILEE------PLLINTSLSAAERRekaLAMM---AKVGL-------RPEHYD----RYPHMFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 652 KKPGFLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHR---PETIASADRVLYL 704
Cdd:PRK11308 171 LDPDVVVADEPVSALDVSVQAQVLNLMmdlqQELGLSYVFISHDlsvVEHIADEVMVMYL 230
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
271-586 |
1.44e-10 |
|
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: 64.43 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 271 IDTIQQALTtQVLEGILDVLLVVTALCMMLLYSPEMTLIAV----LAAVIYGVMRTLWYPSLRQSAEdAWDagaRESGYF 346
Cdd:COG4615 115 VRTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTLvllgLGVAGYRLLVRRARRHLRRARE-AED---RLFKHF 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 347 LETLSGILSLRINgvtTHREAAWLNLNVTRRNTQLRQSRL--LMYYDIAHTLT--------GSVVSAIILW-KGAGEVLn 415
Cdd:COG4615 190 RALLEGFKELKLN---RRRRRAFFDEDLQPTAERYRDLRIraDTIFALANNWGnllffaliGLILFLLPALgWADPAVL- 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 416 GTFTVGMLvaYLSyqmrfsSSISSLTDKFFAWRMLDVYNERLADIVLtptEGNQQQTAQENNSTSTTPSIFQErvtedtd 495
Cdd:COG4615 266 SGFVLVLL--FLR------GPLSQLVGALPTLSRANVALRKIEELEL---ALAAAEPAAADAAAPPAPADFQT------- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 496 lpLTLTHIAFSHKGSNK-------PIlrgvSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDY 568
Cdd:COG4615 328 --LELRGVTYRYPGEDGdegftlgPI----DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR 401
|
330
....*....|....*...
gi 749181994 569 YQIRRRIGTVLQEDHLFR 586
Cdd:COG4615 402 EAYRQLFSAVFSDFHLFD 419
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
244-442 |
1.70e-10 |
|
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: 62.50 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 244 VFHHLVRLPLAWFDARSRGSVNARFDAiDT--IQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAA------- 314
Cdd:cd18575 75 VFAHLLRLSPSFFETTRTGEVLSRLTT-DTtlIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIplvvlpi 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 315 VIYG-VMRTLwypslrqsAEDAWDAGARESGYFLETLSGILSLRING-----VTTHREAAWLNLNVTRRNTQLRQsrllm 388
Cdd:cd18575 154 ILFGrRVRRL--------SRASQDRLADLSAFAEETLSAIKTVQAFTredaeRQRFATAVEAAFAAALRRIRARA----- 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 389 yydiahTLTGSVVSAI------ILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTD 442
Cdd:cd18575 221 ------LLTALVIFLVfgaivfVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSE 274
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
515-701 |
1.90e-10 |
|
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: 61.23 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHpDYYQIRRRIGTVLQEDHLFRGSIA-DNI 593
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 594 IFFSEDRNHERMIQCARLA-LIDSdimtmpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEI 672
Cdd:cd03265 95 YIHARLYGVPGAERRERIDeLLDF------VGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
|
170 180 190
....*....|....*....|....*....|....
gi 749181994 673 QISQTLRQLK----VPVLLIAH-RPETIASADRV 701
Cdd:cd03265 169 HVWEYIEKLKeefgMTILLTTHyMEEAEQLCDRV 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
514-707 |
1.94e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ---IR-RRIGTVLQE-------- 581
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFVFQSfmliptln 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 -------DHLFRGSiadniiffSEDRNHERMIQCARLALIDSDIMTMPmgyqtligetgGGLSGGQKQRILLARALYKKP 654
Cdd:PRK10584 105 alenvelPALLRGE--------SSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
239-444 |
2.17e-10 |
|
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: 62.44 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 239 QWTA---------RVFHHLVRLPLAWFDARSRGSVNARFdaIDTIQQA---LTTQVLEGILDVLLVVTALCMMLLYSPEM 306
Cdd:cd18554 71 QWIAnkilydirkDLFDHLQKLSLRYYANNRSGEIISRV--INDVEQTkdfITTGLMNIWLDMITIIIAICIMLVLNPKL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 307 TLIAVLAAVIYGVMRTLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRL 386
Cdd:cd18554 149 TFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRW 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 387 LMY-YDIAHTLTgSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKF 444
Cdd:cd18554 229 NAKtFSAVNTIT-DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSF 286
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
515-707 |
2.69e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.41 E-value: 2.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGI--HLPNEGTIRTFGIPHThpdYYQIR--RRIGTVL--QEDHLFRG- 587
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQ---ASNIRdtERAGIAIihQELALVKEl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIFFSEDRNHERM------IQCARL---ALIDSD----IMTMPMGYQTLIGetggglsggqkqrilLARALYKKP 654
Cdd:PRK13549 98 SVLENIFLGNEITPGGIMdydamyLRAQKLlaqLKLDINpatpVGNLGLGQQQLVE---------------IAKALNKQA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 655 GFLLLDEATSHLdVESEIQ----ISQTLRQLKVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:PRK13549 163 RLLILDEPTASL-TESETAvlldIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDG 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
519-692 |
2.93e-10 |
|
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: 63.61 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 519 SLTLHTGEVVAITGKSGCGKSTLVKlILGIHLPNEGTIRTfgIPHthpdyyqiRRRIGTVLQEDHLFRGSIADNIIF--- 595
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLT--KPA--------KGKLFYVPQRPYMTLGTLRDQIIYpds 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 596 ---FSE----DRNHERMIQCARLalidSDIMTMPMGYQTlIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDV 668
Cdd:TIGR00954 541 sedMKRrglsDKDLEQILDNVQL----THILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....
gi 749181994 669 ESEIQISQTLRQLKVPVLLIAHRP 692
Cdd:TIGR00954 616 DVEGYMYRLCREFGITLFSVSHRK 639
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
518-674 |
2.93e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 61.39 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQED------HLFRGSIAD 591
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDPntslnpRLNIGQILE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 -----NIIFFSEDRNhERMIQCARLALIDSDIMTMPMgyQTLigetggglSGGQKQRILLARALYKKPGFLLLDEATSHL 666
Cdd:COG4167 112 eplrlNTDLTAEERE-ERIFATLRLVGLLPEHANFYP--HML--------SSGQKQRVALARALILQPKIIIADEALAAL 180
|
....*...
gi 749181994 667 DVESEIQI 674
Cdd:COG4167 181 DMSVRSQI 188
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
513-708 |
3.54e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI-----RTFGIPHThpdyyqiRRRIGTVLQE----DH 583
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLfigekRMNDVPPA-------ERGVGMVFQSyalyPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 LfrgSIADNIIF------FSEDRNHERMIQCARL----ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKK 653
Cdd:PRK11000 90 L---SVAENMSFglklagAKKEEINQRVNQVAEVlqlaHLLDRKPKALSGG---------------QRQRVAIGRTLVAE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 654 PGFLLLDEATSHLD----VESEIQISQTLRQLKVPVLLIAH-RPETIASADRVLYLTDGY 708
Cdd:PRK11000 152 PSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGR 211
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
179-425 |
3.70e-10 |
|
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: 61.69 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 179 ILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLVRLPLAWFDA 258
Cdd:cd18571 16 LLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLMRLPISFFDT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 259 RSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSLRQSAEDAWDA 338
Cdd:cd18571 96 KMTGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILWILLFLKKRKKLDYKRFDL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 339 GARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVVSAIILWKGAGEVLNGTF 418
Cdd:cd18571 176 SSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKNILITFLAAKLVIDGEI 255
|
....*..
gi 749181994 419 TVGMLVA 425
Cdd:cd18571 256 TLGMMLA 262
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
511-682 |
4.45e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.80 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIgTVLQEDHLFRGSIA 590
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL-ALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 -DNIIFF--SEDRNHermiqCARLALIDSDIMTMPM---GYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATS 664
Cdd:PRK11231 93 vRELVAYgrSPWLSL-----WGRLSAEDNARVNQAMeqtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170
....*....|....*...
gi 749181994 665 HLDVESEIQISQTLRQLK 682
Cdd:PRK11231 168 YLDINHQVELMRLMRELN 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
513-680 |
6.17e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 59.29 E-value: 6.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR--------TFGIPHTHPDYYQIRRRIGTVLqedhl 584
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtplaeQRDEPHENILYLGHLPGLKPEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 frgSIADNIIFFSED-RNHERMIQCArLALID-SDIMTMPMGYqtligetgggLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:TIGR01189 89 ---SALENLHFWAAIhGGAQRTIEDA-LAAVGlTGFEDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEP 154
|
170
....*....|....*...
gi 749181994 663 TSHLDVESEIQISQTLRQ 680
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRA 172
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
514-707 |
8.94e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.23 E-value: 8.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILG----IHLPN----EGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLF 585
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RGSIADNIIFFS---------EDRNHERMIQCARLALIDSDimtmpmgyqTLIGETGGGLSGGQKQRILLARALYK---- 652
Cdd:PRK13547 96 FAFSAREIVLLGrypharragALTHRDGEIAWQALALAGAT---------ALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 653 -----KPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLardwNLGVLAIVHDPNLAARhADRIAMLADG 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
510-667 |
9.93e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 9.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTfgiphthpdyyqIRRRIGTVLQEDHLFRGSI 589
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIF---FSEDRnHERMIQCARLaliDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHL 666
Cdd:PLN03130 696 RDNILFgspFDPER-YERAIDVTAL---QHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
.
gi 749181994 667 D 667
Cdd:PLN03130 772 D 772
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
510-674 |
1.03e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGihlpnegtirtfGIPHTHPDYYQIRRRIGTVLQEDHLFRGSI 589
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG------------ELSHAETSSVVIRGSVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFFSeDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVE 669
Cdd:PLN03232 696 RENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
....*
gi 749181994 670 SEIQI 674
Cdd:PLN03232 775 VAHQV 779
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
170-444 |
1.10e-09 |
|
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: 60.19 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 170 IITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHLV 249
Cdd:cd18540 7 LIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 250 RLPLAWFDARSRGSVNARFDAiDTiqQALTTQVLEGILDVL----LVVTALCMMLLYSPEMTLIaVLAAVIYGVMRTLWY 325
Cdd:cd18540 87 TLSFSYFDKTPVGWIMARVTS-DT--QRLGEIISWGLVDLVwgitYMIGILIVMLILNWKLALI-VLAVVPVLAVVSIYF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 326 PS--LRQSAEdawdagARE-----SGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRL-LMYYDIAHTLt 397
Cdd:cd18540 163 QKkiLKAYRK------VRKinsriTGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLsALFLPIVLFL- 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 749181994 398 GSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKF 444
Cdd:cd18540 236 GSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVL 282
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
524-707 |
1.24e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 524 TGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFRGsiadniiffsedrnhe 603
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 604 rmiqcarlalidsdimtmpmgyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQIS-------- 675
Cdd:smart00382 65 ------------------------------------LRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrll 108
|
170 180 190
....*....|....*....|....*....|....*....
gi 749181994 676 -QTLRQLKVPVLLIAHRPETIASA------DRVLYLTDG 707
Cdd:smart00382 109 lLLKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLI 147
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
243-441 |
1.38e-09 |
|
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: 59.84 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFdAIDT--IQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIA-------VLA 313
Cdd:cd18573 79 RLFKSILRQDAAFFDKNKTGELVSRL-SSDTsvVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMllvvppiAVG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 314 AVIYG-VMRtlwypSLRQSAEDAwdagaresgyfLETLSGILSLRINGVTT-------HREAAWLNLNVTR-RNTQLRQS 384
Cdd:cd18573 158 AVFYGrYVR-----KLSKQVQDA-----------LADATKVAEERLSNIRTvrafaaeRKEVERYAKKVDEvFDLAKKEA 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 385 RLLMYYDIAHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18573 222 LASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLS 278
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
514-711 |
1.96e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP---HTHPDYYQIR-RRIGTVLQEDHLFRGSI 589
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPmskLSSAAKAELRnQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 AdniiffSEDRNHERMIQCARLALIDSDIMTM--PMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD 667
Cdd:PRK11629 104 A------LENVAMPLLIGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 749181994 668 VESEIQISQTLRQLKV----PVLLIAHRPETIASADRVLYLTDGYFTD 711
Cdd:PRK11629 178 ARNADSIFQLLGELNRlqgtAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
515-709 |
2.11e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQ-IRRRIGTVLQEDHLF-RGSIADN 592
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHLVpEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 I----------IFFSEDRNHERMIQCARLAL-IDSDimtMPMGYQTLigetggglsgGQKQRILLARALYKKPGFLLLDE 661
Cdd:PRK11288 100 LylgqlphkggIVNRRLLNYEAREQLEHLGVdIDPD---TPLKYLSI----------GQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 662 ATSHLDV-ESEI--QISQTLRQLKVPVLLIAHRPETI-ASADRVLYLTDGYF 709
Cdd:PRK11288 167 PTSSLSArEIEQlfRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRY 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
515-707 |
2.15e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHlPN---EGTIRTFGIPHTHPDYYQIRRR-IGTVLQEDHLFRG-SI 589
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFFSE------DRNHERMIQCARLAL----IDSDIMTMPMGYQTLigetggglsgGQKQRILLARALYKKPGFLLL 659
Cdd:TIGR02633 96 AENIFLGNEitlpggRMAYNAMYLRAKNLLrelqLDADNVTRPVGDYGG----------GQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 660 DEATSHLdVESEIQ----ISQTLRQLKVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:TIGR02633 166 DEPSSSL-TEKETEilldIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDG 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
514-722 |
2.29e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.77 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLI-----LGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQ-EDHLFRG 587
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNI--------IFFSEDRNHERM---IQCARLALIDSDIMTMPMGyqtligetggGLSGGQKQRILLARALYKKPGF 656
Cdd:PRK14247 98 SIFENValglklnrLVKSKKELQERVrwaLEKAQLWDEVKDRLDAPAG----------KLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 657 LLLDEATSHLDVESEIQISQTLRQLK--VPVLLIAHRPETIAS-ADRVLYLTDG----------YFT----DLTHQYRNG 719
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKkdMTIVLVTHFPQQAARiSDYVAFLYKGqivewgptreVFTnprhELTEKYVTG 247
|
...
gi 749181994 720 SEY 722
Cdd:PRK14247 248 RLY 250
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
518-715 |
5.30e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 5.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPhthpdyYQIRR-----RIGTVL-QEDHLFRG---- 587
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP------IDIRSprdaiRAGIMLcPEDRKAEGiipv 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 -SIADNI-I----FFS----------EDRNHERMIQcaRLAL----IDSDIMTMPMGYQtligetggglsggqkQRILLA 647
Cdd:PRK11288 346 hSVADNInIsarrHHLragclinnrwEAENADRFIR--SLNIktpsREQLIMNLSGGNQ---------------QKAILG 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 749181994 648 RALYKKPGFLLLDEATSHLDV--ESEI-QISQTLRQLKVPVLLIAHR-PETIASADRVLYLTDGYFT-DLTHQ 715
Cdd:PRK11288 409 RWLSEDMKVILLDEPTRGIDVgaKHEIyNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRIAgELARE 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
509-711 |
5.36e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 5.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTfgiphtHPDYyqirrRIGTVLQEDHL---- 584
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP------QPGI-----KVGYLPQEPQLdptk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 -FRGSIAD------------NIIF--FSE---------------------------DRNHERMIQCARLALIDSDIMTMP 622
Cdd:TIGR03719 84 tVRENVEEgvaeikdaldrfNEISakYAEpdadfdklaaeqaelqeiidaadawdlDSQLEIAMDALRCPPWDADVTKLS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 623 MGyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHrpetiasaDRvl 702
Cdd:TIGR03719 164 GG---------------ERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTH--------DR-- 218
|
....*....
gi 749181994 703 yltdgYFTD 711
Cdd:TIGR03719 219 -----YFLD 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
514-681 |
6.16e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.67 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG--IPHTHPDYYQI-----------RRRIGTVLQ 580
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtINLVRDKDGQLkvadknqlrllRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 581 EDHLFRG-SIADNI-------IFFSEDRNHERMIQ-CARLALIDSDIMTMPMgyqtligetggGLSGGQKQRILLARALY 651
Cdd:PRK10619 100 HFNLWSHmTVLENVmeapiqvLGLSKQEARERAVKyLAKVGIDERAQGKYPV-----------HLSGGQQQRVSIARALA 168
|
170 180 190
....*....|....*....|....*....|
gi 749181994 652 KKPGFLLLDEATSHLDVESEIQISQTLRQL 681
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQL 198
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
498-667 |
6.59e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.40 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHI--AFsHKGSN--KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYyQIR 572
Cdd:COG1101 2 LELKNLskTF-NPGTVneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEY-KRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 573 RRIGTVLQeDHL----FRGSIADNI-----------IFFSEDRNHERMIQcARLALID---SDIMTMPMGYqtligetgg 634
Cdd:COG1101 80 KYIGRVFQ-DPMmgtaPSMTIEENLalayrrgkrrgLRRGLTKKRRELFR-ELLATLGlglENRLDTKVGL--------- 148
|
170 180 190
....*....|....*....|....*....|...
gi 749181994 635 gLSGGQKQRILLARALYKKPGFLLLDEATSHLD 667
Cdd:COG1101 149 -LSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
169-425 |
7.31e-09 |
|
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: 57.61 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 169 RIITFALSLEILTLGSPLLNQLVIDEVLVAADRSLLTVVIVALLLLSLTQMLLSLACQWASITLSVNFNMQWTARVFHHL 248
Cdd:cd18586 6 EVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 249 VRLPLawfDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVMRTLWYPSL 328
Cdd:cd18586 86 LELPL---ESRPSGYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRAT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 329 RQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLL-MYYDIAHTLTgSVVSAIILW 407
Cdd:cd18586 163 RKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAgAISAIGKTLR-MALQSLILG 241
|
250
....*....|....*...
gi 749181994 408 KGAGEVLNGTFTVGMLVA 425
Cdd:cd18586 242 VGAYLVIDGELTIGALIA 259
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
510-710 |
8.12e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQ--EDHLFRG 587
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIF------FSEDRNHERMIQCARLalidsdimtmpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDE 661
Cdd:PRK13652 95 TVEQDIAFgpinlgLDEETVAHRVSSALHM-----------LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 662 ATSHLDVESEIQISQTLRQLKV----PVLLIAHRPETIAS-ADRVLYLTDGYFT 710
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEmADYIYVMDKGRIV 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
512-707 |
8.65e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILG-IHLPN-EGTIRTFGIPHTHpdyyQIRRRIGTVLQEDHLF-RGS 588
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNfTGTILANNRKPTK----QILKRTGFVTQDDILYpHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIFFSEDRNHERMIQCARLALIDSDIMTMPMGY--QTLIGETGGGLSGG-QKQRILLARALYKKPGFLLLDEATSH 665
Cdd:PLN03211 157 VRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKceNTIIGNSFIRGISGgERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 666 LDVESEIQISQTLRQLkvpvlliAHRPETIASA------------DRVLYLTDG 707
Cdd:PLN03211 237 LDATAAYRLVLTLGSL-------AQKGKTIVTSmhqpssrvyqmfDSVLVLSEG 283
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
518-707 |
1.12e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGipHTHPDYYQ-I-----RRRIGTVLQEDHLF-----R 586
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG--RVLFDAEKgIclppeKRRIGYVFQDARLFphykvR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 587 GsiadniiffsedrNHERMIQCARLALIDsDIMTMpMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHL 666
Cdd:PRK11144 95 G-------------NLRYGMAKSMVAQFD-KIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 667 DVESE---IQISQTL-RQLKVPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:PRK11144 160 DLPRKrelLPYLERLaREINIPILYVSHSlDEILRLADRVVVLEQG 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
514-680 |
1.46e-08 |
|
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: 55.58 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP--HTHPDYYQIRRRIG------TVLqedhlf 585
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPldFQRDSIARGLLYLGhapgikTTL------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 rgSIADNIIFFSEDRNHERMIQcarlALIDSDImtmpMGYQTLIgetGGGLSGGQKQRILLARALYKKPGFLLLDEATSH 665
Cdd:cd03231 89 --SVLENLRFWHADHSDEQVEE----ALARVGL----NGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|....*
gi 749181994 666 LDVESEIQISQTLRQ 680
Cdd:cd03231 156 LDKAGVARFAEAMAG 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
511-707 |
1.60e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.82 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG-----------IPHTHPDYYQIRRRIGTVL 579
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkinnhnaneaINHGFALVTEERRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 580 QEDHLFRGSIAdNIiffSEDRNHERMIQCARLA-----LIDSDIMTMPmGYQTLIGETGGGlsggQKQRILLARALYKKP 654
Cdd:PRK10982 340 YLDIGFNSLIS-NI---RNYKNKVGLLDNSRMKsdtqwVIDSMRVKTP-GHRTQIGSLSGG----NQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELakkdKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
515-707 |
1.64e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG-IPHTH-PDYyqiRRRIGTVL-QEDHL------- 584
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKRrKEF---ARRIGVVFgQRSQLwwdlpai 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 --FR--GSIADniifFSEDRNHERMIQCA-RLALidSDIMTMP-----MGyqtligetggglsggQKQRILLARALYKKP 654
Cdd:COG4586 115 dsFRllKAIYR----IPDAEYKKRLDELVeLLDL--GELLDTPvrqlsLG---------------QRMRCELAAALLHRP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYnrerGTTILLTSHDMDDIEAlCDRVIVIDHG 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
511-602 |
2.13e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.80 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGihlpnegtirtfgiphtHPDYyqirrrigTVLQEDHLFRG-SI 589
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-----------------HPAY--------KILEGDILFKGeSI 73
|
90
....*....|...
gi 749181994 590 ADniiFFSEDRNH 602
Cdd:CHL00131 74 LD---LEPEERAH 83
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
506-723 |
2.97e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 506 SHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtfgiphthpdyYQIRRRIGTVLQeDHlf 585
Cdd:PRK15064 326 TKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-----------WSENANIGYYAQ-DH-- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 rgsIADniifFSEDRN-HERMIQCARLAliDSDIMTMPMGYQTL-----IGETGGGLSGGQKQRILLARALYKKPGFLLL 659
Cdd:PRK15064 392 ---AYD----FENDLTlFDWMSQWRQEG--DDEQAVRGTLGRLLfsqddIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 660 DEATSHLDVESEIQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDGYFTDLTHQYrngSEYL 723
Cdd:PRK15064 463 DEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSlATRIIEITPDGVVDFSGTY---EEYL 524
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
505-708 |
3.56e-08 |
|
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: 54.19 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 505 FSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPN---EGTIRTFGIPhthpdyyqirrrigtVLQE 581
Cdd:cd03233 13 TGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP---------------YKEF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLFRGSIadniIFFSEDRNH------ERMIQCARLALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPG 655
Cdd:cd03233 78 AEKYPGEI----IYVSEEDVHfptltvRETLDFALRCKGNEFVRGISGG---------------ERKRVSIAEALVSRAS 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 749181994 656 FLLLDEATSHLDVESEIQISQTLRQ----LKVPVLLIAHRP--ETIASADRVLYLTDGY 708
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTmadvLKTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
503-707 |
3.68e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.79 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 503 IAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTfgiphthpDYYQIRRRIGTVLQ-- 580
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQC--------DKMLLRRRSRQVIEls 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 581 ---EDHLFRGSIADNIIFFSEDRNH--------ERMIQCARL--------ALIDS----DIMTMPMGyQTLIGETGGGLS 637
Cdd:PRK10261 92 eqsAAQMRHVRGADMAMIFQEPMTSlnpvftvgEQIAESIRLhqgasreeAMVEAkrmlDQVRIPEA-QTILSRYPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 638 GGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQkemsMGVIFITHDMGVVAEiADRVLVMYQG 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
515-718 |
4.09e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 4.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVK----LILGIHLPnEGTIRTFGipHT-------HPDYYQIRRRIGTVLQEDH 583
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELLG--RTvqregrlARDIRKSRANTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 LF-RGSIADNII---------------FFSEDRNHERMIQCARLALIDsdimtmpMGYQTLigetgGGLSGGQKQRILLA 647
Cdd:PRK09984 97 LVnRLSVLENVLigalgstpfwrtcfsWFTREQKQRALQALTRVGMVH-------FAHQRV-----STLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 648 RALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPE-TIASADRVLYLTDG--YFTDLTHQYRN 718
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINqndgITVVVTLHQVDyALRYCERIVALRQGhvFYDGSSQQFDN 242
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
518-674 |
4.32e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.18 E-value: 4.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFR------GSIAD 591
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLnprqriSQILD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 -----NIIFFSEDRnHERMIQCAR-LALIDSDIMTMPmgyqtligetgGGLSGGQKQRILLARALYKKPGFLLLDEATSH 665
Cdd:PRK15112 112 fplrlNTDLEPEQR-EKQIIETLRqVGLLPDHASYYP-----------HMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
....*....
gi 749181994 666 LDVESEIQI 674
Cdd:PRK15112 180 LDMSMRSQL 188
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
511-681 |
4.44e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGtVLQEDHLFRGSIA 590
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG-LLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIFFSEDRNHERMIqcARLALIDSDIMTMPM---GYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLD 667
Cdd:PRK10253 98 VQELVARGRYPHQPLF--TRWRKEDEEAVTKAMqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170
....*....|....
gi 749181994 668 VESEIQISQTLRQL 681
Cdd:PRK10253 176 ISHQIDLLELLSEL 189
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
518-717 |
4.54e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRRRIGTVLQEDHLFrgsiadniiffs 597
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF------------ 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 598 eDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGG---QKQRILLARALYKKPGFLLLDEATSHLDVESEIQI 674
Cdd:PRK10522 410 -DQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLskgQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 675 SQTL----RQLKVPVLLIAHRPETIASADRVLYLTDGYFTDLTHQYR 717
Cdd:PRK10522 489 YQVLlpllQEMGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEER 535
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
503-707 |
5.02e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 503 IAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIhLPN------EGTIRTFGIPHTHPDYYQIRR--- 573
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLLHASEQTLRGvrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 574 -RIGTVLQED-------HLFRGSIADniiFFSEDRNHER------MIQC-ARLALIDSDIMTMPMGYQtligetgggLSG 638
Cdd:PRK15134 92 nKIAMIFQEPmvslnplHTLEKQLYE---VLSLHRGMRReaargeILNClDRVGIRQAAKRLTDYPHQ---------LSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 639 GQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqelnMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
511-661 |
5.67e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 54.77 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG--IPH-THPDYYQIRRRIGTVLQEDHLFRG 587
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenIPAmSRSRLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 588 -SIADNIIFfsEDRNHERMIQcarlALIDSDIMTM--PMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDE 661
Cdd:PRK11831 99 mNVFDNVAY--PLREHTQLPA----PLLHSTVMMKleAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDE 169
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
525-690 |
8.22e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.56 E-value: 8.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 525 GEVVAITGKSGCGKSTLVKLILGIHLPNegtirtFGIPHTHPDYYQIRRRI-GTVLQeDHL------------------- 584
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKPN------LGDYDEEPSWDEVLKRFrGTELQ-DYFkklangeikvahkpqyvdl 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 ----FRGSIADNIiffseDRNHERMIQ---CARLAL---IDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKP 654
Cdd:COG1245 172 ipkvFKGTVRELL-----EKVDERGKLdelAEKLGLeniLDRDISELSGG---------------ELQRVAIAAALLRDA 231
|
170 180 190
....*....|....*....|....*....|....*....
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQL---KVPVLLIAH 690
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELaeeGKYVLVVEH 270
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
511-707 |
9.55e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.53 E-value: 9.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGihlpnegtirtfgiphtHPDYyqirrrigTVLQEDHLFRGsia 590
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-----------------HPKY--------EVTSGSILLDG--- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNI------------IFFS---------------------EDRNHERMIQ------CARLAL--IDSDIMTMPM------ 623
Cdd:COG0396 64 EDIlelspderaragIFLAfqypveipgvsvsnflrtalnARRGEELSAReflkllKEKMKElgLDEDFLDRYVnegfsg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 624 GyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESeIQI-SQTLRQLKVP---VLLIAHRPETIA--S 697
Cdd:COG0396 144 G---------------EKKRNEILQMLLLEPKLAILDETDSGLDIDA-LRIvAEGVNKLRSPdrgILIITHYQRILDyiK 207
|
250
....*....|
gi 749181994 698 ADRVLYLTDG 707
Cdd:COG0396 208 PDFVHVLVDG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
513-707 |
1.28e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIhLPNE-GTIRTFGiphthpdyyqirRRIGTVLQEDHLfrgsiAD 591
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGA-LPRTsGYVTLDG------------HEVVTRSPQDGL-----AN 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIFFSEDRNH----------ERMIQCA------------------------RLALIDSDIMTMPMGyqtligetggGLS 637
Cdd:PRK10762 328 GIVYISEDRKRdglvlgmsvkENMSLTAlryfsraggslkhadeqqavsdfiRLFNIKTPSMEQAIG----------LLS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 638 GGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVP----VLLIAHRPETIASADRVLYLTDG 707
Cdd:PRK10762 398 GGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEglsiILVSSEMPEVLGMSDRILVMHEG 471
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
179-441 |
2.81e-07 |
|
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: 52.79 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 179 ILTLGSPLLNQLVIDEVLVAADRS--------LLTVVIVAllllsltqMLLSLACQWASITLSVNFNMQWTARVFHHLVR 250
Cdd:cd18548 13 LLELLLPTLMADIIDEGIANGDLSyilrtgllMLLLALLG--------LIAGILAGYFAAKASQGFGRDLRKDLFEKIQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 251 LPLAWFDARSRGSVNARF--DaIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLI-----AVLAAVIYGVMRTL 323
Cdd:cd18548 85 FSFAEIDKFGTSSLITRLtnD-VTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALIllvaiPILALVVFLIMKKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 324 wYPSLR--QSAEDAWDAGARESgyfletLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIAHTLTGSVV 401
Cdd:cd18548 164 -IPLFKkvQKKLDRLNRVVREN------LTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLA 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 749181994 402 SAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18548 237 IVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLS 276
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
510-711 |
2.91e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLIlgihlpNEGTIRTFGIPHT------------HPDYYQIRRRIGT 577
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTL------NRMNDKVSGYRYSgdvllggrsifnYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 578 VLQEDHLFRGSIADNIIffSEDRNHE-------RMIQCARLALIDsdimtMPMGYQTLIGETGGGLSGGQKQRILLARAL 650
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVL--AGVRAHKlvprkefRGVAQARLTEVG-----LWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAHRPETIAS-ADRVLYLTDGYFTD 711
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNLAQAARiSDRAALFFDGRLVE 242
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
515-682 |
3.04e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.58 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH----------PDYYQIRRRIgTVLQEDHL 584
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQalqknlvayvPQSEEVDWSF-PVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 FRGSIAdNIIFFSEDRNHERMIQCARLALID-SDIMTMPMGyqtligetggGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:PRK15056 102 MMGRYG-HMGWLRRAKKRDRQIVTAALARVDmVEFRHRQIG----------ELSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170
....*....|....*....
gi 749181994 664 SHLDVESEIQISQTLRQLK 682
Cdd:PRK15056 171 TGVDVKTEARIISLLRELR 189
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
511-690 |
3.14e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKST----LVKLIlgihlPNEGTIRTFGIPHTHPDYYQ---IRRRIGTVLQEDH 583
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 lfrGSI-----ADNII---------FFSEDRNHERMIQCARLALIDSDI-MTMPMGYQTligetggglsgGQKQRILLAR 648
Cdd:PRK15134 373 ---SSLnprlnVLQIIeeglrvhqpTLSAAQREQQVIAVMEEVGLDPETrHRYPAEFSG-----------GQRQRIAIAR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 649 ALYKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAH 690
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKSLqqkhQLAYLFISH 484
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
508-712 |
3.55e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 508 KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGihLPNEGTIrTFGI--PHTHPDYYQIRRRIGTVLQED-HL 584
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVI-TGGDrlVNGRPLDSSFQRSIGYVQQQDlHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 FRGSIADNIIFFSEDRNHERMIQCARLALIDS--DIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLL-LDE 661
Cdd:TIGR00956 849 PTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEviKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 662 ATSHLDVESEIQISQTLRQLK---VPVLLIAHRPETI--ASADRVLYLTDG----YFTDL 712
Cdd:TIGR00956 929 PTSGLDSQTAWSICKLMRKLAdhgQAILCTIHQPSAIlfEEFDRLLLLQKGgqtvYFGDL 988
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
515-707 |
3.80e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.11 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGI---PHTHPDYYQIRRR-IGTVLQEDHLF-RGSI 589
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiaKISDAELREVRRKkIAMVFQSFALMpHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 590 ADNIIFFSE------DRNHERMIQCARlalidsdimtmPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:PRK10070 124 LDNTAFGMElaginaEERREKALDALR-----------QVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 664 SHLDVESEIQISQTLRQLKVP----VLLIAHR-PETIASADRVLYLTDG 707
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqrtIVFISHDlDEAMRIGDRIAIMQNG 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
521-681 |
4.14e-07 |
|
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: 51.64 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 521 TLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH-PDYYQIRRRiGTVlqeDHLFRGSIADniiFFSEd 599
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYkPQYIKADYE-GTV---RDLLSSITKD---FYTH- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 600 rnhermiqcarlALIDSDIMTmPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLR 679
Cdd:cd03237 93 ------------PYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
..
gi 749181994 680 QL 681
Cdd:cd03237 160 RF 161
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
515-557 |
5.82e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.47 E-value: 5.82e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR 557
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
515-709 |
6.41e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTH--PDYYQiRRRIGTVLQEDHLFRG-SIAD 591
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFngPKSSQ-EAGIGIIHQELNLIPQlTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIFFSEDRNH------ERMIQ-----CARLAL-IDSDIM--TMPMGYQtligetggglsggqkQRILLARALYKKPGFL 657
Cdd:PRK10762 99 NIFLGREFVNRfgridwKKMYAeadklLARLNLrFSSDKLvgELSIGEQ---------------QMVEIAKVLSFESKVI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 658 LLDEATSHL-DVESEiQISQTLRQLKVP---VLLIAHRPETIAS-ADRVLYLTDGYF 709
Cdd:PRK10762 164 IMDEPTDALtDTETE-SLFRVIRELKSQgrgIVYISHRLKEIFEiCDDVTVFRDGQF 219
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
512-707 |
9.71e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 9.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIhLP-----NEGTIRTFGIPhTHPDyyQIR-RRIGTVLQ----- 580
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGI-LPagvrqTAGRVLLDGKP-VAPC--ALRgRKIATIMQnprsa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 581 ------------EDHLFRGSIADNiiffsedrnhERMIQCARLALIDSDimtmpmgyQTLIGETGGGLSGGQKQRILLAR 648
Cdd:PRK10418 92 fnplhtmhtharETCLALGKPADD----------ATLTAALEAVGLENA--------ARVLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 749181994 649 ALYKKPGFLLLDEATSHLDVESEIQISQTL----RQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLesivQKRALGMLLVTHDMGVVARlADDVAVMSHG 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
515-702 |
1.49e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILgihlpnegtirtfgiphthpdYYQIRRRIGTVLQedhLFRgsiADNII 594
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL---------------------YASGKARLISFLP---KFS---RNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 595 FFSEDRNhermiqcarlaLIDSDIMTMPMG--YQTLigetggglSGGQKQRILLARALYKKPG--FLLLDEATSHLDves 670
Cdd:cd03238 64 FIDQLQF-----------LIDVGLGYLTLGqkLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLH--- 121
|
170 180 190
....*....|....*....|....*....|....*...
gi 749181994 671 EIQISQ------TLRQLKVPVLLIAHRPETIASADRVL 702
Cdd:cd03238 122 QQDINQllevikGLIDLGNTVILIEHNLDVLSSADWII 159
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
509-711 |
1.50e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 509 GSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTfgiphtHPDYyqirrRIGTVLQEDHL---- 584
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP------APGI-----KVGYLPQEPQLdpek 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 -FRGSIAD------------NIIF--FSEDR-----------------------NHERMIQCARLAL----IDSDIMTMP 622
Cdd:PRK11819 86 tVRENVEEgvaevkaaldrfNEIYaaYAEPDadfdalaaeqgelqeiidaadawDLDSQLEIAMDALrcppWDAKVTKLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 623 MGyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHrpetiasaDRvl 702
Cdd:PRK11819 166 GG---------------ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTH--------DR-- 220
|
....*....
gi 749181994 703 yltdgYFTD 711
Cdd:PRK11819 221 -----YFLD 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
515-707 |
1.71e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP-HTHPDYYQIRRRIGTVLQEDHLFRG-SIADN 592
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEiDFKSSKEALENGISMVHQELNLVLQrSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 II--------FFSEdrnHERMIQCARLALIDSDIMTMPmgyqtliGETGGGLSGGQKQRILLARALYKKPGFLLLDEATS 664
Cdd:PRK10982 94 MWlgryptkgMFVD---QDKMYRDTKAIFDELDIDIDP-------RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 665 HL---DVESEIQISQTLRQLKVPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK10982 164 SLtekEVNHLFTIIRKLKERGCGIVYISHKMEEIFQlCDEITILRDG 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
521-690 |
1.83e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 521 TLHTGEVVAITGKSGCGKSTLVKLILGIHLPNegtirtFGIPHTHPDYYQIRRRI-GTVLQeDHL--------------- 584
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPN------LGDYEEEPSWDEVLKRFrGTELQ-NYFkklyngeikvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 585 --------FRGSIADNIIFFSEDRNHERMIQcaRLAL---IDSDIMTMPMGyqtligetggglsggQKQRILLARALYKK 653
Cdd:PRK13409 168 yvdlipkvFKGKVRELLKKVDERGKLDEVVE--RLGLeniLDRDISELSGG---------------ELQRVAIAAALLRD 230
|
170 180 190
....*....|....*....|....*....|....*....
gi 749181994 654 PGFLLLDEATSHLDVESEIQISQTLRQL--KVPVLLIAH 690
Cdd:PRK13409 231 ADFYFFDEPTSYLDIRQRLNVARLIRELaeGKYVLVVEH 269
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
515-707 |
1.90e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.40 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR---TFGIPHTHP-DYYQIRRRIGTVLQ--EDHLFRGS 588
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTigeRVITAGKKNkKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIF------FSEDRNHERMIQCARLALIDSDIMT-----MPMGyqtligetggglsggQKQRILLARALYKKPGFL 657
Cdd:PRK13634 103 VEKDICFgpmnfgVSEEDAKQKAREMIELVGLPEELLArspfeLSGG---------------QMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 749181994 658 LLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFYKLHkekgLTTVLVTHSMEDAARyADQIVVMHKG 222
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
512-706 |
2.00e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIH---LPNEGTI--RTFGIPHThpdYYQIRRRIGTVLQEDHL-F 585
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgYSNDLTLfgRRRGSGET---IWDIKKHIGYVSSSLHLdY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 586 RGSI-ADNII---FFSE--------DRNHERMIQCARLALIDSDIMTMPmgYQTLigetggglSGGQKQRILLARALYKK 653
Cdd:PRK10938 350 RVSTsVRNVIlsgFFDSigiyqavsDRQQKLAQQWLDILGIDKRTADAP--FHSL--------SWGQQRLALIVRALVKH 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 749181994 654 PGFLLLDEATSHLD------VES--EIQISQTLRQLkvpvLL-----------IAHRPETIASADRVLYLTD 706
Cdd:PRK10938 420 PTLLILDEPLQGLDplnrqlVRRfvDVLISEGETQL----LFvshhaedapacITHRLEFVPDGDIYRYVQT 487
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
521-690 |
2.59e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.58 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 521 TLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI-RTFGIPHThPDYyqIRRRI-GTVlqEDHLFrgSIADNI---IF 595
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdPELKISYK-PQY--IKPDYdGTV--EDLLR--SITDDLgssYY 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 596 FSEdrnherMIQcaRLALidSDIMTMPM-----GyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVES 670
Cdd:PRK13409 434 KSE------IIK--PLQL--ERLLDKNVkdlsgG---------------ELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180
....*....|....*....|....
gi 749181994 671 EIQISQTLRQL----KVPVLLIAH 690
Cdd:PRK13409 489 RLAVAKAIRRIaeerEATALVVDH 512
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
244-444 |
2.86e-06 |
|
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: 49.62 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 244 VFHHLVRLPLAWFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCM-MLLYSPEMTLI-AVLAAVIYGVMR 321
Cdd:cd18784 75 LFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVfMFKLSWQLSLVtLIGLPLIAIVSK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 322 TL--WYPSLRQSAEDAWdagARESGYFLETLSGILSLR-INGVTTHREAAWLNLNVTRRnTQLRQSRLLMYYDIAHTLTG 398
Cdd:cd18784 155 VYgdYYKKLSKAVQDSL---AKANEVAEETISSIRTVRsFANEDGEANRYSEKLKDTYK-LKIKEALAYGGYVWSNELTE 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 749181994 399 SVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKF 444
Cdd:cd18784 231 LALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVY 276
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
515-712 |
3.10e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGT--IRTFGIP---HTHPDYYQIRRRIGTVLQ--EDHLFRG 587
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtiVGDYAIPanlKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIF----FSEDRnHERMIQCARLAlidsDIMTMPMGYqtlIGETGGGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:PRK13645 107 TIEKDIAFgpvnLGENK-QEAYKKVPELL----KLVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 664 SHLDVESE---IQISQTL-RQLKVPVLLIAHRPETIAS-ADRVLYLTDGYFTDL 712
Cdd:PRK13645 179 GGLDPKGEedfINLFERLnKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISI 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
502-690 |
3.23e-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: 50.45 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 502 HIAFSHKGSNKPILRGVSLTLHTGEVVAITGKSGCGKS----TLVKLilgihLPN-----EGTIRTFGIPHTHPDYYQIR 572
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRL-----LPDpaahpSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 573 R----RIGTVLQE-----DHLFRgsIADNII-------FFSEDRNHERMIQCARLALIDSDimTMPM---------Gyqt 627
Cdd:COG4172 88 RirgnRIAMIFQEpmtslNPLHT--IGKQIAevlrlhrGLSGAAARARALELLERVGIPDP--ERRLdayphqlsgG--- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 628 ligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAH 690
Cdd:COG4172 161 ------------QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQrelgMALLLITH 215
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
515-556 |
3.38e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 50.27 E-value: 3.38e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI 556
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
521-690 |
3.82e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.17 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 521 TLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTfGI-----P-HTHPDYYqirrriGTVlqEDHLfRGSIADNI- 593
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLkisykPqYISPDYD------GTV--EEFL-RSANTDDFg 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 594 --IFFSEdrnherMIQCARL-ALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLLDEATSHLDVES 670
Cdd:COG1245 432 ssYYKTE------IIKPLGLeKLLDKNVKDLSGG---------------ELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180
....*....|....*....|....
gi 749181994 671 EIQISQTLRQL----KVPVLLIAH 690
Cdd:COG1245 491 RLAVAKAIRRFaenrGKTAMVVDH 514
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
517-690 |
3.92e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 48.83 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 517 GVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIP-HTHPDyYQIRRRiGTV--LQEDHLFRG-SIADN 592
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiEGLPG-HQIARM-GVVrtFQHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 II----------FFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEA 662
Cdd:PRK11300 101 LLvaqhqqlktgLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190
....*....|....*....|....*....|..
gi 749181994 663 TSHLDVESEIQISQTLRQLK----VPVLLIAH 690
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRnehnVTVLLIEH 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
508-709 |
3.96e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.01 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 508 KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILG------IhlpnEGTIRTFGIPHthPDYYQirRRIGTVLQE 581
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrktagvI----TGEILINGRPL--DKNFQ--RSTGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 DHLFRGSIADNIIFFSedrnhermiQCAR-LALidsdimtmpmgyqtligetggglsgGQKQRILLARALYKKPGFLLLD 660
Cdd:cd03232 88 DVHSPNLTVREALRFS---------ALLRgLSV-------------------------EQRKRLTIGVELAAKPSILFLD 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 661 EATSHLDVESEIQISQTLRQLK---VPVLLIAHRP--ETIASADRVLYLTDG----YF 709
Cdd:cd03232 134 EPTSGLDSQAAYNIVRFLKKLAdsgQAILCTIHQPsaSIFEKFDRLLLLKRGgktvYF 191
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
515-682 |
4.03e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 48.72 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQI-RRRIGTVLQEDHLF-RGSIADN 592
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKImREAVAIVPEGRRVFsRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 593 II---FFSED---------------RNHERMIQCARlalidsdimTMPMGYQtligetggglsggqkQRILLARALYKKP 654
Cdd:PRK11614 101 LAmggFFAERdqfqerikwvyelfpRLHERRIQRAG---------TMSGGEQ---------------QMLAIGRALMSQP 156
|
170 180
....*....|....*....|....*...
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQLK 682
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLR 184
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
528-710 |
4.43e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 528 VAITGKSGCGKSTLVKLILGIHLPNEGTIrtfgiphthpdYYQIRRRIGtVLQEDHLFRGSIADNIIFFsedrnherMIQ 607
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMA-VFSQHHVDGLDLSSNPLLY--------MMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 608 C------ARL-ALIDSDIMTMPMGYQTLigetgGGLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQ 680
Cdd:PLN03073 598 CfpgvpeQKLrAHLGSFGVTGNLALQPM-----YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL 672
|
170 180 190
....*....|....*....|....*....|.
gi 749181994 681 LKVPVLLIAHRPETIA-SADRVLYLTDGYFT 710
Cdd:PLN03073 673 FQGGVLMVSHDEHLISgSVDELWVVSEGKVT 703
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
243-441 |
4.58e-06 |
|
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: 49.17 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFDAiDT--IQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIA-------VLA 313
Cdd:cd18780 80 RLFSAIIAQEIAFFDVTRTGELLNRLSS-DTqvLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMlsvvpplSIG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 314 AVIYGvmrtlWYpsLRQSAEDAWDAGARESGYFLETLSGILSLR-INGVTTHREAAWLNLNVTrRNTQLRQSRLLMYYDI 392
Cdd:cd18780 159 AVIYG-----KY--VRKLSKKFQDALAAASTVAEESISNIRTVRsFAKETKEVSRYSEKINES-YLLGKKLARASGGFNG 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 393 AHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLT 441
Cdd:cd18780 231 FMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLS 279
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
243-444 |
4.62e-06 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 49.01 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFDAiDTIQQAlttQVLEGILDVLL--VVTALCM---MLLYSPEMTLIAVLA-AVI 316
Cdd:cd18589 74 LVFAAVLRQEIAFFDSNQTGDIVSRVTT-DTEDMS---ESLSENLSLLMwyLARGLFLfifMLWLSPKLALLTALGlPLL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 317 YGVMRTL--WYPSLRQSAEDAWdagARESGYFLETLSGILSLRI----NGVTTHREAawlNLNVTRRNTQLRQsrllMYY 390
Cdd:cd18589 150 LLVPKFVgkFQQSLAVQVQKSL---ARANQVAVETFSAMKTVRSfaneEGEAQRYRQ---RLQKTYRLNKKEA----AAY 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 391 DI---AHTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTDKF 444
Cdd:cd18589 220 AVsmwTSSFSGLALKVGILYYGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYY 276
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
517-711 |
5.74e-06 |
|
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: 49.42 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 517 GVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRT-FG---IPHTHPDYY---QIRRRIGTVLQEDHLF-RGS 588
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGdewVDMTKPGPDgrgRAKRYIGILHQEYDLYpHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIiffSEDRNHERMIQCARLALIdsdIMTMPMGY-----QTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:TIGR03269 382 VLDNL---TEAIGLELPDELARMKAV---ITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPT 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 664 SHLDVESEIQISQTL----RQLKVPVLLIAHRPETIAS-ADRVLYLTDGYFTD 711
Cdd:TIGR03269 456 GTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVK 508
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
525-690 |
5.77e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.52 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 525 GEVVAITGKSGCGKSTLVKLILGIHLPNEGTirtfgipHTHPDYYQ--IRRRIGTVLQE-------------------DH 583
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK-------FDDPPDWDeiLDEFRGSELQNyftkllegdvkvivkpqyvDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 L---FRGSIADNIiffseDRNHERMIQ---CARLAL---IDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKP 654
Cdd:cd03236 99 IpkaVKGKVGELL-----KKKDERGKLdelVDQLELrhvLDRNIDQLSGG---------------ELQRVAIAAALARDA 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 749181994 655 GFLLLDEATSHLDVESEIQISQTLRQLKVP---VLLIAH 690
Cdd:cd03236 159 DFYFFDEPSSYLDIKQRLNAARLIRELAEDdnyVLVVEH 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
510-690 |
8.08e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 8.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILG-IHL--------------------PN--EGTIRTF---GIPH 563
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGeVLLddgriiyeqdlivarlqqdpPRnvEGTVYDFvaeGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 564 TH---PDYYQIRRRIGTVLQEDHLFRGSIADNIIFFS-----EDRNHErmiQCARLAL-IDSDIMTMPMGYQtligetgg 634
Cdd:PRK11147 94 QAeylKRYHDISHLVETDPSEKNLNELAKLQEQLDHHnlwqlENRINE---VLAQLGLdPDAALSSLSGGWL-------- 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 635 glsggqkQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAH 690
Cdd:PRK11147 163 -------RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISH 211
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
245-433 |
1.03e-05 |
|
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: 47.95 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 245 FHHLVRLPLAWFDARSRGSV----NarfDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVM 320
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLmsvlN---NDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAG 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 321 rTLWYpslRQSAEDAWDAgARESgyfLETLSGILSLRINGVTT-------HREAAwlnlNVTRRNTQLRQSRL------L 387
Cdd:cd18565 171 -TYWF---QRRIEPRYRA-VREA---VGDLNARLENNLSGIAVikaftaeDFERE----RVADASEEYRDANWrairlrA 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 749181994 388 MYYDIAHTLTGsVVSAIILWKGAGEVLNG------TFTVGMLVAYLSYQMRF 433
Cdd:cd18565 239 AFFPVIRLVAG-AGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRL 289
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
516-712 |
1.28e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 516 RGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHT-HPDYYQIRRRIGTVLQ---EDHLFRG-SIA 590
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMAYITEsrrDNGFFPNfSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNI----------------IFFSEDRNHERMIQCARLAL----IDSDIMTMPMGYQtligetggglsggqkQRILLARAL 650
Cdd:PRK09700 360 QNMaisrslkdggykgamgLFHEVDEQRTAENQRELLALkchsVNQNITELSGGNQ---------------QKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 749181994 651 YKKPGFLLLDEATSHLDVESEIQISQTLRQL----KVPVLLIAHRPETIASADRVLYLTDGYFTDL 712
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaddgKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
498-698 |
1.38e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.40 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 498 LTLTHIAFShkgSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTI--RTFGIPHTHPDYYQ-IRRR 574
Cdd:PRK13541 2 LSLHQLQFN---IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIyyKNCNINNIAKPYCTyIGHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 575 IGTVLQEdhlfrgSIADNIIFFSEDRNHERMIQCA----RLA-LIDSDIMTMPMGYQtligetggglsggqkQRILLARA 649
Cdd:PRK13541 79 LGLKLEM------TVFENLKFWSEIYNSAETLYAAihyfKLHdLLDEKCYSLSSGMQ---------------KIVAIARL 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 650 LYKKPGFLLLDEATSHLDVESEiQISQTLRQLKVP----VLLIAHRPETIASA 698
Cdd:PRK13541 138 IACQSDLWLLDEVETNLSKENR-DLLNNLIVMKANsggiVLLSSHLESSIKSA 189
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
518-707 |
1.61e-05 |
|
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: 47.90 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHlPN--EGTIRTFGIP-HTHPDYYQIRRRIGTVlQEDHLFRGSIAD--- 591
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGkfEGNVFINGKPvDIRNPAQAIRAGIAMV-PEDRKRHGIVPIlgv 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 --NIIFFSEDRNHERMI--QCARLALIDSDIMTM---------PMGyqtligetggGLSGGQKQRILLARALYKKPGFLL 658
Cdd:TIGR02633 357 gkNITLSVLKSFCFKMRidAAAELQIIGSAIQRLkvktaspflPIG----------RLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 659 LDEATSHLDVESEIQISQTLRQLK---VPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAqegVAIIVVSSElAEVLGLSDRVLVIGEG 479
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
518-704 |
1.82e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrTFGIPH--THPDY--YQIRRRIGTVLQEDHLF---RGSIA 590
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEI-IFNGQRidTLSPGklQALRRDIQFIFQDPYASldpRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNII-------FFSEDRNHERMIQC-ARLALIDSDIMTMPMGYQTligetggglsgGQKQRILLARALYKKPGFLLLDEA 662
Cdd:PRK10261 422 DSIMeplrvhgLLPGKAAAARVAWLlERVGLLPEHAWRYPHEFSG-----------GQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 749181994 663 TSHLDVESEIQISQTL----RQLKVPVLLIAHR---PETIASADRVLYL 704
Cdd:PRK10261 491 VSALDVSIRGQIINLLldlqRDFGIAYLFISHDmavVERISHRVAVMYL 539
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
513-557 |
3.51e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 46.76 E-value: 3.51e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 749181994 513 PILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR 557
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW 62
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
242-425 |
4.01e-05 |
|
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: 46.28 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 242 ARVFHHLVRLPLAwFDARSRGSVNARFDAIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEM---TLIAVLAAVIYG 318
Cdd:cd18587 79 SRLFERVLGLRLE-ARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLalvPLVAIPLVLLYG 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 319 VmrtLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRqSRLLMyyDIAHTLTG 398
Cdd:cd18587 158 L---LLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLK-SRLLS--SSATNFAQ 231
|
170 180 190
....*....|....*....|....*....|.
gi 749181994 399 SVVS----AIILWkGAGEVLNGTFTVGMLVA 425
Cdd:cd18587 232 FVQQlvtvAIVIV-GVYLISDGELTMGGLIA 261
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
245-440 |
4.03e-05 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 46.18 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 245 FHHLVRLPLAWFDARSRGSVNARFdAIDTiqqALTTQVLEGILDVLL-----VVTALCMMLLYSPEMTLIAVLAAVIYGV 319
Cdd:cd18590 76 FSSLVQQDIGFFEKTKTGDLTSRL-STDT---TLMSRSVALNANVLLrslvkTLGMLGFMLSLSWQLTLLTLIEMPLTAI 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 320 MRTLWYPSLRQSAEDAWDAGARESGYFLETLSGILSLRINGVTTHREAAWLN-LNVTRRNTQLRQSRLLMYYDIAHTLTG 398
Cdd:cd18590 152 AQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEaLERTYNLKDRRDTVRAVYLLVRRVLQL 231
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 749181994 399 SVvSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSL 440
Cdd:cd18590 232 GV-QVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTL 272
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
518-667 |
4.27e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPhTHPDYYQIRRRIG------------TVLQ--EDH 583
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP-VDAGDIATRRRVGymsqafslygelTVRQnlELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 --LFRGSIADniiffSEDRNHERMIQCARLALIDSDIMTMPMGyqtligetggglsggQKQRILLARALYKKPGFLLLDE 661
Cdd:NF033858 364 arLFHLPAAE-----IAARVAEMLERFDLADVADALPDSLPLG---------------IRQRLSLAVAVIHKPELLILDE 423
|
....*.
gi 749181994 662 ATSHLD 667
Cdd:NF033858 424 PTSGVD 429
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
641-690 |
4.70e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 4.70e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAH 690
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISH 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
515-707 |
6.29e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHlPN---------EGTIRTFGiphthpdyyQIR--RRIGTVL--QE 581
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyegeilfDGEVCRFK---------DIRdsEALGIVIihQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 582 ----DHLfrgSIADNIIFFSE---------DRNHERMIQ-CARLALIDSD---IMTMPMGYQTLIGetggglsggqkqri 644
Cdd:NF040905 87 laliPYL---SIAENIFLGNErakrgvidwNETNRRARElLAKVGLDESPdtlVTDIGVGKQQLVE-------------- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 749181994 645 lLARALYKKPGFLLLDEATSHL-DVESEiQISQTLRQLK---VPVLLIAHRPETIAS-ADRVLYLTDG 707
Cdd:NF040905 150 -IAKALSKDVKLLILDEPTAALnEEDSA-ALLDLLLELKaqgITSIIISHKLNEIRRvADSITVLRDG 215
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
226-338 |
6.50e-05 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 45.29 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 226 QWASITLSVNFnmqwtarvFHHLVRLPLAWFDARSRGSVNARFD----AIDTIQQALTTQVLEGILDVLLVVTALcmMLL 301
Cdd:cd18560 67 QNAYRELSLKT--------FAHLHSLSLDWHLSKKTGEVVRIMDrgteSANTLLSYLVFYLVPTLLELIVVSVVF--AFH 136
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 749181994 302 YSPEMTLIAVLAAVIYGVMR---TLWYPSLRQSAEDAWDA 338
Cdd:cd18560 137 FGAWLALIVFLSVLLYGVFTikvTEWRTKFRRAANKKDNE 176
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
511-560 |
1.06e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 1.06e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG 560
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER 62
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
516-712 |
1.18e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.43 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 516 RGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrTFGIPHTHPDYYQIRRRIGTV-LQEDHLFRG------- 587
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRI-MLNGKEINALSTAQRLARGLVyLPEDRQSSGlyldapl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 -----SIADNIIFFSEDRNHERMI-QCARLAL------IDSDIMTMPMGYQtligetggglsggqkQRILLARALYKKPG 655
Cdd:PRK15439 359 awnvcALTHNRRGFWIKPARENAVlERYRRALnikfnhAEQAARTLSGGNQ---------------QKVLIAKCLEASPQ 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 656 FLLLDEATSHLDVESEIQISQTLRQL---KVPVLLIAHRPETIAS-ADRVLYLTDGYFTDL 712
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIaaqNVAVLFISSDLEEIEQmADRVLVMHQGEISGA 484
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
641-719 |
1.29e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLK----VPVLLIAHRPETIA-SADRVLYLTDG----Y--- 708
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrefnTAIIMITHDLGVVAgICDKVLVMYAGrtmeYgna 246
|
90
....*....|....
gi 749181994 709 ---FTDLTHQYRNG 719
Cdd:PRK09473 247 rdvFYQPSHPYSIG 260
|
|
| Peptidase_C39_likeD |
cd02421 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
25-138 |
1.69e-04 |
|
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 not conserved in this sub-family.
Pssm-ID: 239102 [Multi-domain] Cd Length: 124 Bit Score: 41.84 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 25 LACLAMMACWHGLQTDLTTLRERFSISTQGMTLQRLIECAAGIQLSSRAVRLEPEDLKSLSLPCILHWNMNHFVVLHKVR 104
Cdd:cd02421 9 LDCLVLLARQFGKPASRDSLVAGLPLDDGRLSPALFPRAAARAGLSARVVRRPLDAIPTLLLPAILLLKNGRACVLLGVD 88
|
90 100 110
....*....|....*....|....*....|....*.
gi 749181994 105 RSRLVIHDP--DKGKITLSLQDAGKHFTGVALELMP 138
Cdd:cd02421 89 DGHARILDPesGGGEVEISLEELEEEYSGYAIFVKP 124
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
507-560 |
1.73e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 1.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 749181994 507 HKGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFG 560
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG 85
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
512-557 |
1.83e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.94 E-value: 1.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR 557
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
518-552 |
2.93e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 43.74 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|....*
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPN 552
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN 60
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
511-704 |
4.05e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 511 NKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIR-TFGIPHTHPDYYQIR--RRIGTVLQedHLFRg 587
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlAKGIKLGYFAQHQLEflRADESPLQ--HLAR- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 sIADniiffsedrnhERMIQCARLAL----IDSDIMTMPMGyqtligetggGLSGGQKQRILLARALYKKPGFLLLDEAT 663
Cdd:PRK10636 401 -LAP-----------QELEQKLRDYLggfgFQGDKVTEETR----------RFSGGEKARLVLALIVWQRPNLLLLDEPT 458
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 749181994 664 SHLDVESEIQISQTLRQLKVPVLLIAHRPETIASADRVLYL 704
Cdd:PRK10636 459 NHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYL 499
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
514-679 |
4.37e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPN--EGTIRTFGIPHTHPDYYQIRrriGTVLQED-HLFRGSIA 590
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQETFARIS---GYCEQNDiHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 591 DNIIFFS------EDRNHERMI---QCARLALIDS---DIMTMP--MGYQTligetggglsgGQKQRILLARALYKKPGF 656
Cdd:PLN03140 972 ESLIYSAflrlpkEVSKEEKMMfvdEVMELVELDNlkdAIVGLPgvTGLST-----------EQRKRLTIAVELVANPSI 1040
|
170 180
....*....|....*....|...
gi 749181994 657 LLLDEATSHLDVESEIQISQTLR 679
Cdd:PLN03140 1041 IFMDEPTSGLDARAAAIVMRTVR 1063
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
243-320 |
4.67e-04 |
|
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: 42.85 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARFDA-IDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLI----AVLAAVIY 317
Cdd:cd18577 85 RYLKALLRQDIAWFDKNGAGELTSRLTSdTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVllatLPLIAIVG 164
|
...
gi 749181994 318 GVM 320
Cdd:cd18577 165 GIM 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
510-707 |
4.81e-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: 43.85 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 510 SNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIrTFGIPHTHPDYYQIRRRIGTVLQEDHLFRG-S 588
Cdd:TIGR01257 941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTV-LVGGKDIETNLDAVRQSLGMCPQHNILFHHlT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIFFSE--DRNHERmiqcarlALIDSDIMTMPMGYQTLIGETGGGLSGGQKQRILLARALYKKPGFLLLDEATSHL 666
Cdd:TIGR01257 1020 VAEHILFYAQlkGRSWEE-------AQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 749181994 667 DVESEIQISQTL---RQLKVPVLLIAHRPETIASADRVLYLTDG 707
Cdd:TIGR01257 1093 DPYSRRSIWDLLlkyRSGRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
518-707 |
6.99e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.99 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 518 VSLTLHTGEVVAITGKSGCGKSTLVKLILGIHlP--NEGTIRTFGIPHT--HPDYyQIRRRIGTVlQEDHLFRG-----S 588
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKPVKirNPQQ-AIAQGIAMV-PEDRKRDGivpvmG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 589 IADNIIFFSEDR--NHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQkQRILLARALYKKPGFLLLDEATSHL 666
Cdd:PRK13549 358 VGKNITLAALDRftGGSRIDDAAELKTILESIQRLKVKTASPELAIARLSGGNQ-QKAVLAKCLLLNPKILILDEPTRGI 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 667 DVESEIQISQTLRQLK---VPVLLIAHR-PETIASADRVLYLTDG 707
Cdd:PRK13549 437 DVGAKYEIYKLINQLVqqgVAIIVISSElPEVLGLSDRVLVMHEG 481
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
512-681 |
7.88e-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: 42.61 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtfgIPHThpdyyqirRRIGTVLQedhlFRGSIAD 591
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE---IGET--------VKLAYVDQ----SRDALDP 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 592 NIIFFSEDRNHERMIQ-----------CARLALIDSDimtmpmgYQTLIGETGGGlsggQKQRILLARALYKKPGFLLLD 660
Cdd:TIGR03719 400 NKTVWEEISGGLDIIKlgkreipsrayVGRFNFKGSD-------QQKKVGQLSGG----ERNRVHLAKTLKSGGNVLLLD 468
|
170 180
....*....|....*....|.
gi 749181994 661 EATSHLDVEseiqisqTLRQL 681
Cdd:TIGR03719 469 EPTNDLDVE-------TLRAL 482
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
641-693 |
7.91e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 7.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 749181994 641 KQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAHRPE 693
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHARE 402
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
508-546 |
1.20e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.20e-03
10 20 30
....*....|....*....|....*....|....*....
gi 749181994 508 KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLIL 546
Cdd:TIGR00630 617 KGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTL 655
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
527-591 |
1.35e-03 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 39.78 E-value: 1.35e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 749181994 527 VVAITGKSGCGKSTLVKLI---LGIHLPNEGTIRT--FG-IPHTHPDYYQIRRRIGTVLQEDHLFRGSIAD 591
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLakkLGLPYLDTGGIRTeeVGkLASEVAAIPEVRKALDERQRELAKKPGIVLE 71
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
243-357 |
1.83e-03 |
|
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: 40.95 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 243 RVFHHLVRLPLAWFDARSRGSVNARF--DaIDTIQQALTTQVLEGILDVLLVVTALCMMLLYSPEMTLIAVLAAVIYGVM 320
Cdd:cd18580 77 KLLRSVLRAPMSFFDTTPSGRILNRFskD-IGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLL 155
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 749181994 321 RTLWYPSLRQSAedAWDAGAReS---GYFLETLSGILSLR 357
Cdd:cd18580 156 QRYYLRTSRQLR--RLESESR-SplySHFSETLSGLSTIR 192
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
514-690 |
1.83e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.69 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 514 ILRGV-------SLTLHTGEVVAITGKSGCGKSTLVKLIlgihlpnEGTIRTFGIPHTHPDYYQI-----------RRRI 575
Cdd:PRK10636 9 IRRGVrvlldnaTATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQLawvnqetpalpQPAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 576 GTVLQEDHLFRGSIADniIFFSEDRNHERMIQCARLALIDSDIMTMPMGYQTLIGETGGGLSGGQ----------KQRIL 645
Cdd:PRK10636 82 EYVIDGDREYRQLEAQ--LHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLErpvsdfsggwRMRLN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 749181994 646 LARALYKKPGFLLLDEATSHLDVESEIQISQTLRQLKVPVLLIAH 690
Cdd:PRK10636 160 LAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISH 204
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
494-681 |
1.87e-03 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.93 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 494 TDLPLTLTHIAFSHKGsnKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGIPHTHPDYYQIRR 573
Cdd:PRK10575 8 SDTTFALRNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 574 RIGTVLQEDHLFRGSIADNII-------------FFSEDRNH-ERMIQCARLA-----LIDSdimtmpmgyqtligetgg 634
Cdd:PRK10575 86 KVAYLPQQLPAAEGMTVRELVaigrypwhgalgrFGAADREKvEEAISLVGLKplahrLVDS------------------ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 749181994 635 gLSGGQKQRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL 681
Cdd:PRK10575 148 -LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
512-547 |
1.94e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 1.94e-03
10 20 30
....*....|....*....|....*....|....*.
gi 749181994 512 KPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILG 547
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG 49
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
241-450 |
2.25e-03 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 40.56 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 241 TARVFHHLVRLPLAWFDARSRGSVNARFD----AIDTIQQALTTQVLEGILDVLLVVTALCmmLLYSPEMTLIAVLAAVI 316
Cdd:cd18582 74 ALRVFRHLHSLSLRFHLSRKTGALSRAIErgtrGIEFLLRFLLFNILPTILELLLVCGILW--YLYGWSYALITLVTVAL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 317 YG---VMRTLWYPSLRQSAEDAwDAGAreSGYFLETLSGILSLRINGVTTHREAAWLNLNVTRRNTQLRQSRLLMYYDIA 393
Cdd:cd18582 152 YVaftIKVTEWRTKFRREMNEA-DNEA--NAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIG 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 749181994 394 HTLTGSVVSAIILWKGAGEVLNGTFTVGMLVAYLSYQMRFSSSISSLTdkfFAWRML 450
Cdd:cd18582 229 QALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLG---FVYREI 282
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
240-353 |
3.74e-03 |
|
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: 40.13 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 240 WTARV----FHHLVRLPLAWFD--ARSRGSVNARFdAIDTIQ-QALTTQVLEGILDVL-LVVTALCMMLLYSPEMTLIA- 310
Cdd:cd18578 83 LTRRLrklaFRAILRQDIAWFDdpENSTGALTSRL-STDASDvRGLVGDRLGLILQAIvTLVAGLIIAFVYGWKLALVGl 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 749181994 311 ----VLAAVIYGVMRtlwypSLRQSAEDAWDAGARESGYFLETLSGI 353
Cdd:cd18578 162 atvpLLLLAGYLRMR-----LLSGFEEKNKKAYEESSKIASEAVSNI 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
527-702 |
3.90e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 527 VVAITGKSGCGKSTLVKLIL-------------GIHLPN---EGTIRT---FGIPHTHPDYYQIRRRIgtvlqedhlfrg 587
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKyaltgelppnskgGAHDPKlirEGEVRAqvkLAFENANGKKYTITRSL------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 588 SIADNIIFFSEDRnhermiqcarlalIDSDIMTMP----MGYQTLIGETGgglsggqkqRILLARALYKKPGFLLLDEAT 663
Cdd:cd03240 92 AILENVIFCHQGE-------------SNWPLLDMRgrcsGGEKVLASLII---------RLALAETFGSNCGILALDEPT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 749181994 664 SHLDVES-EIQISQTLR---QLKVP-VLLIAHRPETIASADRVL 702
Cdd:cd03240 150 TNLDEENiEESLAEIIEerkSQKNFqLIVITHDEELVDAADHIY 193
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
508-704 |
5.42e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 39.13 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 508 KGSNKPILRGVSLTLHTGEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRtfgipHTHPDYYQI---RRRIGTVLQEDH- 583
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLK-----KEQPGNHDRiegLEHIDKVIVIDQs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 584 ----------------------------------------LFRG-SIADnIIFFSEDRNHERMIQCARLALIDSDIMTMP 622
Cdd:cd03271 79 pigrtprsnpatytgvfdeirelfcevckgkrynretlevRYKGkSIAD-VLDMTVEEALEFFENIPKIARKLQTLCDVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 623 MGYQTLiGETGGGLSGGQKQRILLARALYKK---PGFLLLDEATSHL---DVESEIQISQTLRQLKVPVLLIAHRPETIA 696
Cdd:cd03271 158 LGYIKL-GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLhfhDVKKLLEVLQRLVDKGNTVVVIEHNLDVIK 236
|
....*...
gi 749181994 697 SADRVLYL 704
Cdd:cd03271 237 CADWIIDL 244
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
515-546 |
5.51e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 5.51e-03
10 20 30
....*....|....*....|....*....|..
gi 749181994 515 LRGVSLTLHTGEVVAITGKSGCGKSTLVKLIL 546
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNDIL 652
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
525-690 |
6.39e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 38.32 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 525 GEVVAITGKSGCGKSTLVKLILGIHLPNEGTIRTFGI-PHTHPDYYQIRrriGTVLQedhlfrgsiadniiffsedrnhe 603
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGItPVYKPQYIDLS---GGELQ----------------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749181994 604 rmiqcarlalidsdimtmpmgyqtligetggglsggqkqRILLARALYKKPGFLLLDEATSHLDVESEIQISQTLRQL-- 681
Cdd:cd03222 79 ---------------------------------------RVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLse 119
|
170
....*....|.
gi 749181994 682 --KVPVLLIAH 690
Cdd:cd03222 120 egKKTALVVEH 130
|
|
| |
