|
Name |
Accession |
Description |
Interval |
E-value |
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
22-713 |
0e+00 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 994.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 22 LLDGLLTLCSLHYKPASRAMLTTGLPLAAQRLSAELLPRAAARAGLQGRLLQRKLEQIPSIALPAMLLLKEGRSAVLLGW 101
Cdd:TIGR03375 1 LLDCLLLLARHYGRPVSREALVAGLPLEDGRLTPELLPRAARRAGLSARLVKRSLDDISPLLLPAILLLKDGRACVLLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 102 EGD-TARLLLSESDGGEVQVSRETLSQDYSGRVFFAQPQHKFDITSGTLI-PRARSWFRDTLKRSRWLYADAIAASLVIN 179
Cdd:TIGR03375 81 DEDgKARVLLPETGDGEQELSLDALEALYSGYAIFVRPQFRFDARADELIsPRPKHWFWSTLKESWPLYRDVLIASLLIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 180 LIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIVGMAMKVRPA 259
Cdd:TIGR03375 161 LLALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTLRSYFLDVAGKKADLILSAKLFERVLGLRMEARPA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 260 RVGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHMLQKPLTATLERTMALG 339
Cdd:TIGR03375 241 SVGSFANQLREFESVRDFFTSATLTALIDLPFALLFLLVIAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRES 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 340 AERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALS 419
Cdd:TIGR03375 321 AQRNAVLVESLSGLETIKALNAEGRFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGELT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 420 MGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERNYDERPLSRKALQGAMTFREVDFTYPNQQNLA 499
Cdd:TIGR03375 401 MGGLIACVMLSGRALAPLGQLAGLLTRYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETPA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLV 579
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 580 SGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERL 659
Cdd:TIGR03375 561 LGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERF 640
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 660 KQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEALKKGQ 713
Cdd:TIGR03375 641 KDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEALRKGR 694
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-708 |
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: 696.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 18 HDDPLLDGLLTLCSLHYKPASRAMLTTGLPLAAQRLSAELLPRAAARAGLQGRLLQRKLEQIPSIALPAMLLLKEGRSAV 97
Cdd:COG2274 12 AADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPAILHWDGNHFVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 98 LLGWEGDTARLLLSESdgGEVQVSRETLSQDYSGRVFFAQPQHKFDitSGTLIPRARSWFRDTLKRSRWLYADAIAASLV 177
Cdd:COG2274 92 LEGVDGDKVTIADPAT--GRRKLSLEEFAESWTGVALLLEPTPEFD--KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 178 INLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIVGMAMKVR 257
Cdd:COG2274 168 INLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 258 PAR-VGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHMLQKPLTATLERTM 336
Cdd:COG2274 248 ESRsVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREES 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 337 ALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDG 416
Cdd:COG2274 328 EASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 417 ALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERNYDERPLSRKALQGAMTFREVDFTYPNQQ 496
Cdd:COG2274 408 QLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDS 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRD 576
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRE 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGE 656
Cdd:COG2274 568 NITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETE 647
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 814585811 657 ERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:COG2274 648 AIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
165-457 |
7.16e-147 |
|
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: 429.94 E-value: 7.16e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISAT 244
Cdd:cd18587 1 RRIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 245 LFERIVGMAMKVRPARVGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHML 324
Cdd:cd18587 81 LFERVLGLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 325 QKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVA 404
Cdd:cd18587 161 QKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 405 MIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSV 457
Cdd:cd18587 241 IVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
152-708 |
2.32e-121 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 374.89 E-value: 2.32e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 152 RARSWFRDTLKRSRWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLD 231
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 232 LAGKKTDLIISATLFERIVGMAMK-VRPARVGSFAQNI-HEFQGMRDFLTSlTLASLIDLPFTLI-ILVVIAMLGGHLVW 308
Cdd:COG1132 87 RLAQRVVADLRRDLFEHLLRLPLSfFDRRRTGDLLSRLtNDVDAVEQFLAH-GLPQLVRSVVTLIgALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 309 IPIIAFPLALGIGHMLQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSG 388
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 389 LAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERN 468
Cdd:COG1132 246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 469 YDERPLSRKALQGAMTFREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI 548
Cdd:COG1132 326 DPPGAVPLPPVRGEIEFENVSFSYPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 549 RQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQN 628
Cdd:COG1132 405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 629 VALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
148-709 |
2.64e-112 |
|
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: 350.59 E-value: 2.64e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 148 TLIPRARSWFRDTLKRSRWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRS 227
Cdd:COG4618 2 SRASAGRSELRAALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 228 LCLDLAGKKTDLIISATLFERIVGMAMKvrpARVGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLV 307
Cdd:COG4618 82 RILVRVGARLDRRLGPRVFDAAFRAALR---GGGGAAAQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 308 WIPIIA----FPLALgIGHML-QKPLTATLERTM-----ALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTigtls 377
Cdd:COG4618 159 LLALVGalvlVALAL-LNERLtRKPLKEANEAAIranafAEAALRNAEVIEAMGMLPALRRRWQRANARALALQA----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 378 rlelRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSV 457
Cdd:COG4618 233 ----RASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 458 DQMMELPQERnydERPLSRKALQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD 537
Cdd:COG4618 309 NELLAAVPAE---PERMPLPRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 538 SGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLvsgARY--VDDEMVLQAAELAGVHEF-ARLhPQGYELQV 614
Cdd:COG4618 386 AGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI---ARFgdADPEKVVAAAKLAGVHEMiLRL-PDGYDTRI 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 615 GERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE-NKTVILVTHRASLLSLVDRLLVIDR 693
Cdd:COG4618 462 GEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRD 541
|
570
....*....|....*.
gi 814585811 694 GQILADGPKAAVMEAL 709
Cdd:COG4618 542 GRVQAFGPRDEVLARL 557
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
481-700 |
1.83e-111 |
|
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: 336.10 E-value: 1.83e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 481 GAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNI 560
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPP 640
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 641 ILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
173-709 |
4.48e-94 |
|
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: 302.34 E-value: 4.48e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 173 AASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFErivgm 252
Cdd:TIGR01842 13 LFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFA----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 253 AMKVRPARVGSF--AQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLggHlVWIPIIA-------FPLALGIGHM 323
Cdd:TIGR01842 88 ASFSATLRRGSGdgLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLL--H-PWIGILAlggavvlVGLALLNNRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 324 LQKPLTATLERTMALG-----AERQSSLIETLAGLDAVkvnnaeserQYQWEQ-TIGTLSRLEL---RVKVLSGLAMNIT 394
Cdd:TIGR01842 165 TKKPLKEATEASIRANnladsALRNAEVIEAMGMMGNL---------TKRWGRfHSKYLSAQSAasdRAGMLSNLSKYFR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 395 LLIQqvagVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERnydERPL 474
Cdd:TIGR01842 236 IVLQ----SLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSR---DPAM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 475 SRKALQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVS 554
Cdd:TIGR01842 309 PLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARA 634
Cdd:TIGR01842 389 TFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARA 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 635 LLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENK-TVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEAL 709
Cdd:TIGR01842 469 LYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
277-708 |
2.00e-81 |
|
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: 269.71 E-value: 2.00e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 277 FLTSLTLASLIDLPFTLIILVVIAMLGghlVWIPIIAFPLALGIGhmlqkpltatlERTMALGAERQSSLIETLAGLDAV 356
Cdd:COG4987 143 ILAAVAFLAFFSPALALVLALGLLLAG---LLLPLLAARLGRRAG-----------RRLAAARAALRARLTDLLQGAAEL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 357 KVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALS---MGGLVACYMLSGRA 433
Cdd:COG4987 209 AAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSgplLALLVLAALALFEA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 434 LGPLAQLSGLLTRYQQAkvtMVSVDQMMELPQERNYDERPLSRKAlQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKI 513
Cdd:COG4987 289 LAPLPAAAQHLGRVRAA---ARRLNELLDAPPAVTEPAEPAPAPG-GPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 514 GIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQA 593
Cdd:COG4987 365 AIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 594 AELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVI 673
Cdd:COG4987 445 LERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVL 524
|
410 420 430
....*....|....*....|....*....|....*
gi 814585811 674 LVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:COG4987 525 LITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
153-708 |
1.25e-76 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 256.61 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 153 ARSWFRDTLKRSRWLYADAIAASLVINLIALAAPLFVMNVYDRVV-PNQATATLWMLAIGICGAYLFDLLLKSLRSLCLD 231
Cdd:COG4988 4 LDKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 232 LAGKKTDLIISATLFERIVGM-AMKVRPARVGSFAQNIHE----FQG-MRDFLTSLTLASLIdlpfTLIILVVIAMLGGH 305
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALgPAWLRGKSTGELATLLTEgveaLDGyFARYLPQLFLAALV----PLLILVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 306 LVWIPIIAFPL-----ALgIGHMLQKPLTATLERTMALGAerqsSLIETLAGLDAVKVNNAeSERQyqwEQTIGTLSR-- 378
Cdd:COG4988 160 SGLILLVTAPLiplfmIL-VGKGAAKASRRQWRALARLSG----HFLDRLRGLTTLKLFGR-AKAE---AERIAEASEdf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 379 ----LE-LRVKVLSGLAMNI--TLliqqvaGVAMI-IFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSgllTRYQQA 450
Cdd:COG4988 231 rkrtMKvLRVAFLSSAVLEFfaSL------SIALVaVYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLG---SFYHAR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 451 KVTMVSVDQMMEL----PQERNYDERPLSRKAlQGAMTFREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSL 526
Cdd:COG4988 302 ANGIAAAEKIFALldapEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGRP-ALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 527 AKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLH 606
Cdd:COG4988 380 LNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAAL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 607 PQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVD 686
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
|
570 580
....*....|....*....|..
gi 814585811 687 RLLVIDRGQILADGPKAAVMEA 708
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
165-460 |
1.55e-76 |
|
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: 247.88 E-value: 1.55e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISAT 244
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 245 LFERIVGMAM-KVRPARVGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHM 323
Cdd:cd18566 81 AFEHLLSLPLsFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 324 LQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGV 403
Cdd:cd18566 161 LGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 404 AMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKvtmVSVDQM 460
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVR---VAVRRL 294
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
112-700 |
1.70e-72 |
|
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: 249.27 E-value: 1.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 112 ESDGGEVQVSRETLSQDYSGRVFFAQPQHKFDITSgtliPRARSW--FRDTLKRSRWLYADAIAASLVINLIALAAPLFV 189
Cdd:TIGR01193 104 DPTVGITKISKEDFYEEWTGIAIFISPTPEYKPIK----EKENSLlkFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 190 MNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIVGMAMKVRPAR-VGSFAQNI 268
Cdd:TIGR01193 180 QKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRrTGEIVSRF 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 269 HEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHMLQKPLTATLERTMALGAERQSSLIE 348
Cdd:TIGR01193 260 TDASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 349 TLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYM 428
Cdd:TIGR01193 340 DLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNA 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 429 LSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERNYDERPLSRKALQGAMTFREVDFTYPNQQNlALRGINLNVR 508
Cdd:TIGR01193 420 LLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN-ILSDISLTIK 498
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 509 AGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARY-VDD 587
Cdd:TIGR01193 499 MNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKEnVSQ 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 588 EMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSvI 667
Cdd:TIGR01193 579 DEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-L 657
|
570 580 590
....*....|....*....|....*....|...
gi 814585811 668 ENKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:TIGR01193 658 QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
205-708 |
5.66e-67 |
|
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: 231.14 E-value: 5.66e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 205 LWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIVGMamkvrPAR------VGSFAQNIhefqgmrDFL 278
Cdd:TIGR02203 53 LWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGL-----PVSffdrqpTGTLLSRI-------TFD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 279 TSLTLASLIDLPFTLI--ILVVIAMLG------GHLVWIPIIAFPLALGIGHMLQKPLTATLERTMALGAERQSSLIETL 350
Cdd:TIGR02203 121 SEQVASAATDAFIVLVreTLTVIGLFIvllyysWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 351 AGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLS 430
Cdd:TIGR02203 201 QGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 431 GRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERNYDERPLSRkaLQGAMTFREVDFTYPNQQNLALRGINLNVRAG 510
Cdd:TIGR02203 281 IALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIER--ARGDVEFRNVTFRYPGRDRPALDSISLVIEPG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 511 EKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARY-VDDEM 589
Cdd:TIGR02203 359 ETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 590 VLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN 669
Cdd:TIGR02203 439 IERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQG 518
|
490 500 510
....*....|....*....|....*....|....*....
gi 814585811 670 KTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:TIGR02203 519 RTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR 557
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
484-708 |
8.88e-66 |
|
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: 217.10 E-value: 8.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYV 563
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILL 643
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 644 LDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
481-712 |
2.31e-63 |
|
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: 210.54 E-value: 2.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 481 GAMTFREVDFTYpNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNI 560
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPP 640
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 641 ILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEalKKG 712
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA--KKG 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
483-695 |
5.73e-62 |
|
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: 204.54 E-value: 5.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGY 562
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAGTLRDNLvsgaryvddemvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQ 695
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
484-707 |
3.65e-61 |
|
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: 205.08 E-value: 3.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQ-QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGY 562
Cdd:cd03249 2 EFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
483-700 |
1.12e-60 |
|
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: 203.87 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGY 562
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQG 218
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
280-708 |
1.42e-60 |
|
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: 213.79 E-value: 1.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 280 SLTLASLIDLPFTLIILVVIA--MLGGHLVWIPIIAFPLaLGIGHMLQKpLTATLERTMAlgaERQSSLIETLAGLDAVK 357
Cdd:TIGR02204 137 SMALRNALMCIGGLIMMFITSpkLTSLVLLAVPLVLLPI-LLFGRRVRK-LSRESQDRIA---DAGSYAGETLGAIRTVQ 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 358 VNNAESERQYQWEQTIGT---LSRLELRVKVLSgLAMNITLLIQQVAGvaMIIFGVYQIIDGALSMGGLVACYMLSGRAL 434
Cdd:TIGR02204 212 AFGHEDAERSRFGGAVEKayeAARQRIRTRALL-TAIVIVLVFGAIVG--VLWVGAHDVIAGKMSAGTLGQFVFYAVMVA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 435 GPLAQLSGLLTRYQQAKVTMvsvDQMMELPQERNYDERPLSRKAL----QGAMTFREVDFTYPNQQN-LALRGINLNVRA 509
Cdd:TIGR02204 289 GSIGTLSEVWGELQRAAGAA---ERLIELLQAEPDIKAPAHPKTLpvplRGEIEFEQVNFAYPARPDqPALDGLNLTVRP 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 510 GEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEM 589
Cdd:TIGR02204 366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 590 VLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN 669
Cdd:TIGR02204 446 VEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG 525
|
410 420 430
....*....|....*....|....*....|....*....
gi 814585811 670 KTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:TIGR02204 526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
485-712 |
8.39e-59 |
|
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: 198.61 E-value: 8.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYpNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVA 564
Cdd:cd03253 3 FENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 QDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 645 DEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEalKKG 712
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA--KGG 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
481-701 |
1.37e-55 |
|
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: 189.24 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 481 GAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNI 560
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLAGTLRDNLVSGARYvDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPP 640
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEY-SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 641 ILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGP 701
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
260-707 |
3.73e-55 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 201.10 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 260 RVGSFAQNIHEF--QGMRDFLTSLTLaslidlpftLIILVVIAMLGG-HLVWIPIIAFPLALGIGHMLQKPLTATLERTM 336
Cdd:TIGR00958 263 RLSSDTQTMSRSlsLNVNVLLRNLVM---------LLGLLGFMLWLSpRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 337 ALGAERQSSLIETLAGLDAVK---VNNAESERQYQWEQTIGTLSRLELRVKVLSglaMNITLLIQQVAGVAMIIFGVYQI 413
Cdd:TIGR00958 334 EAVAKANQVAEEALSGMRTVRsfaAEEGEASRFKEALEETLQLNKRKALAYAGY---LWTTSVLGMLIQVLVLYYGGQLV 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 414 IDGALSMGGLVAcYMLSGRALGP-LAQLSGLLTRYQQA-----KVtMVSVDQMMELPQERNYdeRPlsrKALQGAMTFRE 487
Cdd:TIGR00958 411 LTGKVSSGNLVS-FLLYQEQLGEaVRVLSYVYSGMMQAvgaseKV-FEYLDRKPNIPLTGTL--AP---LNLEGLIEFQD 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNL-ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQD 566
Cdd:TIGR00958 484 VSFSYPNRPDVpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:TIGR00958 564 PVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 647 PTSAMDNTGEERLKQRLQSviENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:TIGR00958 644 ATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
169-454 |
4.86e-54 |
|
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: 187.71 E-value: 4.86e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 169 ADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFER 248
Cdd:cd18588 5 GEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 249 IVGMAMKVRPAR-VGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHMLQKP 327
Cdd:cd18588 85 LLRLPLSYFESRqVGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 328 LTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMII 407
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILW 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 814585811 408 FGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTM 454
Cdd:cd18588 245 FGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSV 291
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
145-696 |
1.10e-53 |
|
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: 195.04 E-value: 1.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 145 TSGTLIPRARSWFRDTLKRSRWLYADAIAASLVINLIALAAPLFVMNVYDRVV-PNQATATLWMLAIGICGAY----LFD 219
Cdd:COG5265 12 APPRLDLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDaLLSGAAALLVVPVGLLLAYgllrLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 220 LLLKSLRSLCLDLAGKKTDLIISATLFERIVGMAMKV---RpaRVGSFAQNIHefQGMR--DFLTSLTLAS----LIDLP 290
Cdd:COG5265 92 VLFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFhleR--QTGGLSRDIE--RGTKgiEFLLRFLLFNilptLLEIA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 291 FTLIILVViaMLGGHLVWIPIIAfpLALGIGHMLqkplTAT-----LERTM-ALGAERQSSLIETLAGLDAVKVNNAES- 363
Cdd:COG5265 168 LVAGILLV--KYDWWFALITLVT--VVLYIAFTV----VVTewrtkFRREMnEADSEANTRAVDSLLNYETVKYFGNEAr 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 364 -ERQYQweqtiGTLSRLEL-RVKVLSGLAM-NITL-LIQQVAGVAMIIFGVYQIIDGALSMGGLVA--CYMLSgralgpL 437
Cdd:COG5265 240 eARRYD-----EALARYERaAVKSQTSLALlNFGQaLIIALGLTAMMLMAAQGVVAGTMTVGDFVLvnAYLIQ------L 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 438 AQ-LSGLLTRYQQAKVTMVSVDQMMEL------PQERNyDERPLSRKalQGAMTFREVDFTY-PNQQnlALRGINLNVRA 509
Cdd:COG5265 309 YIpLNFLGFVYREIRQALADMERMFDLldqppeVADAP-DAPPLVVG--GGEVRFENVSFGYdPERP--ILKGVSFEVPA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 510 GEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEM 589
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEE 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 590 VLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN 669
Cdd:COG5265 464 VEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG 543
|
570 580 590
....*....|....*....|....*....|
gi 814585811 670 KTVILVTHRaslLSLV---DRLLVIDRGQI 696
Cdd:COG5265 544 RTTLVIAHR---LSTIvdaDEILVLEAGRI 570
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
165-691 |
2.04e-52 |
|
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: 189.81 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLfdllLKSLRSLCLDLAGKKTDLIISAT 244
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLL----LRALLGWLQERAAARAAAAVKSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 245 LFERIVGMAMKVRPARV-----GSFAQNIHEfqGMRD-------FLTSLTLASLIdlpfTLIILVVIAML-----GGHLV 307
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLqgrpsGELATLALE--GVEAldgyfarYLPQLVLAVIV----PLAILAAVFPQdwisgLILLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 308 WIPIIAFPLALgIGHMLQKpltATLERTMALgaERQSS-LIETLAGLDAVKVNNA---------ESERQYQwEQTIGTLs 377
Cdd:TIGR02857 153 TAPLIPIFMIL-IGWAAQA---AARKQWAAL--SRLSGhFLDRLRGLPTLKLFGRakaqaaairRSSEEYR-ERTMRVL- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 378 rlelRVKVLSGLAMNITLLIQqVAGVAMIIfGVyQIIDGALSMGGLVACYMLSGRALGPLAQLSgllTRYQQAKVTMVSV 457
Cdd:TIGR02857 225 ----RIAFLSSAVLELFATLS-VALVAVYI-GF-RLLAGDLDLATGLFVLLLAPEFYLPLRQLG---AQYHARADGVAAA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 458 DQMMELPQERnydERPLSRKALQGA-----MTFREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVG 532
Cdd:TIGR02857 295 EALFAVLDAA---PRPLAGKAPVTAapassLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 533 LYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYEL 612
Cdd:TIGR02857 371 FVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDT 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 613 QVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVI 691
Cdd:TIGR02857 451 PIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
379-700 |
9.65e-51 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 186.71 E-value: 9.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 379 LELRVKVLS--GLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVS 456
Cdd:PRK13657 229 LAAQMPVLSwwALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 457 VDQMMELPQERN--YDERPLSRkaLQGAMTFREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLY 534
Cdd:PRK13657 309 FFEVEDAVPDVRdpPGAIDLGR--VKGAVEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 535 QPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQV 614
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 615 GERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRG 694
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
....*.
gi 814585811 695 QILADG 700
Cdd:PRK13657 546 RVVESG 551
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
165-454 |
4.84e-50 |
|
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: 176.94 E-value: 4.84e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISAT 244
Cdd:cd18783 1 KRLFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 245 LFERIVGMAMKV---RPArvGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIpIIAFPLALGIG 321
Cdd:cd18783 81 TFDRLLSLPIDFferTPA--GVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALV-VLAFSALIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 322 HMLQKPLTAT-LERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQV 400
Cdd:cd18783 158 ILAFLPPFRRrLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 401 AGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTM 454
Cdd:cd18783 238 MTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSV 291
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
474-696 |
1.03e-49 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 173.81 E-value: 1.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 474 LSRKALQGAMTFREVDFTYPNQQN-LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQID 552
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 553 VSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALA 632
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814585811 633 RALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
485-711 |
1.36e-49 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 173.29 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVA 564
Cdd:COG1122 3 LENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 Q--DIQLLAGTLRDNLVSGAR---YVDDEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALL 636
Cdd:COG1122 82 QnpDDQLFAPTVEEDVAFGPEnlgLPREEIrerVEEALELVGLEHLADRPP-----------HELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 637 LNPPILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHRASLL-SLVDRLLVIDRGQILADGPKAAVM---EALKK 711
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNkEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFsdyELLEE 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
436-707 |
4.57e-48 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 178.67 E-value: 4.57e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 436 PLAQLSGLLTRYQQAKVTMVSVDQMMELPQERNYDERPLSRkaLQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGI 515
Cdd:PRK11176 297 PLKSLTNVNAQFQRGMAACQTLFAILDLEQEKDEGKRVIER--AKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVAL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 516 IGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLV--SGARYVDDEmVLQA 593
Cdd:PRK11176 375 VGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAyaRTEQYSREQ-IEEA 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 594 AELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVI 673
Cdd:PRK11176 454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
250 260 270
....*....|....*....|....*....|....
gi 814585811 674 LVTHRASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:PRK11176 534 VIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| Peptidase_C39_likeD |
cd02421 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
18-138 |
9.83e-48 |
|
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: 164.34 E-value: 9.83e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 18 HDDPLLDGLLTLCSLHYKPASRAMLTTGLPLAAQRLSAELLPRAAARAGLQGRLLQRKLEQIPSIALPAMLLLKEGRSAV 97
Cdd:cd02421 4 RDDPLLDCLVLLARQFGKPASRDSLVAGLPLDDGRLSPALFPRAAARAGLSARVVRRPLDAIPTLLLPAILLLKNGRACV 83
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 814585811 98 LLGWEGDTARLLLSESDGGEVQVSRETLSQDYSGRVFFAQP 138
Cdd:cd02421 84 LLGVDDGHARILDPESGGGEVEISLEELEEEYSGYAIFVKP 124
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
283-678 |
1.01e-47 |
|
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: 176.78 E-value: 1.01e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 283 LASLIDLPFtLIILVVIAMLGGHLVwiPIIAFPLAlgighmlqkpltATLERTMALG-AERQSSLIETLAGLDAVKVNNA 361
Cdd:TIGR02868 147 AIAVLSVPA-ALILAAGLLLAGFVA--PLVSLRAA------------RAAEQALARLrGELAAQLTDALDGAAELVASGA 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 362 ESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLS 441
Cdd:TIGR02868 212 LPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 442 GLLTRYQQAKVTMVSVDQMMELPQERNYDERPLSRKALQGAMT--FREVDFTYPnQQNLALRGINLNVRAGEKIGIIGRS 519
Cdd:TIGR02868 292 AAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTleLRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPS 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 520 GSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGV 599
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGL 450
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 600 HEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHR 678
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
486-696 |
1.02e-47 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 166.24 E-value: 1.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQ 565
Cdd:cd03246 4 ENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 DIQLLAGTLRDNLvsgaryvddemvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNPPILLLD 645
Cdd:cd03246 84 DDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 814585811 646 EPTSAMDNTGEERLKQRLQSV-IENKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
296-700 |
4.13e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 175.78 E-value: 4.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 296 LVVIAMLGGHLVWIPIiafPLALGIG--------------HMLQKPLTATLertMALGAERQSSLIETLAGLDAVKVNNA 361
Cdd:PRK11160 145 LVVILVLTIGLSFFDL---TLALTLGgillllllllpllfYRLGKKPGQDL---THLRAQYRVQLTEWLQGQAELTLFGA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 362 ESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVyQIIDGALSMGGLVA----CYMLSGRALGPL 437
Cdd:PRK11160 219 EDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAA-GGVGGNAQPGALIAlfvfAALAAFEALMPV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 438 A----QLSGLLTRYQQakvtmvsVDQMMELPQERNYDERPlSRKALQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKI 513
Cdd:PRK11160 298 AgafqHLGQVIASARR-------INEITEQKPEVTFPTTS-TAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKV 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 514 GIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEM---V 590
Cdd:PRK11160 370 ALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEAlieV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 591 LQAAELAGVHEfarlHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENK 670
Cdd:PRK11160 450 LQQVGLEKLLE----DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK 525
|
410 420 430
....*....|....*....|....*....|
gi 814585811 671 TVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:PRK11160 526 TVLMITHRLTGLEQFDRICVMDNGQIIEQG 555
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
503-700 |
5.02e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 173.11 E-value: 5.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGL--YQpdsGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVS 580
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 581 GARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLK 660
Cdd:PRK11174 446 GNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 814585811 661 QRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
171-452 |
1.68e-45 |
|
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: 164.31 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18586 7 VGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAMKVRPArvGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHMLQKPLTA 330
Cdd:cd18586 87 ELPLESRPS--GYWQQLLRDLDTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 331 TLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGV 410
Cdd:cd18586 165 PLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGA 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 814585811 411 YQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKV 452
Cdd:cd18586 245 YLVIDGELTIGALIAASILSGRALAPIDQLVGAWKQLSAARQ 286
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
485-695 |
9.16e-43 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 153.78 E-value: 9.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVA 564
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 Q--DIQLLAGTLRDNLVSGAR---YVDDEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALL 636
Cdd:cd03225 82 QnpDDQFFGPTVEEEVAFGLEnlgLPEEEIeerVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 637 LNPPILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHRASLLS-LVDRLLVIDRGQ 695
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
483-700 |
3.38e-42 |
|
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: 151.31 E-value: 3.38e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrQIDVSELRHNIGY 562
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAGTLRDNLvsgaryvddemvlqaaelagvhefarlhpqgyelqvgerGQNLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
165-454 |
6.24e-42 |
|
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: 154.29 E-value: 6.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISAT 244
Cdd:cd18782 1 RRALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 245 LFERIVGMAMKV-RPARVGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHM 323
Cdd:cd18782 81 IIDHLLRLPLGFfDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 324 LQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGV 403
Cdd:cd18782 161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 814585811 404 AMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTM 454
Cdd:cd18782 241 LVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSL 291
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
405-708 |
1.91e-40 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 157.19 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 405 MIIFGVYQIidGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQER-NYDERPLSrkalQGAM 483
Cdd:PRK10790 268 LMLFGFSAS--GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQyGNDDRPLQ----SGRI 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQnLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYV 563
Cdd:PRK10790 342 DIDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLLAGTLRDNLVSGaRYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILL 643
Cdd:PRK10790 421 QQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 644 LDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
165-452 |
5.34e-40 |
|
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: 148.75 E-value: 5.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISAT 244
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 245 LFERIVGMAMKV---RpaRVGSF------AQNIhefqgmRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFP 315
Cdd:cd18570 81 YFKHLLKLPLSFfetR--KTGEIisrfndANKI------REAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 316 LALGIGHMLQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITL 395
Cdd:cd18570 153 LYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 396 LIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKV 452
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKV 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
485-695 |
1.13e-38 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 142.22 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYP---NQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqidvselrhNIG 561
Cdd:cd03250 3 VEDASFTWDsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAGTLRDNLVSGARYvDDEM---VLQAAELagVHEFARLhPQGYELQVGERGQNLSGGQRQNVALARALLLN 638
Cdd:cd03250 70 YVSQEPWIQNGTIRENILFGKPF-DEERyekVIKACAL--EPDLEIL-PDGDLTEIGEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 639 PPILLLDEPTSAMD-NTGEERLKQRLQSVI-ENKTVILVTHRASLLSLVDRLLVIDRGQ 695
Cdd:cd03250 146 ADIYLLDDPLSAVDaHVGRHIFENCILGLLlNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
499-696 |
2.40e-37 |
|
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: 138.70 E-value: 2.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNL 578
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARYVDDEmvLQAAelagvhefarlhpqgyeLQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEER 658
Cdd:cd03369 103 DPFDEYSDEE--IYGA-----------------LRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 814585811 659 LKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:cd03369 164 IQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
480-702 |
5.80e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 139.74 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 480 QGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHN 559
Cdd:PRK13632 5 SVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 IGYVAQ--DIQLLAGTLRDNLVSG---ARYVDDEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVAL 631
Cdd:PRK13632 85 IGIIFQnpDNQFIGATVEDDIAFGlenKKVPPKKMkdiIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814585811 632 ARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLSLVDRLLVIDRGQILADG-PK 702
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGkPK 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
472-708 |
8.36e-37 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 148.94 E-value: 8.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 472 RPLSRKALQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQI 551
Cdd:TIGR00957 1274 APPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI 1353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 552 DVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEmVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVAL 631
Cdd:TIGR00957 1354 GLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEE-VWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 632 ARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
485-696 |
9.58e-37 |
|
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: 137.24 E-value: 9.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQN--LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL----RH 558
Cdd:cd03255 3 LKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 559 NIGYVAQDIQLLAG-TLRDN-----LVSGARYVDD-EMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVAL 631
Cdd:cd03255 83 HIGFVFQSFNLLPDlTALENvelplLLAGVPKKERrERAEELLERVGLGDRLNHYP-----------SELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 632 ARALLLNPPILLLDEPTSAMD-NTGEE--RLKQRLQSViENKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDsETGKEvmELLRELNKE-AGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
489-696 |
1.87e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.10 E-value: 1.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQ 568
Cdd:COG4619 5 GLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 569 LLAGTLRDNLVSGARYVDDEMVLQAAELAgvheFARLH-PQGY-ELQVgergQNLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:COG4619 85 LWGGTVRDNLPFPFQLRERKFDRERALEL----LERLGlPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 647 PTSAMDntgeERLKQRLQSVI------ENKTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:COG4619 157 PTSALD----PENTRRVEELLreylaeEGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
165-454 |
5.96e-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: 137.31 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISAT 244
Cdd:cd18568 1 RKLLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 245 LFERIVGMAMKVRPAR-VGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHM 323
Cdd:cd18568 81 FYKHLLSLPLSFFASRkVGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 324 LQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGV 403
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 814585811 404 AMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTM 454
Cdd:cd18568 241 AVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISV 291
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
484-709 |
6.19e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 135.58 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYV 563
Cdd:COG1131 2 EVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLLAG-TLRDNLVSGARY------VDDEMVLQAAELAGVHEFARlhpqgyelqvgERGQNLSGGQRQNVALARALL 636
Cdd:COG1131 79 PQEPALYPDlTVRENLRFFARLyglprkEARERIDELLELFGLTDAAD-----------RKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 637 LNPPILLLDEPTSAMDNTGEERLKQRLQS-VIENKTVILVTHrasLLS----LVDRLLVIDRGQILADGPKAAVMEAL 709
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTH---YLEeaerLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
482-699 |
1.03e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYP--NQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL--- 556
Cdd:COG1136 4 LLELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 557 -RHNIGYVAQDIQLLAG-TLRDN-----LVSGA-RYVDDEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQN 628
Cdd:COG1136 84 rRRHIGFVFQFFNLLPElTALENvalplLLAGVsRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814585811 629 VALARALLLNPPILLLDEPTSAMD-NTGEERLKQrLQSVIE--NKTVILVTHRASLLSLVDRLLVIDRGQILAD 699
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDsKTGEEVLEL-LRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
490-701 |
8.95e-35 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 132.32 E-value: 8.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 490 FTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RHNIGYVAQD 566
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaRRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQLLAG-TLRDN------LVSGARYVDDEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNP 639
Cdd:cd03258 91 FNLLSSrTVFENvalpleIAGVPKAEIEERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 640 PILLLDEPTSAMD-NTGEERLkQRLQSVieNK----TVILVTHRASLL-SLVDRLLVIDRGQILADGP 701
Cdd:cd03258 160 KVLLCDEATSALDpETTQSIL-ALLRDI--NRelglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGT 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
484-706 |
2.19e-34 |
|
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: 131.27 E-value: 2.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYV 563
Cdd:cd03295 2 EFENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLLAG-TLRDNLV--------SGARYvdDEMVLQAAELAGV--HEFARLHPqgyelqvgergQNLSGGQRQNVALA 632
Cdd:cd03295 81 IQQIGLFPHmTVEENIAlvpkllkwPKEKI--RERADELLALVGLdpAEFADRYP-----------HELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 633 RALLLNPPILLLDEPTSAMDNTGEERLKQ---RLQSVIeNKTVILVTHRA-SLLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEefkRLQQEL-GKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
482-708 |
2.34e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.36 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYpnQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQidvseLRHNIG 561
Cdd:COG1121 6 AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG---TLRDnLVSGARY-----------VDDEMVLQAAELAGVHEFARLhpqgyelQVGErgqnLSGGQRQ 627
Cdd:COG1121 79 YVPQRAEVDWDfpiTVRD-VVLMGRYgrrglfrrpsrADREAVDEALERVGLEDLADR-------PIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 628 NVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTH-RASLLSLVDRLLVIDRGQIlADGPKAAV 705
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHdLGAVREYFDRVLLLNRGLV-AHGPPEEV 225
|
...
gi 814585811 706 MEA 708
Cdd:COG1121 226 LTP 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
484-708 |
3.51e-34 |
|
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: 137.34 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD---SGSLLVDGVDIRQIDVSELRHNI 560
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQD--IQLLAGTLRDNLVSGARYVD------DEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALA 632
Cdd:COG1123 86 GMVFQDpmTQLNPVTVGDQIAEALENLGlsraeaRARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 633 RALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLS-LVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAeIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
484-716 |
4.93e-34 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 131.42 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTY----PNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQ---IDVSEL 556
Cdd:TIGR04521 2 KLKNVSYIYqpgtPFEKK-ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 557 RHNIGYVAQ--DIQLLAGT-LRD------NL-VSGARYvdDEMVLQAAELAGVHEfarlhpqgyelQVGERGQ-NLSGGQ 625
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLFEETvYKDiafgpkNLgLSEEEA--EERVKEALELVGLDE-----------EYLERSPfELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 626 RQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVI--ENKTVILVTHRAS-LLSLVDRLLVIDRGQILADGPK 702
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkeKGLTVILVTHSMEdVAEYADRVIVMHKGKIVLDGTP 227
|
250
....*....|....*..
gi 814585811 703 AAVM---EALKKGQISV 716
Cdd:TIGR04521 228 REVFsdvDELEKIGLDV 244
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
483-700 |
1.18e-33 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 128.41 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqIDVSELRHNIGY 562
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAG-TLRDNLVSG--ARYVD----DEMVLQAAELAGVHEFARLHPQGyelqvgergqnLSGGQRQNVALARAL 635
Cdd:cd03259 77 VFQDYALFPHlTVAENIAFGlkLRGVPkaeiRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 636 LLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN--KTVILVTH-RASLLSLVDRLLVIDRGQILADG 700
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
484-708 |
1.25e-33 |
|
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: 135.80 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYP---NQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQI---DVSELR 557
Cdd:COG1123 262 EVRNLSKRYPvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 558 HNIGYVAQD-----------IQLLAGTLRDNLVSGARYVdDEMVLQAAELAGVH-EFARLHPqgYElqvgergqnLSGGQ 625
Cdd:COG1123 342 RRVQMVFQDpysslnprmtvGDIIAEPLRLHGLLSRAER-RERVAELLERVGLPpDLADRYP--HE---------LSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 626 RQNVALARALLLNPPILLLDEPTSAMDNTGE-------ERLKQRLqsvieNKTVILVTHRaslLSLV----DRLLVIDRG 694
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQaqilnllRDLQREL-----GLTYLFISHD---LAVVryiaDRVAVMYDG 481
|
250
....*....|....
gi 814585811 695 QILADGPKAAVMEA 708
Cdd:COG1123 482 RIVEDGPTEEVFAN 495
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
500-702 |
1.99e-33 |
|
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: 128.39 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRH---NIGYVAQDIQLLAG-TLR 575
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrrRMGMLFQSGALFDSlTVF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSGARY-------VDDEMVLQAAELAGVHEFARLHPqgyelqvGErgqnLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:cd03261 96 ENVAFPLREhtrlseeEIREIVLEKLEAVGLRGAEDLYP-------AE----LSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 649 SAMD--NTGE-ERLKQRLQSVIeNKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPK 702
Cdd:cd03261 165 AGLDpiASGViDDLIRSLKKEL-GLTSIMVTHDlDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
488-710 |
4.13e-33 |
|
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: 128.00 E-value: 4.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDI 567
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 -------QLLAGTLRDNLVSGARYVDDEMVLQAAELAGVH-EFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNP 639
Cdd:COG1124 89 yaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYP-----------HQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 640 PILLLDEPTSAMD--NTGE-----ERLKQRlqsviENKTVILVTHRASLLS-LVDRLLVIDRGQILADGPKAAVMEALK 710
Cdd:COG1124 158 ELLLLDEPTSALDvsVQAEilnllKDLREE-----RGLTYLFVSHDLAVVAhLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
500-649 |
4.93e-33 |
|
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: 124.30 E-value: 4.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAG-TLRDNL 578
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 579 VSGARYVDDEMVLQAAELAGVHEFARLHPQGYELqVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTS 649
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRP-VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
482-706 |
9.31e-33 |
|
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: 127.08 E-value: 9.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIG 561
Cdd:COG1120 1 MLEAENLSVGYGGRP--VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG-TLRDnLVSGARY-----------VDDEMVLQAAELAGVHEFArlhpqgyelqvgERG-QNLSGGQRQN 628
Cdd:COG1120 79 YVPQEPPAPFGlTVRE-LVALGRYphlglfgrpsaEDREAVEEALERTGLEHLA------------DRPvDELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 629 VALARALLLNPPILLLDEPTSAMDntgeerLKQRLQ--------SVIENKTVILVTH---RASLLSlvDRLLVIDRGQIL 697
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLD------LAHQLEvlellrrlARERGRTVVMVLHdlnLAARYA--DRLVLLKDGRIV 217
|
....*....
gi 814585811 698 ADGPKAAVM 706
Cdd:COG1120 218 AQGPPEEVL 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
485-704 |
1.05e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 125.94 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQnLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQI---DVSELRHNIG 561
Cdd:COG2884 4 FENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG-TLRDNL-----VSGA-RYVDDEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARA 634
Cdd:COG2884 83 VVFQDFRLLPDrTVYENValplrVTGKsRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814585811 635 LLLNPPILLLDEPTSAMD-NTGEE--RLKQRLQSVieNKTVILVTHRASLLSLVD-RLLVIDRGQILADGPKAA 704
Cdd:COG2884 152 LVNRPELLLADEPTGNLDpETSWEimELLEEINRR--GTTVLIATHDLELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
409-707 |
1.94e-32 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 132.91 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 409 GVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERNYDERPLSrkALQGAMTFREV 488
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVP--EGRGELDVNIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQ 568
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 569 LLAGTLRDNLVSGARYVDDEMVLQAAELAGVHE-FARLhPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDdILRL-PQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 648 TSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
484-695 |
3.25e-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: 122.35 E-value: 3.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYV 563
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQdiqllagtlrdnlvsgaryvddemvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNPPILL 643
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 644 LDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHRASLLS-LVDRLLVIDRGQ 695
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
488-707 |
4.95e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 4.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQ-- 565
Cdd:PRK13635 11 ISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQnp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 DIQLLAGTLRDNLVSG------ARyvdDEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALL 636
Cdd:PRK13635 91 DNQFVGATVQDDVAFGlenigvPR---EEMverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 637 LNPPILLLDEPTSAMDNTGEE-------RLKQRlqsviENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRRevletvrQLKEQ-----KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
500-708 |
8.18e-32 |
|
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: 123.94 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RHNIGYVAQDIQLLAG-TLR 575
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRRIGMLFQGGALFDSlTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSGARYVDD-------EMVLQAAELAGVHEFARLHPqgyelqvGErgqnLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:COG1127 101 ENVAFPLREHTDlseaeirELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 649 S-----AMDNTGE--ERLKQRLqsvieNKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:COG1127 170 AgldpiTSAVIDEliRELRDEL-----GLTSVVVTHDlDSAFAIADRVAVLADGKIIAEGTPEELLAS 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
379-702 |
8.64e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 133.18 E-value: 8.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 379 LELRVKVLSGLamnitlLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALgplaqLSGLLTRYQQAKVTMVSVD 458
Cdd:PLN03232 1136 LTIRLETLGGV------MIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTL-----LSGVLRQASKAENSLNSVE 1204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 459 QM---MELPQERN---YDERPLSRKALQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVG 532
Cdd:PLN03232 1205 RVgnyIDLPSEATaiiENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR 1284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 533 LYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYvDDEMVLQAAELAGVHEFARLHPQGYEL 612
Cdd:PLN03232 1285 IVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRNPFGLDA 1363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 613 QVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVID 692
Cdd:PLN03232 1364 EVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLS 1443
|
330
....*....|.
gi 814585811 693 RGQILA-DGPK 702
Cdd:PLN03232 1444 SGQVLEyDSPQ 1454
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
482-699 |
1.88e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 123.66 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQQN--LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDirqidVSELRHN 559
Cdd:COG1116 7 ALELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 IGYVAQDIQLLA-GTLRDNLVSGARYVD------DEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALA 632
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGvpkaerRERARELLELVGLAGFEDAYPH-----------QLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 633 RALLLNPPILLLDEPTSAMDntgeERLKQRLQSVI------ENKTVILVTHraSL---LSLVDRLLVIDR--GQILAD 699
Cdd:COG1116 151 RALANDPEVLLMDEPFGALD----ALTRERLQDELlrlwqeTGKTVLFVTH--DVdeaVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
488-700 |
3.55e-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: 121.84 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQID---VSELRHNIGYVA 564
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 QD-----------IQLLAGTLRDNLVSGARYVDDEMVLQAAELAG-VHEFARLHPqgYElqvgergqnLSGGQRQNVALA 632
Cdd:cd03257 89 QDpmsslnprmtiGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlPEEVLNRYP--HE---------LSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 633 RALLLNPPILLLDEPTSAMDNTGEE---RLKQRLQSVIeNKTVILVTHRASLLS-LVDRLLVIDRGQILADG 700
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAqilDLLKKLQEEL-GLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
486-696 |
6.20e-31 |
|
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: 119.04 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYVAQ 565
Cdd:cd03230 4 RNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 DIQLLAG-TLRDNLvsgaryvddemvlqaaelagvhefarlhpqgyelqvgergqNLSGGQRQNVALARALLLNPPILLL 644
Cdd:cd03230 81 EPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 645 DEPTSAMDNTGEERLKQRLQS-VIENKTVILVTHR-ASLLSLVDRLLVIDRGQI 696
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
483-699 |
9.15e-31 |
|
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: 120.27 E-value: 9.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPN--QQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRqidvsELRHNI 560
Cdd:cd03293 1 LEVRNVSKTYGGggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLA-GTLRDNLVSGARYVD------DEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALAR 633
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGvpkaeaRERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 634 ALLLNPPILLLDEPTSAMDntgeERLKQRLQSVI------ENKTVILVTH---RASLLSlvDRLLVIDR--GQILAD 699
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALD----ALTREQLQEELldiwreTGKTVLLVTHdidEAVFLA--DRVVVLSArpGRIVAE 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
484-714 |
1.18e-30 |
|
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: 120.73 E-value: 1.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYpnQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRqIDVSELRHNIGYV 563
Cdd:COG4555 3 EVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLLAG-TLRDNLvsgaRYV-------DDEMVLQAAELagVHEFarlhpqGYELQVGERGQNLSGGQRQNVALARAL 635
Cdd:COG4555 80 PDERGLYDRlTVRENI----RYFaelyglfDEELKKRIEEL--IELL------GLEEFLDRRVGELSTGMKKKVALARAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 636 LLNPPILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHRASLLS-LVDRLLVIDRGQILADGPKAAVMEALKKGQ 713
Cdd:COG4555 148 VHDPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEaLCDRVVILHKGKVVAQGSLDELREEIGEEN 227
|
.
gi 814585811 714 I 714
Cdd:COG4555 228 L 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
485-705 |
1.60e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 120.55 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQqNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RHNIG 561
Cdd:COG3638 5 LRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQL----------LAGTL--RDNLVSGARYVDDEMVLQAAELagvheFARLHPQGYELQvgeRGQNLSGGQRQNV 629
Cdd:COG3638 84 MIFQQFNLvprlsvltnvLAGRLgrTSTWRSLLGLFPPEDRERALEA-----LERVGLADKAYQ---RADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 630 ALARALLLNPPILLLDEPTSAMD-NTGEE--RLKQRLQSViENKTVILVTHRASL-LSLVDRLLVIDRGQILADGPKAAV 705
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDpKTARQvmDLLRRIARE-DGITVVVNLHQVDLaRRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
496-708 |
2.03e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 119.71 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI--RQIDVSELRHNIGYVAQDIQL---L 570
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLfphL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 571 agTLRDNLVSGARYV----DDEMVLQAAEL---AGVHEFARLHPqgyelqvgerGQnLSGGQRQNVALARALLLNPPILL 643
Cdd:COG1126 93 --TVLENVTLAPIKVkkmsKAEAEERAMELlerVGLADKADAYP----------AQ-LSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 644 LDEPTSAMD--NTGE-----ERLKQrlqsviENKTVILVTH------RASllslvDRLLVIDRGQILADGPKAAVMEA 708
Cdd:COG1126 160 FDEPTSALDpeLVGEvldvmRDLAK------EGMTMVVVTHemgfarEVA-----DRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
483-695 |
5.51e-30 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 116.52 E-value: 5.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQ--IDVSELRHNI 560
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLAG-TLRDNLVSGaryvddemvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNP 639
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 640 PILLLDEPTSAMDNTGEERLKQRLQSVIEN--KTVILVTHR-ASLLSLVDRLLVIDRGQ 695
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDlDEAARLADRVVVLRDGK 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
485-701 |
6.57e-30 |
|
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: 118.05 E-value: 6.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLY-----QPDSGSLLVDGVDIR--QIDVSELR 557
Cdd:cd03260 3 LRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYdlDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 558 HNIGYVAQDIQLLAGTLRDNLVSGARYVD-------DEMVLQAAELAGVHEFA--RLHPQGyelqvgergqnLSGGQRQN 628
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGiklkeelDERVEEALRKAALWDEVkdRLHALG-----------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 629 VALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTH---RASLLSlvDRLLVIDRGQILADGP 701
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqQAARVA--DRTAFLLNGRLVEFGP 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
499-696 |
1.71e-29 |
|
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: 116.48 E-value: 1.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI--RQIDVSELRHNIGYVAQDIQLLAG-TLR 575
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPHlTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSGARYVDDEMVLQAAELA-------GVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:cd03262 95 ENITLAPIKVKGMSKAEAEERAlellekvGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 814585811 649 SAMD-NTGEERLKQRLQSVIENKTVILVTHRASLLSLV-DRLLVIDRGQI 696
Cdd:cd03262 164 SALDpELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
490-696 |
2.02e-29 |
|
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: 115.82 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 490 FTYPNQQNLaLRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQidvSELRHNIGYVAQDI-- 567
Cdd:cd03226 7 FSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 QLLAGTLRDNLVSGARYVDD-----EMVLQAAELAGVHEfarLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03226 83 QLFTDSVREELLLGLKELDAgneqaETVLKDLDLYALKE---RHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHRASLLSLV-DRLLVIDRGQI 696
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKVcDRVLLLANGAI 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
422-697 |
2.45e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 125.62 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 422 GLVACYMLSGRALgplaqLSGLLTRYQQAKVTMVSVDQM---MELPQERNY---DERPLSRKALQGAMTFREVDFTYPNQ 495
Cdd:PLN03130 1176 GLLLSYALNITSL-----LTAVLRLASLAENSLNAVERVgtyIDLPSEAPLvieNNRPPPGWPSSGSIKFEDVVLRYRPE 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLR 575
Cdd:PLN03130 1251 LPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVR 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSGARYVDDEMvLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTG 655
Cdd:PLN03130 1331 FNLDPFNEHNDADL-WESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 814585811 656 EERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQIL 697
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
486-696 |
4.08e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.53 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTY-PNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVA 564
Cdd:PRK13650 8 KNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 Q--DIQLLAGTLRDNLV-----SGARYVD-DEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALL 636
Cdd:PRK13650 88 QnpDNQFVGATVEDDVAfglenKGIPHEEmKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 637 LNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
482-700 |
5.03e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 117.21 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGS---LLVDGVDIRQIDVSELRH 558
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 559 NIGYVAQ--DIQLLAGTLRDNLVSGA--RYVD-DEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVA 630
Cdd:PRK13640 85 KVGIVFQnpDNQFVGATVGDDVAFGLenRAVPrPEMikiVRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 631 LARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENK--TVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
172-452 |
5.43e-29 |
|
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: 117.23 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 172 IAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIVG 251
Cdd:cd18555 8 LLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 252 MAMK---VRParVGSFAQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHMLQKPL 328
Cdd:cd18555 88 LPYSffeNRS--SGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 329 TATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIF 408
Cdd:cd18555 166 KKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 814585811 409 GVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKV 452
Cdd:cd18555 246 GAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKS 289
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
489-700 |
7.54e-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: 114.55 E-value: 7.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIdvselRHNIGYVAQ--- 565
Cdd:cd03235 4 DLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQrrs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 ----------DIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFArlhpqgyELQVGErgqnLSGGQRQNVALARAL 635
Cdd:cd03235 79 idrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 636 LLNPPILLLDEPTSAMDNTGEE---RLKQRLQSviENKTVILVTH-RASLLSLVDRLLVIDRGqILADG 700
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEdiyELLRELRR--EGMTILVVTHdLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
479-697 |
8.49e-29 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 115.78 E-value: 8.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 479 LQGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRH 558
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 559 NIGYVAQDIQLLAGTLRDNLVSGARYVDDEMvLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLN 638
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPECKCTDDRL-WEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 639 PPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQIL 697
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILV 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
497-714 |
1.16e-28 |
|
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: 114.74 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqIDVSELRHNIGYVAQDIQLLAG-TLR 575
Cdd:cd03299 12 EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI--TNLPPEKRDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSGARYV------DDEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPILLLDEPTS 649
Cdd:cd03299 90 KNIAYGLKKRkvdkkeIERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 650 AMDNTGEERLKQRLQSVIENK--TVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAVMEALKKGQI 714
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFgvTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
496-707 |
1.91e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIR--QIDVSELRHNIGYVAQDIQLLAG- 572
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 573 TLRDNLVSGARYVddemvlQAAELAGVHEFAR--LHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:PRK09493 93 TALENVMFGPLRV------RGASKEEAEKQARelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 651 MDntgeERLKQRLQSVI-----ENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAVME 707
Cdd:PRK09493 167 LD----PELRHEVLKVMqdlaeEGMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
278-700 |
2.33e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 122.39 E-value: 2.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 278 LTSLTLASLIDLPFTLIILVV-------IAMLGGHLVWIPIIafPLALGIGHMLQKPLTATLERTmalgAERQSSLIETL 350
Cdd:PLN03232 413 QIAEQLHGLWSAPFRIIVSMVllyqqlgVASLFGSLILFLLI--PLQTLIVRKMRKLTKEGLQWT----DKRVGIINEIL 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 351 AGLDAVKVnnaeserqYQWEQT----IGTLSRLEL----RVKVLSglAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGG 422
Cdd:PLN03232 487 ASMDTVKC--------YAWEKSfesrIQGIRNEELswfrKAQLLS--AFNSFILNSIPVVVTLVSFGVFVLLGGDLTPAR 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 423 LVACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMeLPQERNYDERPLSRKALQgAMTFREVDFTYPNQ-QNLALR 501
Cdd:PLN03232 557 AFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELL-LSEERILAQNPPLQPGAP-AISIKNGYFSWDSKtSKPTLS 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 502 GINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVdgvdirqidvseLRHNIGYVAQDIQLLAGTLRDNLVSG 581
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFG 702
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 582 ARYvDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMD-NTGEERLK 660
Cdd:PLN03232 703 SDF-ESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDaHVAHQVFD 781
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 814585811 661 QRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:PLN03232 782 SCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG 821
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
484-705 |
2.36e-28 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 113.82 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RHNI 560
Cdd:cd03256 2 EVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQL----------LAGTL--RDNLVSGARYVDDEMVLQAAEL---AGVHEFARlhpqgyelqvgERGQNLSGGQ 625
Cdd:cd03256 81 GMIFQQFNLierlsvlenvLSGRLgrRSTWRSLFGLFPKEEKQRALAAlerVGLLDKAY-----------QRADQLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 626 RQNVALARALLLNPPILLLDEPTSAMDNTGEER----LKQRLQSviENKTVILVTHRASL-LSLVDRLLVIDRGQILADG 700
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQvmdlLKRINRE--EGITVIVSLHQVDLaREYADRIVGLKDGRIVFDG 227
|
....*
gi 814585811 701 PKAAV 705
Cdd:cd03256 228 PPAEL 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
489-700 |
3.43e-28 |
|
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: 111.37 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYvaqdiq 568
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 569 llagtlrdnlvsgaryvddemVLQAAELAGVHEFArlhpqgyelqvgERG-QNLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:cd03214 78 ---------------------VPQALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 648 TSAMDNTGEERLKQRLQSVI--ENKTVILVTH---RASLLSlvDRLLVIDRGQILADG 700
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLAreRGKTVVMVLHdlnLAARYA--DRVILLKDGRIVAQG 180
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
484-701 |
3.59e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.95 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYP--NQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RH 558
Cdd:COG1135 3 ELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 559 NIGYVAQDIQLLAG-TLRDNlvsgaryvddemVLQAAELAG---------VHEFARLhpqgyelqVG--ERGQ----NLS 622
Cdd:COG1135 83 KIGMIFQHFNLLSSrTVAEN------------VALPLEIAGvpkaeirkrVAELLEL--------VGlsDKADaypsQLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 623 GGQRQNVALARALLLNPPILLLDEPTSAMD-NTGEE------RLKQRLqsvieNKTVILVTH-----RasllSLVDRLLV 690
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDpETTRSildllkDINREL-----GLTIVLITHemdvvR----RICDRVAV 213
|
250
....*....|.
gi 814585811 691 IDRGQILADGP 701
Cdd:COG1135 214 LENGRIVEQGP 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
283-700 |
3.94e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.77 E-value: 3.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 283 LASLIDLPFTLIILVV-------IAMLGGHLVWIpiIAFPLALGIGHMLQKPLTATLERTmalgAERQSSLIETLAGLDA 355
Cdd:PLN03130 418 LHTLWSAPFRIIIAMVllyqqlgVASLIGSLMLV--LMFPIQTFIISKMQKLTKEGLQRT----DKRIGLMNEVLAAMDT 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 356 VKVnnaeserqYQWEQT----IGTLSRLEL----RVKVLSglAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACY 427
Cdd:PLN03130 492 VKC--------YAWENSfqskVQTVRDDELswfrKAQLLS--AFNSFILNSIPVLVTVVSFGVFTLLGGDLTPARAFTSL 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 428 MLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMMeLPQERNYDERPLSRKALQgAMTFREVDFTY-PNQQNLALRGINLN 506
Cdd:PLN03130 562 SLFAVLRFPLFMLPNLITQAVNANVSLKRLEELL-LAEERVLLPNPPLEPGLP-AISIKNGYFSWdSKAERPTLSNINLD 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVdgvdirqidvseLRHNIGYVAQDIQLLAGTLRDNLVSGARYvD 586
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPF-D 706
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 587 DEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMD-NTGEERLKQRLQS 665
Cdd:PLN03130 707 PERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDaHVGRQVFDKCIKD 786
|
410 420 430
....*....|....*....|....*....|....*
gi 814585811 666 VIENKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:PLN03130 787 ELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEG 821
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
485-706 |
4.37e-28 |
|
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: 113.64 E-value: 4.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYpnQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSG-SLLVDGVDIRQIDVSELRHNIGYV 563
Cdd:COG1119 6 LRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLL---AGTLRDNLVSGA-------RYVDDEMVLQAAELA---GVHEFArlhpqgyelqvGERGQNLSGGQRQNVA 630
Cdd:COG1119 84 SPALQLRfprDETVLDVVLSGFfdsiglyREPTDEQRERARELLellGLAHLA-----------DRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 631 LARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN--KTVILVTHRAS-LLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEeIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
485-708 |
5.07e-28 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 113.16 E-value: 5.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQI---DVSELRHNIG 561
Cdd:TIGR02315 4 VENLSKVYPNGKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRKLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG-TLRDNLVSGA------------RYV--DDEMVLQAAELAGVHEFARLhpqgyelqvgeRGQNLSGGQR 626
Cdd:TIGR02315 83 MIFQHYNLIERlTVLENVLHGRlgykptwrsllgRFSeeDKERALSALERVGLADKAYQ-----------RADQLSGGQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 627 QNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENK--TVILVTHRASL-LSLVDRLLVIDRGQILADGPKA 703
Cdd:TIGR02315 152 QRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLaKKYADRIVGLKAGEIVFDGAPS 231
|
....*
gi 814585811 704 AVMEA 708
Cdd:TIGR02315 232 ELDDE 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
500-704 |
7.01e-28 |
|
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: 112.53 E-value: 7.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL----RHNIGYVAQDIQLLAG-TL 574
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFQLLPTlTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNlvsgaryvddemVLQAAELAGVHE-FARLHpqgYELQ---VGER-----GQnLSGGQRQNVALARALLLNPPILLLD 645
Cdd:COG4181 108 LEN------------VMLPLELAGRRDaRARAR---ALLErvgLGHRldhypAQ-LSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 646 EPTSAMD-NTGE------ERLKQRLQSvienkTVILVTHRASLLSLVDRLLVIDRGQILADGPKAA 704
Cdd:COG4181 172 EPTGNLDaATGEqiidllFELNRERGT-----TLVLVTHDPALAARCDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
499-706 |
1.35e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 111.76 E-value: 1.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL-RHNIGYVAQDIQLLAG-TLRD 576
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGA-------------RYVDDEMVLQAAELAgvhEFARLHPQGYELqVGergqNLSGGQRQNVALARALLLNPPILL 643
Cdd:cd03219 95 NVMVAAqartgsglllaraRREEREARERAEELL---ERVGLADLADRP-AG----ELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 644 LDEPTSAMDNTGEERLKQRLQSVIE-NKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIRELRErGITVLLVEHDmDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
499-707 |
2.20e-27 |
|
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: 110.60 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQLLAG-TLRD 576
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGARYVDDEMVlqAAELAGVHE-FARLHpqgyELQvGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTG 655
Cdd:cd03224 95 NLLLGAYARRRAKR--KARLERVYElFPRLK----ERR-KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 656 EERLKQRLQSVIENK-TVILVTHRASL-LSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:cd03224 168 VEEIFEAIRELRDEGvTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
488-706 |
9.23e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.46 E-value: 9.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQID-VSELRHNIGYVAQ- 565
Cdd:PRK13644 7 VSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 -DIQLLAGTLRDNLVSGAryvdDEMVLQAAELAGVHEFArLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:PRK13644 86 pETQFVGRTVEEDLAFGP----ENLCLPPIEIRKRVDRA-LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 645 DEPTSAMDNTGEERLKQRLQSVIEN-KTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
171-452 |
1.30e-26 |
|
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: 110.33 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAMKVRPA-RVGSFAQNI-HEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGHMLQKPL 328
Cdd:cd07346 84 RLSLSFFDRnRTGDLMSRLtSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 329 TATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIF 408
Cdd:cd07346 164 RKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 814585811 409 GVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKV 452
Cdd:cd07346 244 GGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALA 287
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
510-700 |
2.61e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 107.38 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 510 GEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGV---DIRQ-IDVSELRHNIGYVAQDIQLLAG-TLRDNLVSGARY 584
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQYALFPHlNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 585 VDD-EMVLQAAELagvheFARLHPQgyelQVGERG-QNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQR 662
Cdd:cd03297 103 KRNrEDRISVDEL-----LDLLGLD----HLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 814585811 663 LQSVIE--NKTVILVTHRAS-LLSLVDRLLVIDRGQILADG 700
Cdd:cd03297 174 LKQIKKnlNIPVIFVTHDLSeAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
487-700 |
3.15e-26 |
|
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: 106.89 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 487 EVDFTYPNQQnlALRGINLNVRAGeKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRqIDVSELRHNIGYVAQD 566
Cdd:cd03264 5 NLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQLLAG-TLRDNL--------VSGARYvdDEMVLQAAELAGVHEFArlhpqgyelqvGERGQNLSGGQRQNVALARALLL 637
Cdd:cd03264 81 FGVYPNfTVREFLdyiawlkgIPSKEV--KARVDEVLELVNLGDRA-----------KKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 638 NPPILLLDEPTSAMDNtgEERLKQR--LQSVIENKTVILVTHRAS-LLSLVDRLLVIDRGQILADG 700
Cdd:cd03264 148 DPSILIVDEPTAGLDP--EERIRFRnlLSELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
499-711 |
6.04e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.21 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI--RQIDVSELRHNIGYVAQ--DIQLLAGTL 574
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQypEYQLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGARYV---DDEM---VLQAAELAGVHefarlhpqgYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:PRK13637 102 EKDIAFGPINLglsEEEIenrVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 649 SAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLS-LVDRLLVIDRGQILADGPKAAV---MEALKK 711
Cdd:PRK13637 173 AGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAkLADRIIVMNKGKCELQGTPREVfkeVETLES 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
482-705 |
7.01e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.80 E-value: 7.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqIDVS-ELRhNI 560
Cdd:COG3842 5 ALELENVSKRYGDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--TGLPpEKR-NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQL---LagTLRDNLVSG--ARYVD----DEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVAL 631
Cdd:COG3842 80 GMVFQDYALfphL--TVAENVAFGlrMRGVPkaeiRARVAELLELVGLEGLADRYPH-----------QLSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 632 ARALLLNPPILLLDEPTSAMDNtgeeRLKQRLQSVI------ENKTVILVTHR---AslLSLVDRLLVIDRGQILADGPK 702
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDA----KLREEMREELrrlqreLGITFIYVTHDqeeA--LALADRIAVMNDGRIEQVGTP 220
|
...
gi 814585811 703 AAV 705
Cdd:COG3842 221 EEI 223
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
499-701 |
8.75e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.12 E-value: 8.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RHNIGYVAQDIQLLAG-TL 574
Cdd:PRK11153 20 ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaRRQIGMIFQHFNLLSSrTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDN------LVSGARYVDDEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:PRK11153 100 FDNvalpleLAGTPKAEIKARVTELLELVGLSDKADRYPA-----------QLSGGQKQRVAIARALASNPKVLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 649 SAMDntgeerlKQRLQSVIE-----NK----TVILVTHRASLL-SLVDRLLVIDRGQILADGP 701
Cdd:PRK11153 169 SALD-------PATTRSILEllkdiNRelglTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
499-696 |
1.36e-25 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 105.88 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSElrHNIGYVAQDIQLLAG-TLRDN 577
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGARYVDDEMVLQAAELAG-VHEFARL-HPQGYElqvgERGQN-LSGGQRQNVALARALLLNPPILLLDEPTSAMDNT 654
Cdd:cd03296 95 VAFGLRVKPRSERPPEAEIRAkVHELLKLvQLDWLA----DRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 814585811 655 GEERLKQRLQSVIE--NKTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:cd03296 171 VRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRI 215
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
485-696 |
3.77e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 104.03 E-value: 3.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQnLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI---RQIDVSELRHNIG 561
Cdd:cd03292 3 FINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG-TLRDNLVSGARYVD------DEMVLQAAELAGVHEFARLHPQGyelqvgergqnLSGGQRQNVALARA 634
Cdd:cd03292 82 VVFQDFRLLPDrNVYENVAFALEVTGvppreiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 635 LLLNPPILLLDEPTSAMDNTGEERLKQRLQSVieNK---TVILVTHRASLL-SLVDRLLVIDRGQI 696
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKI--NKagtTVVVATHAKELVdTTRHRVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
500-705 |
7.94e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.06 E-value: 7.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI--------RQIDVSELRHNIGYVAQDIQLLA 571
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 G-TLRDNLVSGARYVDDEMVLQAAELaGVHEFARLHPQGYELQVGERgqnLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:PRK11264 99 HrTVLENIIEGPVIVKGEPKEEATAR-ARELLAKVGLAGKETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 651 MD-NTGEERLKQRLQSVIENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAV 705
Cdd:PRK11264 175 LDpELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGPAKAL 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
491-700 |
9.67e-25 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.97 E-value: 9.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 491 TYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYVAQ-DIQL 569
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQfDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 570 LAGTLRDNLVSGARyvddemvlqaaeLAGVHEF-ARLHPQGYELQVG------ERGQNLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03263 88 DELTVREHLRFYAR------------LKGLPKSeIKEEVELLLRVLGltdkanKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTH---RASLLSlvDRLLVIDRGQILADG 700
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdEAEALC--DRIAIMSDGKLRCIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
500-688 |
1.30e-24 |
|
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: 102.17 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYVAQDIQLLAG-TLRDNL 578
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARY----VDDEMVLQAAELAGVHEFARLhpqgyelqvgeRGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNT 654
Cdd:COG4133 97 RFWAALyglrADREAIDEALEAVGLAGLADL-----------PVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAA 165
|
170 180 190
....*....|....*....|....*....|....*
gi 814585811 655 GEERLKQRLQSVIEN-KTVILVTHRASLLSLVDRL 688
Cdd:COG4133 166 GVALLAELIAAHLARgGAVLLTTHQPLELAAARVL 200
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
499-706 |
1.33e-24 |
|
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: 103.58 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL-RHNIGYVAQDIQLLAG-TLRD 576
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGARYVDDEMVLQAAE--LAGVHEFARLHPQGYEL--QVG------ERGQNLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:COG0411 99 NVLVAAHARLGRGLLAALLrlPRARREEREARERAEELleRVGladradEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 647 PTSAMDNTGEERLKQRLQSV--IENKTVILVTHRASLL-SLVDRLLVIDRGQILADGPKAAVM 706
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLrdERGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGTPAEVR 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
499-696 |
1.51e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 102.33 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRqiDVSELRHNIGYVAQDIQLLAG-TLRDN 577
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYPHmTVYDN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGARYVD------DEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPILLLDEPTSAM 651
Cdd:cd03301 93 IAFGLKLRKvpkdeiDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 652 D-------NTGEERLKQRLQsvienKTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:cd03301 162 DaklrvqmRAELKRLQQRLG-----TTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
482-711 |
1.62e-24 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 103.14 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLY-----QPDSGSLLVDGVDI--RQIDVS 554
Cdd:TIGR00972 1 AIEIENLNLFYGEKE--ALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlvpgVRIEGKVLFDGQDIydKKIDVV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQDIQLLAGTLRDNLVSGARY-------VDDEMVLQAAELAGVHEFA--RLHPQGYelqvgergqNLSGGQ 625
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFPMSIYDNIAYGPRLhgikdkkELDEIVEESLKKAALWDEVkdRLHDSAL---------GLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 626 RQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTH---RASLLSlvDRLLVIDRGQILADGPK 702
Cdd:TIGR00972 150 QQRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHnmqQAARIS--DRTAFFYDGELVEYGPT 227
|
....*....
gi 814585811 703 AAVMEALKK 711
Cdd:TIGR00972 228 EQIFTNPKE 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
499-707 |
1.64e-24 |
|
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: 102.75 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL-RHNIGYVAQDIQLLAG-TLRD 576
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGARYVDDEMVLQAAeLAGVHE-FARLHpqgyELQvGERGQNLSGGQRQNVALARALLLNPPILLLDEPT-----SA 650
Cdd:COG0410 98 NLLLGAYARRDRAEVRAD-LERVYElFPRLK----ERR-RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSlglapLI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 651 MDNTGE--ERLKQrlqsviENKTVILVTHRASL-LSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:COG0410 172 VEEIFEiiRRLNR------EGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
496-700 |
1.89e-24 |
|
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: 102.06 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYVAQDIQLLAG-TL 574
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGARY------VDDEMVLQAAELAGVHEFArlhpqgyelqvGERGQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:cd03265 91 WENLYIHARLygvpgaERRERIDELLDFVGLLEAA-----------DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 649 SAMDNTGEERLKQRLQSVIE--NKTVILVTH---RASLLSlvDRLLVIDRGQILADG 700
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEefGMTILLTTHymeEAEQLC--DRVAIIDHGRIIAEG 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
398-695 |
2.04e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 398 QQVAGVAMIIFGVYQIIDGALSMGGLV----ACYMLSG------RALGPLAQLSGLLTRyqqakvtMVSVDQMMELPQER 467
Cdd:COG4178 276 GQLAVIFPILVAAPRYFAGEITLGGLMqaasAFGQVQGalswfvDNYQSLAEWRATVDR-------LAGFEEALEAADAL 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 468 NYDERPLSRKAlQGAMTFREVDFTYPNQQNLaLRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGsllvdgvd 547
Cdd:COG4178 349 PEAASRIETSE-DGALALEDLTLRTPDGRPL-LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------- 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 548 irQIDVSELRHnIGYVAQDIQLLAGTLRDNLV--SGARYVDDEMVLQAAELAGVHEFA-RLHpqgyelQVGERGQNLSGG 624
Cdd:COG4178 419 --RIARPAGAR-VLFLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAeRLD------EEADWDQVLSLG 489
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 625 QRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQ 695
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
486-708 |
3.95e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.46 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrQIDVSELRHNIGYVAQ 565
Cdd:COG1118 6 RNISKRFGSFT--LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 DIQL---------LAGTLRDNLVSGARyvDDEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALL 636
Cdd:COG1118 83 HYALfphmtvaenIAFGLRVRPPSKAE--IRARVEELLELVQLEGLADRYPS-----------QLSGGQRQRVALARALA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 637 LNPPILLLDEPTSAMDNtgeeRLKQRLQSVI------ENKTVILVTH-RASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:COG1118 150 VEPEVLLLDEPFGALDA----KVRKELRRWLrrlhdeLGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
281-707 |
4.72e-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: 108.49 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 281 LTLASLIDLPFTLIILVVIAMlggHLVWIPIIAFPLAlGIGHM-LQKPLTATLE--------RTMALGAERQSSLIETLA 351
Cdd:TIGR00957 429 MDLATYINMIWSAPLQVILAL---YFLWLNLGPSVLA-GVAVMvLMVPLNAVMAmktktyqvAHMKSKDNRIKLMNEILN 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 352 GLDAVKVnnaeserqYQWE----QTIGTLSRLELRVKVLSGLAMNITLLIQQVAG--VAMIIFGVYQIID--GALSMGGL 423
Cdd:TIGR00957 505 GIKVLKL--------YAWElaflDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPflVALITFAVYVTVDenNILDAEKA 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 424 VACYMLSGRALGPLAQLSGLLTRYQQAKVTMVSVDQMmeLPQERnYDERPLSRKALQ----GAMTFREVDFTYPNQQNLA 499
Cdd:TIGR00957 577 FVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIF--LSHEE-LEPDSIERRTIKpgegNSITVHNATFTWARDLPPT 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqidvselrhNIGYVAQDIQLLAGTLRDNLV 579
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENIL 720
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 580 SGA-----RYvddEMVLQAAELAGVHEfarLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNT 654
Cdd:TIGR00957 721 FGKalnekYY---QQVLEACALLPDLE---ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 655 GEERLKQRL---QSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:TIGR00957 795 VGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
276-692 |
6.11e-24 |
|
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: 108.07 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 276 DFLTSLTLASLIDLpfTLIILVVIAMLGGHLVWIPIIAFPLALgIGHMLQKPLTATLERTMALGAERQSS----LIETLA 351
Cdd:TIGR01271 996 DDMLPLTLFDFIQL--TLIVLGAIFVVSVLQPYIFIAAIPVAV-IFIMLRAYFLRTSQQLKQLESEARSPifshLITSLK 1072
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 352 GLDAVKV-----------NNAESERQYQWEQTIGTLSRLELRVkvlsglamNITLLIQQVAgVAMIIFGVYQiiDGALSM 420
Cdd:TIGR01271 1073 GLWTIRAfgrqsyfetlfHKALNLHTANWFLYLSTLRWFQMRI--------DIIFVFFFIA-VTFIAIGTNQ--DGEGEV 1141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 421 GGLVACYMLsgralgplaqlsgLLTRYQQAKVTMVSVDQMM----------ELPQERNYD---------------ERPLS 475
Cdd:TIGR01271 1142 GIILTLAMN-------------ILSTLQWAVNSSIDVDGLMrsvsrvfkfiDLPQEEPRPsggggkyqlstvlviENPHA 1208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 476 RKAL--QGAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDsGSLLVDGVDIRQIDV 553
Cdd:TIGR01271 1209 QKCWpsGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTL 1287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 554 SELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEmVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALAR 633
Cdd:TIGR01271 1288 QTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEE-IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLAR 1366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 634 ALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVID 692
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIE 1425
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
483-700 |
8.24e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.75 E-value: 8.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGY 562
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQ--DIQLLAGT--------LRDNLVSgaryvDDEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNV 629
Cdd:PRK13648 88 VFQnpDNQFVGSIvkydvafgLENHAVP-----YDEMhrrVSEALKQVDMLERADYEP-----------NALSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 630 ALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENK--TVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEG 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
482-677 |
1.29e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.88 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLY--QPD---SGSLLVDGVDI--RQIDVS 554
Cdd:COG1117 11 KIEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQDIQLLAGTLRDNLVSGARYVD-------DEMVLQAAELAG----VHEfaRLHpqgyelqvgERGQNLSG 623
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGikskselDEIVEESLRKAAlwdeVKD--RLK---------KSALGLSG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 624 GQRQNVALARALLLNPPILLLDEPTSAMD--NTG--EE---RLKQRLqsvienkTVILVTH 677
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDpiSTAkiEElilELKKDY-------TIVIVTH 211
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
484-697 |
1.37e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 102.84 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSElRhNIGYV 563
Cdd:COG3839 5 ELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-R-NIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLL-AGTLRDNLVSGARY--VD----DEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALL 636
Cdd:COG3839 81 FQSYALYpHMTVYENIAFPLKLrkVPkaeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 637 LNPPILLLDEPTSAMD-----NTGEE--RLKQRLqsvieNKTVILVTHRAS-LLSLVDRLLVIDRGQIL 697
Cdd:COG3839 150 REPKVFLLDEPLSNLDaklrvEMRAEikRLHRRL-----GTTTIYVTHDQVeAMTLADRIAVMNDGRIQ 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
498-696 |
2.87e-23 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 98.85 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 498 LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSelRHNIGYVAQDIQLLAG-TLRD 576
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGARY------VDDEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:cd03300 92 NIAFGLRLkklpkaEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 651 MDntgeERLKQRLQsvIENK--------TVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:cd03300 161 LD----LKLRKDMQ--LELKrlqkelgiTFVFVTHdQEEALTMSDRIAVMNKGKI 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
494-702 |
3.38e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.16 E-value: 3.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 494 NQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQI-DVSELRHNIGYVAQ--DIQLL 570
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIRNKAGMVFQnpDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 571 AGTLRDNLVSGARYV---DDEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:PRK13633 100 ATIVEEDVAFGPENLgipPEEIrerVDESLKKVGMYEYRRHAP-----------HLLSGGQKQRVAIAGILAMRPECIIF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 645 DEPTSAMDNTGEERLKQRLQSV--IENKTVILVTHRASLLSLVDRLLVIDRGQILADG-PK 702
Cdd:PRK13633 169 DEPTAMLDPSGRREVVNTIKELnkKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGtPK 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
496-697 |
4.75e-23 |
|
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: 99.26 E-value: 4.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL----RHNIGYVAQDIQLLA 571
Cdd:cd03294 36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 G-TLRDNLVSG------ARYVDDEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:cd03294 116 HrTVLENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 645 DEPTSAMDNT-----GEERLkqRLQSVIEnKTVILVTHR-ASLLSLVDRLLVIDRGQIL 697
Cdd:cd03294 185 DEAFSALDPLirremQDELL--RLQAELQ-KTIVFITHDlDEALRLGDRIAIMKDGRLV 240
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
499-708 |
8.60e-23 |
|
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: 99.74 E-value: 8.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQP---DSGSLLVDGVDIRQIDVSELRH----NIGYVAQD----- 566
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 ------IQLLAGTLRDNLVSGARYVDDEMV--LQAAELAGVHEFARLHPqgYElqvgergqnLSGGQRQNVALARALLLN 638
Cdd:COG0444 100 npvmtvGDQIAEPLRIHGGLSKAEARERAIelLERVGLPDPERRLDRYP--HE---------LSGGMRQRVMIARALALE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 639 PPILLLDEPTSAMDNTGE-------ERLKQRLqsvieNKTVILVTHRaslLSLV----DRLLVIDRGQILADGPKAAVME 707
Cdd:COG0444 169 PKLLIADEPTTALDVTIQaqilnllKDLQREL-----GLAILFITHD---LGVVaeiaDRVAVMYAGRIVEEGPVEELFE 240
|
.
gi 814585811 708 A 708
Cdd:COG0444 241 N 241
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
172-425 |
9.43e-23 |
|
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: 99.07 E-value: 9.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 172 IAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFE---- 247
Cdd:cd18567 8 LLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRhllr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 248 --------RIVGMAMkvrpARVGSfAQNIhefqgmRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALG 319
Cdd:cd18567 88 lplsyfekRHLGDIV----SRFGS-LDEI------QQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 320 IGHMLQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQ 399
Cdd:cd18567 157 LRLALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFG 236
|
250 260
....*....|....*....|....*.
gi 814585811 400 VAGVAMIIFGVYQIIDGALSMGGLVA 425
Cdd:cd18567 237 LENILVIYLGALLVLDGEFTVGMLFA 262
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
481-696 |
1.14e-22 |
|
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: 98.39 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 481 GAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDsGSLLVDGVDIRQIDVSELRHNI 560
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLAGTLRDNLVSGARYVDDEmVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPP 640
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDPYGKWSDEE-IWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 641 ILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
500-696 |
1.38e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.07 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvDIRqidvselrhnIGYVAQDIQLLAG-TLRDNL 578
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQEPPLDDDlTVLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARYVDDEMV-LQAAELAG------VHEFARLHPQ-----GYE-----------LQVGERGQN-----LSGGQRQNVA 630
Cdd:COG0488 83 LDGDAELRALEAeLEELEAKLaepdedLERLAELQEEfealgGWEaearaeeilsgLGFPEEDLDrpvseLSGGWRRRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 631 LARALLLNPPILLLDEPTSAMDNTG----EERLKQRlqsvieNKTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:COG0488 163 LARALLSEPDLLLLDEPTNHLDLESiewlEEFLKNY------PGTVLVVSHdRYFLDRVATRILELDRGKL 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
496-716 |
1.75e-22 |
|
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: 96.83 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL-RHNIGYVAQDIQLLAG-T 573
Cdd:TIGR03410 12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGA-------RYVDDEMVlqaaELagvheFARLHpqgyELQvGERGQNLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:TIGR03410 92 VEENLLTGLaalprrsRKIPDEIY----EL-----FPVLK----EML-GRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 647 PT-----SAMDNTGE--ERLKQRlqsviENKTVILVTHRASL-LSLVDRLLVIDRGQILADGPKAAVMEALKKGQISV 716
Cdd:TIGR03410 158 PTegiqpSIIKDIGRviRRLRAE-----GGMAILLVEQYLDFaRELADRYYVMERGRVVASGAGDELDEDKVRRYLAV 230
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
499-699 |
1.77e-22 |
|
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: 94.42 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQdiqllagtlrdn 577
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMVYQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 lvsgaryvddemvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEE 657
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 814585811 658 RLKQ---RLQSviENKTVILVTHRAS-LLSLVDRLLVIDRGQILAD 699
Cdd:cd03216 120 RLFKvirRLRA--QGVAVIFISHRLDeVFEIADRVTVLRDGRVVGT 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
497-705 |
2.82e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 2.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQLLAG-TL 574
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELNLVPNlSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNL-----VSGARYVDD-EMVLQAAELagvheFARLhpqGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:COG1129 97 AENIflgrePRRGGLIDWrAMRRRAREL-----LARL---GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 649 SAMDNTGEERLKQ---RLQSviENKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAV 705
Cdd:COG1129 169 ASLTEREVERLFRiirRLKA--QGVAIIYISHRlDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
499-700 |
3.12e-22 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 95.68 E-value: 3.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqiDVSELrhnigyvaqdIQLLAG-----T 573
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSL----------LGLGGGfnpelT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGARYV---DDEMvlqAAELAGVHEFARLhPQGYELQVGergqNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:cd03220 101 GRENIYLNGRLLglsRKEI---DEKIDEIIEFSEL-GDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 814585811 651 MDNTGEERLKQRLQSVIEN-KTVILVTH-RASLLSLVDRLLVIDRGQILADG 700
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQgKTVILVSHdPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
515-700 |
4.32e-22 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 97.95 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 515 IIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDvSELRHnIGYVAQDIQLLAG-TLRDNLVSGARY--VD----D 587
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-PHLRH-INMVFQSYALFPHmTVEENVAFGLKMrkVPraeiK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 588 EMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVI 667
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPH-----------QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 814585811 668 EN--KTVILVTH-RASLLSLVDRLLVIDRGQILADG 700
Cdd:TIGR01187 148 EQlgITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIG 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
491-701 |
7.52e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.57 E-value: 7.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 491 TYPN--QQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL----RHNIGYVA 564
Cdd:PRK10535 13 SYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 QDIQLLAGtlrdnlVSGARYVDDEMVLQAAELAGVHEFAR--LHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPIL 642
Cdd:PRK10535 93 QRYHLLSH------LTAAQNVEVPAVYAGLERKQRLLRAQelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 643 LLDEPTSAMDN-TGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGP 701
Cdd:PRK10535 167 LADEPTGALDShSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
495-706 |
8.50e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.82 E-value: 8.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 495 QQNLALRgINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSElR--------HNIGY---V 563
Cdd:COG3840 11 YGDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RpvsmlfqeNNLFPhltV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLlaGtLRDNLvsgaRYVDDE--MVLQAAELAGVHEF-ARLHPQgyelqvgergqnLSGGQRQNVALARALLLNPP 640
Cdd:COG3840 89 AQNIGL--G-LRPGL----KLTAEQraQVEQALERVGLAGLlDRLPGQ------------LSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 641 ILLLDEPTSAMDNTgeerLKQR-LQSVIE-----NKTVILVTHraSL---LSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:COG3840 150 ILLLDEPFSALDPA----LRQEmLDLVDElcrerGLTVLMVTH--DPedaARIADRVLLVADGRIAADGPTAALL 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
462-707 |
8.59e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 97.21 E-value: 8.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 462 ELPQERNYDERPLSRKALQGAMTFREVDF---TYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDS 538
Cdd:PRK13536 16 LSPIERKHQGISEAKASIPGSMSTVAIDLagvSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 539 GSLLVDGVDIRQiDVSELRHNIGYVAQ-DIQLLAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLhpqgyELQVGER 617
Cdd:PRK13536 96 GKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARL-----ESKADAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 618 GQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTH-RASLLSLVDRLLVIDRGQ 695
Cdd:PRK13536 170 VSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfMEEAERLCDRLCVLEAGR 249
|
250
....*....|...
gi 814585811 696 ILADG-PKAAVME 707
Cdd:PRK13536 250 KIAEGrPHALIDE 262
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
481-706 |
1.02e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 101.01 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 481 GAMTFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNI 560
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLAGTLRDNLVSGARYVDDEmVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPP 640
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVDPFLEASSAE-VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGS 1465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 641 I-LLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADG-PKAAVM 706
Cdd:PTZ00243 1466 GfILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGsPRELVM 1533
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
499-707 |
1.06e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.71 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDvSELRHnIGYVAQDIQLLAG-TLRDN 577
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENRH-VNTVFQSYALFPHmTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGARYVD------DEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPILLLDEPTSAM 651
Cdd:PRK09452 107 VAFGLRMQKtpaaeiTPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 652 DNtgeeRLKQRLQSVIE------NKTVILVTH-RASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:PRK09452 176 DY----KLRKQMQNELKalqrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
482-708 |
2.04e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.64 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQqnLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIG 561
Cdd:PRK13537 7 PIDFRNVEKRYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG-TLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGyELQVGErgqnLSGGQRQNVALARALLLNPP 640
Cdd:PRK13537 84 VVPQFDNLDPDfTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKA-DAKVGE----LSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 641 ILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTH-RASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHfMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
496-696 |
3.16e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.59 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqidvSELRHNIGYVAQDIQLLA-GTL 574
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGARYVDDEMVLQAAELAGVHEFArlhpqgyelqvGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDnt 654
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQALAAVGLADRA-----------NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 814585811 655 GEERLKqrLQSVIENK------TVILVTHRAS-LLSLVDRLLVIDRGQI 696
Cdd:PRK11247 166 ALTRIE--MQDLIESLwqqhgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
171-450 |
3.54e-21 |
|
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: 94.54 E-value: 3.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18779 7 ILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAMK---VRPA-----RVGSFAQnihefqgMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLALGIGH 322
Cdd:cd18779 87 RLPYRffqQRSTgdllmRLSSNAT-------IRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 323 MLQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAG 402
Cdd:cd18779 160 ATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAP 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 814585811 403 VAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQA 450
Cdd:cd18779 240 LVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVGTAQQLQLL 287
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
490-700 |
4.08e-21 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 92.43 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 490 FTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYVAqdiql 569
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVS----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 570 lagtlrDNLVSGARYVDDEMVLQAAELAGV--HEF-ARLHPQGYELQVGE----RGQNLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03266 85 ------DSTGLYDRLTARENLEYFAGLYGLkgDELtARLEELADRLGMEElldrRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSVIE-NKTVILVTHRAS-LLSLVDRLLVIDRGQILADG 700
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
503-706 |
4.89e-21 |
|
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: 95.18 E-value: 4.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGV---DIRQ-IDVSELRHNIGYVAQDIQLLAG-TLRDN 577
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGARYVDdemvlqaAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEE 657
Cdd:TIGR02142 96 LRYGMKRAR-------PSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 814585811 658 RLKQRLQSVIE--NKTVILVTHRAS-LLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:TIGR02142 169 EILPYLERLHAefGIPILYVSHSLQeVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
486-702 |
5.36e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 5.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQqNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVS--ELRHNIGYV 563
Cdd:PRK13639 5 RDLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQ--DIQLLAGTLRDNLVSGARYV---DDEM---VLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARAL 635
Cdd:PRK13639 84 FQnpDDQLFAPTVEEDVAFGPLNLglsKEEVekrVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 636 LLNPPILLLDEPTSAMDNTGEERLKQRLQSVieNK---TVILVTHRASLLSL-VDRLLVIDRGQILADG-PK 702
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGtPK 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
161-631 |
8.95e-21 |
|
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: 96.79 E-value: 8.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 161 LKRSRWLYADAIAASL--------VINLIALAAplfvmnvydRVVPNQATATLWMLAiGICGAYL-----FDLLL----- 222
Cdd:COG4615 8 LRESRWLLLLALLLGLlsglanagLIALINQAL---------NATGAALARLLLLFA-GLLVLLLlsrlaSQLLLtrlgq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 223 KSLRSLCLDLAGKktdliISATLFERIvgmaMKVRPARVgsfaqnihefqgmrdfLTSLT--LASLIDLPFTLIILVV-I 299
Cdd:COG4615 78 HAVARLRLRLSRR-----ILAAPLERL----ERIGAARL----------------LAALTedVRTISQAFVRLPELLQsV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 300 AMLGGHLVWIPIIAFPL------ALGIGHMLQKPLTATLERTMALGAERQSSLIETLA----GLDAVKVNNAESERQYQW 369
Cdd:COG4615 133 ALVLGCLAYLAWLSPPLflltlvLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRalleGFKELKLNRRRRRAFFDE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 370 E--QTIGTLSRLELRVKVLSGLAMNITLLIQQVAgVAMIIFGV--YQIIDGA-LSMGGLVACYMLsgralGPLAQLSGLL 444
Cdd:COG4615 213 DlqPTAERYRDLRIRADTIFALANNWGNLLFFAL-IGLILFLLpaLGWADPAvLSGFVLVLLFLR-----GPLSQLVGAL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 445 TRYQQAKVTMVSVDQM---MELPQERNYDERPLSRKALQGAMTFREVDFTYPNQQ---NLALRGINLNVRAGEKIGIIGR 518
Cdd:COG4615 287 PTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdeGFTLGPIDLTIRRGELVFIVGG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 519 SGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLagtlrDNLVSGARYVDDEMV---LQAAE 595
Cdd:COG4615 367 NGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRLLGLDGEADPARArelLERLE 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 814585811 596 LAGV-----HEFARLhpqgyelqvgergqNLSGGQRQNVAL 631
Cdd:COG4615 442 LDHKvsvedGRFSTT--------------DLSQGQRKRLAL 468
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
499-708 |
1.06e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 93.64 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRH---NIGYVAQD--------- 566
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDpyaslnprm 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 --IQLLAGTLRDN-LVSGARYvdDEMVLQAAELAGV---------HEFarlhpqgyelqvgergqnlSGGQRQNVALARA 634
Cdd:COG4608 113 tvGDIIAEPLRIHgLASKAER--RERVAELLELVGLrpehadrypHEF-------------------SGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 635 LLLNPPILLLDEPTSAMD--------NTGEErLKQRLqsvieNKTVILVTHRaslLSLV----DRLLVIDRGQILADGPK 702
Cdd:COG4608 172 LALNPKLIVCDEPVSALDvsiqaqvlNLLED-LQDEL-----GLTYLFISHD---LSVVrhisDRVAVMYLGKIVEIAPR 242
|
....*.
gi 814585811 703 AAVMEA 708
Cdd:COG4608 243 DELYAR 248
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
479-692 |
1.63e-20 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 97.02 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 479 LQGAMTFREVDFTYPNQQNLAL-RGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQ---------------------- 535
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVPIyKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 536 --------------------------------PDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGAR 583
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 584 YVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRL 663
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270
....*....|....*....|....*....|.
gi 814585811 664 QSVIE--NKTVILVTHRASLLSLVDRLLVID 692
Cdd:PTZ00265 1402 VDIKDkaDKTIITIAHRIASIKRSDKIVVFN 1432
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
499-711 |
1.78e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.30 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqiDVSELrhnigyvaqdIQLLAG-----T 573
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL----------LELGAGfhpelT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGARYVD------DEMVLQAAELAGVHEFArlhpqgyELQVGergqNLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:COG1134 105 GRENIYLNGRLLGlsrkeiDEKFDEIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 648 TSAMDNTGEERLKQRLQSVIEN-KTVILVTH-RASLLSLVDRLLVIDRGQILADGPKAAVMEALKK 711
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESgRTVIFVSHsMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAAYEA 239
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
499-700 |
1.78e-20 |
|
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: 90.42 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdiRQIDVsELRHNIGYVAQDIQL-LAGTLRDN 577
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDI-AARNRIGYLPEERGLyPKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGARYVDdeMVLQAAELAGVHEFARLHPQGYELQVGERgqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEE 657
Cdd:cd03269 91 LVYLAQLKG--LKKEEARRRIDEWLERLELSEYANKRVEE---LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 814585811 658 RLKQRLQSVIEN-KTVILVTHRASLLS-LVDRLLVIDRGQILADG 700
Cdd:cd03269 166 LLKDVIRELARAgKTVILSTHQMELVEeLCDRVLLLNKGRAVLYG 210
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
500-709 |
2.72e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 90.22 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdiRQIDvsELRHNIGYVAQDIQLLAG-TLRDNL 578
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQIT--EPGPDRMVVFQNYSLLPWlTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARYV--------DDEMVLQAAELAGVHEFARLHPqgyelqvgerGQnLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:TIGR01184 76 ALAVDRVlpdlskseRRAIVEEHIALVGLTEAADKRP----------GQ-LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 651 MDNTGEERLKQRLQSVIENK--TVILVTHRasllslVDR-LLVIDRGQILADGPKAAVMEAL 709
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHrvTVLMVTHD------VDEaLLLSDRVVMLTNGPAANIGQIL 200
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
500-694 |
4.07e-20 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 89.70 E-value: 4.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL----RHNIGYVAQDIQLLAGTLR 575
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSGA-----RYvddEMVLQAAELagvHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:cd03290 97 ENITFGSpfnkqRY---KAVTDACSL---QPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 814585811 651 MDNTGEERLKQR--LQSVIENK-TVILVTHRASLLSLVDRLLVIDRG 694
Cdd:cd03290 171 LDIHLSDHLMQEgiLKFLQDDKrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
500-706 |
6.85e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.79 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQL-LAGTLRDnL 578
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLaFPFTVEE-V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARYV-------DDEMVLQAAELAGVHEFA-RLHPQgyelqvgergqnLSGGQRQNVALARALLLNPPILLL------ 644
Cdd:COG4559 96 VALGRAPhgssaaqDRQIVREALALVGLAHLAgRSYQT------------LSGGEQQRVQLARVLAQLWEPVDGgprwlf 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 645 -DEPTSAMDntgeerLKQRLQS-------VIENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAVM 706
Cdd:COG4559 164 lDEPTSALD------LAHQHAVlrlarqlARRGGGVVAVLHDLNLAAQYaDRILLLHQGRLVAQGTPEEVL 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
472-707 |
7.01e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.21 E-value: 7.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 472 RPLSRKALQGAMTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQi 551
Cdd:PRK11607 9 QAKTRKALTPLLEIRNLTKSFDGQH--AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 552 dVSELRHNIGYVAQDIQLLAG-TLRDNLVSGA---RYVDDEMVLQAAE-LAGVH--EFARLHPQgyelqvgergqNLSGG 624
Cdd:PRK11607 86 -VPPYQRPINMMFQSYALFPHmTVEQNIAFGLkqdKLPKAEIASRVNEmLGLVHmqEFAKRKPH-----------QLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 625 QRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTH-RASLLSLVDRLLVIDRGQILADGP 701
Cdd:PRK11607 154 QRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGE 233
|
....*.
gi 814585811 702 KAAVME 707
Cdd:PRK11607 234 PEEIYE 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
500-695 |
7.06e-20 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 90.30 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGsllvdgvdirqidvsELRHN--IGYVAQDIQLLAGTLRDN 577
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG---------------KIKHSgrISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGARYvdDEM----VLQAAELAgvHEFARLHPQGYELqVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMD- 652
Cdd:cd03291 118 IIFGVSY--DEYryksVVKACQLE--EDITKFPEKDNTV-LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDv 192
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 814585811 653 NTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQ 695
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
505-700 |
7.28e-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: 88.70 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 505 LNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSElrHNIGYVAQDIQLLAG-TLRDNLVSGar 583
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGLG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 584 yVDDEMVLQAAELAGVHE-FARLHPQGYELQvgeRGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQR 662
Cdd:cd03298 95 -LSPGLKLTAEDRQAIEVaLARVGLAGLEKR---LPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 814585811 663 LQSVIENK--TVILVTHRAS-LLSLVDRLLVIDRGQILADG 700
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
490-702 |
1.44e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 490 FTYPNQqNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDI-- 567
Cdd:PRK13647 12 FRYKDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPdd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 QLLAGTLRDNLVSGARYVD------DEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPI 641
Cdd:PRK13647 91 QVFSSTVWDDVAFGPVNMGldkdevERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 642 LLLDEPTSAMDNTGEERLKQRLQSVIEN-KTVILVTHRASL-LSLVDRLLVIDRGQILADGPK 702
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDK 222
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
500-707 |
1.92e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 93.69 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDgvdirqidvselrHNIGYVAQDIQLLAGTLRDNLV 579
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 580 sgarYVDDEmvlQAAELAGVHEFARLH------PQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMD- 652
Cdd:PTZ00243 743 ----FFDEE---DAARLADAVRVSQLEadlaqlGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDa 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 653 NTGEERLKQRLQSVIENKTVILVTHRASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:PTZ00243 816 HVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
489-695 |
2.43e-19 |
|
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: 87.49 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNL---ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVD----GVDIRQIDVSEL----R 557
Cdd:COG4778 13 TFTLHLQGGKrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREIlalrR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 558 HNIGYVAQ---------DIQLLAGTLRDNLVSgaryvDDEMVLQAAELagvheFARLhpqgyelQVGERGQNL-----SG 623
Cdd:COG4778 93 RTIGYVSQflrviprvsALDVVAEPLLERGVD-----REEARARAREL-----LARL-------NLPERLWDLppatfSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814585811 624 GQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVIL-VTHRASLLSLV-DRLLVIDRGQ 695
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAVaDRVVDVTPFS 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
496-717 |
2.53e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.72 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRgINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSelRHNIGYVAQDIQLLAG-TL 574
Cdd:PRK10771 12 HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGaryVDDEMVLQAAELAGVHEFARlhpqgyelQVG-----ER--GQnLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:PRK10771 89 AQNIGLG---LNPGLKLNAAQREKLHAIAR--------QMGiedllARlpGQ-LSGGQRQRVALARCLVREQPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 648 TSAMDNTGEERLKQRLQSVIENK--TVILVTHraSL---LSLVDRLLVIDRGQILADGPKAavmeALKKGQISVA 717
Cdd:PRK10771 157 FSALDPALRQEMLTLVSQVCQERqlTLLMVSH--SLedaARIAPRSLVVADGRIAWDGPTD----ELLSGKASAS 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
466-691 |
3.75e-19 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.78 E-value: 3.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 466 ERNYDERPLSR-KALQgamtFREVDFTYPNQQNLAL-RGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLV 543
Cdd:PTZ00265 369 ENNDDGKKLKDiKKIQ----FKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 544 -DGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLV------------------------------------------- 579
Cdd:PTZ00265 445 nDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlnd 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 580 --------------SGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLD 645
Cdd:PTZ00265 525 msnttdsneliemrKNYQTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 814585811 646 EPTSAMDNTGEERLKQRLQSVI--ENKTVILVTHRASLLSLVDRLLVI 691
Cdd:PTZ00265 605 EATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
486-700 |
6.39e-19 |
|
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: 85.73 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqIDVSELRHNIGyVAQ 565
Cdd:cd03268 4 NDLTKTYGKKR--VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY--QKNIEALRRIG-ALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 DIQLLAG--TLRDNLVSGARY--VDDEMVLQAAELAGVHEFARLHPQGYELqvgergqnlsgGQRQNVALARALLLNPPI 641
Cdd:cd03268 79 EAPGFYPnlTARENLRLLARLlgIRKKRIDEVLDVVGLKDSAKKKVKGFSL-----------GMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 642 LLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHRASLLSLV-DRLLVIDRGQILADG 700
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
487-706 |
8.94e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 88.62 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 487 EVDFTYpNQQNLALRgINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG---VDIRQ-IDVSELRHNIGY 562
Cdd:COG4148 4 EVDFRL-RRGGFTLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLPPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAG-TLRDNLVSGARYVDDEMvlQAAELAGVHEFarlhpqgyeLQVG---ERG-QNLSGGQRQNVALARALLL 637
Cdd:COG4148 82 VFQEARLFPHlSVRGNLLYGRKRAPRAE--RRISFDEVVEL---------LGIGhllDRRpATLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 638 NPPILLLDEPTSAMDNT--GE-----ERLKQRLqsvieNKTVILVTH-RASLLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:COG4148 151 SPRLLLMDEPLAALDLArkAEilpylERLRDEL-----DIPILYVSHsLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
500-706 |
9.06e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.75 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQL-LAGTLRDnL 578
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE-V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARYV-------DDEMVLQAAELAGVHEFA-RLHPQgyelqvgergqnLSGGQRQNVALARALLLNPPILLL------ 644
Cdd:PRK13548 97 VAMGRAPhglsraeDDALVAAALAQVDLAHLAgRDYPQ------------LSGGEQQRVQLARVLAQLWEPDGPprwlll 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 645 DEPTSAMDNTGEERL----KQRLQSviENKTVILVTHRASLLSL-VDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK13548 165 DEPTSALDLAHQHHVlrlaRQLAHE--RGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEVL 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
500-708 |
1.70e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 85.62 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG---------------VDIRQIDvsELRHNIGYVA 564
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeirlkpdrdgelvpADRRQLQ--RIRTRLGMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 QDIQLLAG-TLRDNLVSGARYV----DDEMVLQAAEL---AGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALL 636
Cdd:COG4598 102 QSFNLWSHmTVLENVIEAPVHVlgrpKAEAIERAEALlakVGLADKRDAYPA-----------HLSGGQQQRAAIARALA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 637 LNPPILLLDEPTSAMDNtgE---ERLKqrlqsVI-----ENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAVME 707
Cdd:COG4598 171 MEPEVMLFDEPTSALDP--ElvgEVLK-----VMrdlaeEGRTMLVVTHEMGFARDVsSHVVFLHQGRIEEQGPPAEVFG 243
|
.
gi 814585811 708 A 708
Cdd:COG4598 244 N 244
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
499-700 |
2.10e-18 |
|
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: 85.08 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVD--IRQIdvsELRHNIGYV-AQDIQLLAG-TL 574
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRK---KFLRRIGVVfGQKTQLWWDlPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGARYVDDEMVLQAAELAGVHEFARLHPqgyELQVGERgqNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNT 654
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEE---LLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 814585811 655 GEERLKQRLQSVIENK--TVILVTHR-ASLLSLVDRLLVIDRGQILADG 700
Cdd:cd03267 188 AQENIRNFLKEYNRERgtTVLLTSHYmKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
490-700 |
2.28e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.91 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 490 FTYPNQQNL-ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQ--D 566
Cdd:PRK13642 12 FKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQLLAGTLRDNLVSGaryVDDEMVLQAAELAGVHEfARLHPQGYELQVGERGQnLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:PRK13642 92 NQFVGATVEDDVAFG---MENQGIPREEMIKRVDE-ALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 647 PTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLSLVDRLLVIDRGQILADG 700
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
500-700 |
3.34e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 83.37 E-value: 3.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGL--YQPDSGSLLVDGvdiRQIDVSELRHNIGYVAQDIQLLAG-TLRd 576
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLING---RPLDKRSFRKIIGYVPQDDILHPTlTVR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 nlvsgaryvddEMVLQAAELagvhefarlhpqgyelqvgergQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGE 656
Cdd:cd03213 101 -----------ETLMFAAKL----------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 814585811 657 ERLKQRLQSVI-ENKTVILVTH--RASLLSLVDRLLVIDRGQILADG 700
Cdd:cd03213 148 LQVMSLLRRLAdTGRTIICSIHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
500-708 |
3.58e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQL---------- 569
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfefdvrqvv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 570 -LAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFArlhpqgyelqvgERG-QNLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:PRK09536 99 eMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFA------------DRPvTSLSGGERQRVLLARALAQATPVLLLDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 648 TSAMDNTGEER---LKQRLqsVIENKTVILVTHRASLLS-LVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK09536 167 TASLDINHQVRtleLVRRL--VDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAGPPADVLTA 229
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
504-696 |
4.67e-18 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 83.37 E-value: 4.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 504 NLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqIDVSELRHNIGYVAQDIQLLAG-TLRDNLVSGa 582
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH--TGLAPYQRPVSMLFQENNLFAHlTVRQNIGLG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 583 ryVDDEMVLQAAELAGVHEFARlhpqgyelQVG-----ERGQN-LSGGQRQNVALARALLLNPPILLLDEPTSAMDNT-G 655
Cdd:TIGR01277 95 --LHPGLKLNAEQQEKVVDAAQ--------QVGiadylDRLPEqLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLlR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 814585811 656 EERLKQRLQSVIENK-TVILVTHRAS-LLSLVDRLLVIDRGQI 696
Cdd:TIGR01277 165 EEMLALVKQLCSERQrTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
500-700 |
6.22e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 83.36 E-value: 6.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQLLAG-TLRDN 577
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIGYLPQEASIFRKlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 L--VSGARYVDDEMVLQAAElAGVHEFARLHPQgyelqvGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTG 655
Cdd:cd03218 96 IlaVLEIRGLSKKEREEKLE-ELLEEFHITHLR------KSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 814585811 656 EERLKQRLQSVIENKTVILVT-HRAS-LLSLVDRLLVIDRGQILADG 700
Cdd:cd03218 169 VQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEG 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
496-706 |
7.13e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.87 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQdIQLLAGTL- 574
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQ-LRLLRTRLt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 ----RDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVG--ERGQ-----NLSGGQRQNVALARALLLNPPILL 643
Cdd:PRK10619 96 mvfqHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGidERAQgkypvHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 644 LDEPTSAMDN--TGEE-RLKQRLQSviENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAVM 706
Cdd:PRK10619 176 FDEPTSALDPelVGEVlRIMQQLAE--EGKTMVVVTHEMGFARHVsSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
496-699 |
7.15e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.98 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIqlLAGT-- 573
Cdd:COG1101 18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDP--MMGTap 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 ---LRDNLV----SGARY-----VDDEMVLQAAELAgvhefARLHpQGYELQVGERGQNLSGGQRQNVALARALLLNPPI 641
Cdd:COG1101 96 smtIEENLAlayrRGKRRglrrgLTKKRRELFRELL-----ATLG-LGLENRLDTKVGLLSGGQRQALSLLMATLTKPKL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 642 LLLDEPTSAMD-NTGEERLKQRLQSVIENK-TVILVTHraSL---LSLVDRLLVIDRGQILAD 699
Cdd:COG1101 170 LLLDEHTAALDpKTAALVLELTEKIVEENNlTTLMVTH--NMeqaLDYGNRLIMMHEGRIILD 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
482-677 |
7.88e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 83.76 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYP--NQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSElrhn 559
Cdd:COG4525 3 MLTVRHVSVRYPggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 iGYVAQDIQLLAG-TLRDNLVSGARyvddemvlqaaeLAGVHEFARLHPQGYELQ-VGERGQ------NLSGGQRQNVAL 631
Cdd:COG4525 79 -GVVFQKDALLPWlNVLDNVAFGLR------------LRGVPKAERRARAEELLAlVGLADFarrriwQLSGGMRQRVGI 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 814585811 632 ARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSV--IENKTVILVTH 677
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
499-700 |
8.62e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.75 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGS---LLVDGVDIRQID---------------------VS 554
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKekekvleklviqktrfkkikkIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQ--DIQLLAGTLRDNLVSGARY--VDDEMVLQAA----ELAGVhefarlhPQGYeLQvgERGQNLSGGQR 626
Cdd:PRK13651 102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmgVSKEEAKKRAakyiELVGL-------DESY-LQ--RSPFELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 627 QNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN-KTVILVTHRA-SLLSLVDRLLVIDRGQILADG 700
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRTIFFKDGKIIKDG 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
499-696 |
9.73e-18 |
|
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: 81.71 E-value: 9.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQ----LLAGT 573
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKreglVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGARyvddemvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMD- 652
Cdd:cd03215 95 VAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDv 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 814585811 653 NTGEERLKQRLQSVIENKTVILVThraS----LLSLVDRLLVIDRGQI 696
Cdd:cd03215 138 GAKAEIYRLIRELADAGKAVLLIS---SeldeLLGLCDRILVMYEGRI 182
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
499-696 |
1.07e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE---LRHNIGYVAQDIQLLAG-TL 574
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLMDrTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDN-----LVSGARYVDDEMVLQAA-ELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:PRK10908 97 YDNvaiplIIAGASGDDIRRRVSAAlDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 814585811 649 SAMDNTGEE---RLKQRLQSVieNKTVILVTHRASLLSLVD-RLLVIDRGQI 696
Cdd:PRK10908 166 GNLDDALSEgilRLFEEFNRV--GVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
500-701 |
1.15e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.58 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE---LRHNIGYVAQDI--------- 567
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkaFRRDIQMVFQDSisavnprkt 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 --QLLAGTLRD--NLVSGARYVDDEMVLQAAELAGVHeFARLHPQgyelqvgergqnLSGGQRQNVALARALLLNPPILL 643
Cdd:PRK10419 108 vrEIIREPLRHllSLDKAERLARASEMLRAVDLDDSV-LDKRPPQ------------LSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 644 LDEPTSAMD---NTGEERLKQRLQSviENKTVIL-VTHRaslLSLVD----RLLVIDRGQILADGP 701
Cdd:PRK10419 175 LDEAVSNLDlvlQAGVIRLLKKLQQ--QFGTACLfITHD---LRLVErfcqRVMVMDNGQIVETQP 235
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
484-703 |
1.22e-17 |
|
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: 83.32 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE---LRHNI 560
Cdd:TIGR02769 11 TYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDI-----------QLLAGTLRdNLVSGARYVDDEMVLQAAELAGVH-EFARLHPQgyelqvgergqNLSGGQRQN 628
Cdd:TIGR02769 91 QLVFQDSpsavnprmtvrQIIGEPLR-HLTSLDESEQKARIAELLDMVGLRsEDADKLPR-----------QLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 629 VALARALLLNPPILLLDEPTSAMD---NTGEERLKQRLQSVIeNKTVILVTHRASLL-SLVDRLLVIDRGQILADGPKA 703
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDmvlQAVILELLRKLQQAF-GTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVA 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
486-700 |
1.95e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.31 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQ 565
Cdd:PRK13652 7 RDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 --DIQLLAGTLRDNLVSGARY--VDDEMVLQAAELAgvhefarLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPI 641
Cdd:PRK13652 86 npDDQIFSPTVEQDIAFGPINlgLDEETVAHRVSSA-------LHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 642 LLLDEPTSAMDNTGEERLKQRLQSVIEN--KTVILVTHRASLL-SLVDRLLVIDRGQILADG 700
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYG 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
500-694 |
2.03e-17 |
|
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: 87.27 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGsllvdgvdirqidvsELRHN--IGYVAQDIQLLAGTLRDN 577
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG---------------KIKHSgrISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGARYvdDEM----VLQAAELagvHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDN 653
Cdd:TIGR01271 507 IIFGLSY--DEYrytsVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 814585811 654 TGEERLKQR-LQSVIENKTVILVTHRASLLSLVDRLLVIDRG 694
Cdd:TIGR01271 582 VTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
487-701 |
4.42e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.39 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 487 EVDFTypnQQ--NLALRgINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG---VDIRQ-IDVSELRHNI 560
Cdd:PRK11144 3 ELNFK---QQlgDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDIQLLAG-TLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNP 639
Cdd:PRK11144 79 GYVFQDARLFPHyKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 640 PILLLDEPTSAMDNTGEERLKQRLQSVIEN-KTVIL-VTHraSL---LSLVDRLLVIDRGQILADGP 701
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILyVSH--SLdeiLRLADRVVVLEQGKVKAFGP 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
486-714 |
4.78e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.20 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG--VDIRQIDVSELRHNIGYV 563
Cdd:PRK13636 9 EELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQ--DIQLLAGTLRDNLVSGAryvddeMVLQAAElAGVHEFAR--LHPQGYELQVGERGQNLSGGQRQNVALARALLLNP 639
Cdd:PRK13636 88 FQdpDNQLFSASVYQDVSFGA------VNLKLPE-DEVRKRVDnaLKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 640 PILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLSL-VDRLLVIDRGQ-ILADGPKA--AVMEALKKGQ 713
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRvILQGNPKEvfAEKEMLRKVN 240
|
.
gi 814585811 714 I 714
Cdd:PRK13636 241 L 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
483-700 |
5.02e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 81.99 E-value: 5.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTY-PNQ--QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI----RQIDVSE 555
Cdd:PRK13634 3 ITFQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 556 LRHNIGYVAQ--DIQLLAGTLRDNLVSG----------ARYVDDEMVlqaaELAGVHEfARLHPQGYElqvgergqnLSG 623
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGpmnfgvseedAKQKAREMI----ELVGLPE-ELLARSPFE---------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 624 GQRQNVALARALLLNPPILLLDEPTSAMDNTGE-------ERLKQRlqsviENKTVILVTHRAS-LLSLVDRLLVIDRGQ 695
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRkemmemfYKLHKE-----KGLTTVLVTHSMEdAARYADQIVVMHKGT 223
|
....*
gi 814585811 696 ILADG 700
Cdd:PRK13634 224 VFLQG 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
499-687 |
5.31e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.36 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLL--VGLYQPD---SGSLLVDGVDI--RQIDVSELRHNIGYVAQDIQLLA 571
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 GTLRDNLVSGARY--VDDEMVLQAA---ELAGVHEFARLHPQGYELQVGergqnLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:PRK14239 100 MSIYENVVYGLRLkgIKDKQVLDEAvekSLKGASIWDEVKDRLHDSALG-----LSGGQQQRVCIARVLATSPKIILLDE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 814585811 647 PTSAMDNTGEERLKQRLQSVIENKTVILVTH---RASLLSlvDR 687
Cdd:PRK14239 175 PTSALDPISAGKIEETLLGLKDDYTMLLVTRsmqQASRIS--DR 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
500-712 |
5.95e-17 |
|
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: 79.88 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGL--YQPDSGSLLVDGVDIRQIDVSE-LRHNIGyvaqdiqllagtlrd 576
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEErARLGIF--------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 nlvsgaryvddeMVLQA-AELAGVH--EFARlhpqgyELQVGergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDN 653
Cdd:cd03217 81 ------------LAFQYpPEIPGVKnaDFLR------YVNEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 654 TGEERLKQRLQSVI-ENKTVILVTHRASLLSLV--DRLLVIDRGQILADGPKAAVMEALKKG 712
Cdd:cd03217 138 DALRLVAEVINKLReEGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELALEIEKKG 199
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
501-695 |
6.63e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 501 RGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDvSELRHNIGYVAQdiqlLAG-----TLR 575
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDLLYLGH----QPGiktelTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNL---VSGARYVDDEMVLQAAELAGVHEFARLhPQGYelqvgergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMD 652
Cdd:PRK13538 93 ENLrfyQRLHGPGDDEALWEALAQVGLAGFEDV-PVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 814585811 653 NTGEERLKQRLQSVIENK-TVILVTHRaSLLSLVDRLLVIDRGQ 695
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGgMVILTTHQ-DLPVASDKVRKLRLGQ 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
470-696 |
7.27e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 470 DERPLSRKALqgamTFREVDFTYPNqqNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVdGVDIR 549
Cdd:COG0488 307 PPERLGKKVL----ELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 550 qidvselrhnIGYVAQDiqllagtlRDNLvsgaryvDDEM-VLQaaelagvhEFARLHPQGYELQV----------GERG 618
Cdd:COG0488 380 ----------IGYFDQH--------QEEL-------DPDKtVLD--------ELRDGAPGGTEQEVrgylgrflfsGDDA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 619 Q----NLSGGQRQNVALARALLLNPPILLLDEPTSAMDntgeerlkqrLQS--VIENK------TVILVTH-RASLLSLV 685
Cdd:COG0488 427 FkpvgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----------IETleALEEAlddfpgTVLLVSHdRYFLDRVA 496
|
250
....*....|.
gi 814585811 686 DRLLVIDRGQI 696
Cdd:COG0488 497 TRILEFEDGGV 507
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
483-707 |
9.20e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 9.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTY-PNQ--QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI----RQIDVSE 555
Cdd:PRK13643 2 IKFEKVNYTYqPNSpfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 556 LRHNIGYVAQ--DIQLLAGTLRDNLVSG------ARYVDDEMVLQAAELAGV-HEFARLHPqgYELqvgergqnlSGGQR 626
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqnfgiPKEKAEKIAAEKLEMVGLaDEFWEKSP--FEL---------SGGQM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 627 QNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN-KTVILVTHRA-SLLSLVDRLLVIDRGQILADGPKAA 704
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPSD 230
|
...
gi 814585811 705 VME 707
Cdd:PRK13643 231 VFQ 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
482-716 |
9.43e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.33 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQ---QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQI----DVS 554
Cdd:PRK13649 2 GINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQ--DIQLLAGTLRDNLVSGARY--VDDEMVLQAAElagvhefARLHPQGYELQVGERGQ-NLSGGQRQNV 629
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAR-------EKLALVGISESLFEKNPfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 630 ALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN-KTVILVTHrasLLSLV----DRLLVIDRGQILADGPKAA 704
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTH---LMDDVanyaDFVYVLEKGKLVLSGKPKD 231
|
250
....*....|....*
gi 814585811 705 V---MEALKKGQISV 716
Cdd:PRK13649 232 IfqdVDFLEEKQLGV 246
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-716 |
1.21e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDvselRHNIGYV-----------AQDi 567
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLpeerglypkmkVGE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 QLLA-GTLRDnlvsgaryvddeMVLQAAELAGVHEFARLhpqgyelQVGERG----QNLSGGQRQNVALARALLLNPPIL 642
Cdd:COG4152 91 QLVYlARLKG------------LSKAEAKRRADEWLERL-------GLGDRAnkkvEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 643 LLDEPTSAMD--NTgeERLKQRLQSVIEN-KTVILVTHRaslLSLV----DRLLVIDRGQILADGPKAAVMEALKKGQIS 715
Cdd:COG4152 152 ILDEPFSGLDpvNV--ELLKDVIRELAAKgTTVIFSSHQ---MELVeelcDRIVIINKGRKVLSGSVDEIRRQFGRNTLR 226
|
.
gi 814585811 716 V 716
Cdd:COG4152 227 L 227
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
485-696 |
1.26e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.48 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQqNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVA 564
Cdd:PRK10522 325 LRNVTFAYQDN-GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 QDIQLLAGTLRDnlvsGARYVDDEMVLQAAELAGVHEfaRLHPQGYELqvgeRGQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:PRK10522 404 TDFHLFDQLLGP----EGKPANPALVEKWLERLKMAH--KLELEDGRI----SNLKLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 645 DEPTSAMDNTGEERLKQRL--QSVIENKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:PRK10522 474 DEWAADQDPHFRREFYQVLlpLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
499-708 |
1.51e-16 |
|
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: 83.20 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLyQPDSGSLLVDGVDIRQIDVSE---LRHNIGYVAQD--------- 566
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDpfgslsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 --IQLLA---GTLRDNLVSGARyvdDEMVLQAaeLAGV-----------HEFarlhpqgyelqvgergqnlSGGQRQNVA 630
Cdd:COG4172 380 tvGQIIAeglRVHGPGLSAAER---RARVAEA--LEEVgldpaarhrypHEF-------------------SGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 631 LARALLLNPPILLLDEPTSAMDNTGEER---LKQRLQSViENKTVILVTH-----RAsllsLVDRLLVIDRGQILADGPK 702
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDVSVQAQildLLRDLQRE-HGLAYLFISHdlavvRA----LAHRVMVMKDGKVVEQGPT 510
|
....*.
gi 814585811 703 AAVMEA 708
Cdd:COG4172 511 EQVFDA 516
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
483-692 |
1.52e-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: 77.58 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQNLaLRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLlvdgvdirqidVSELRHNIGY 562
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAGTLRDNLVsgaryvddemvlqaaelagvhefarlHPQgyelqvgerGQNLSGGQRQNVALARALLLNPPIL 642
Cdd:cd03223 69 LPQRPYLPLGTLREQLI--------------------------YPW---------DDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLQSviENKTVILVTHRASLLSLVDRLLVID 692
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
495-700 |
5.32e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.52 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 495 QQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGS-----LLVDGVDIR---QIDVSELRHNIGYVAQD 566
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshieLLGRTVQREgrlARDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQLLAG-TLRDNLVSGA-----------RY---VDDEMVLQAAELAGVHEFARlhpqgyelqvgERGQNLSGGQRQNVAL 631
Cdd:PRK09984 95 FNLVNRlSVLENVLIGAlgstpfwrtcfSWftrEQKQRALQALTRVGMVHFAH-----------QRVSTLSGGQQQRVAI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 632 ARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENK--TVILVTHRASL-LSLVDRLLVIDRGQILADG 700
Cdd:PRK09984 164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYaLRYCERIVALRQGHVFYDG 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
488-652 |
6.35e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 77.75 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG--------VDIRQIdvSELRHN 559
Cdd:PRK11124 8 INCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAI--RELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 IGYVAQDIQLLAG-TLRDNLVSGARYV----DDEMVLQAAELagvheFARL----HPQGYELQvgergqnLSGGQRQNVA 630
Cdd:PRK11124 84 VGMVFQQYNLWPHlTVQQNLIEAPCRVlglsKDQALARAEKL-----LERLrlkpYADRFPLH-------LSGGQQQRVA 151
|
170 180
....*....|....*....|..
gi 814585811 631 LARALLLNPPILLLDEPTSAMD 652
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALD 173
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
515-700 |
7.00e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.12 E-value: 7.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 515 IIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI---------------RQI-DVSELRHNIGYVAQ--DIQLLAGTLRD 576
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpysKKIkNFKELRRRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSG--ARYVDDEmvlQAAELAGVHefarLHPQGYELQVGERGQ-NLSGGQRQNVALARALLLNPPILLLDEPTSAMDN 653
Cdd:PRK13631 137 DIMFGpvALGVKKS---EAKKLAKFY----LNKMGLDDSYLERSPfGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 814585811 654 TGEERLKQR-LQSVIENKTVILVTHRA-SLLSLVDRLLVIDRGQILADG 700
Cdd:PRK13631 210 KGEHEMMQLiLDAKANNKTVFVITHTMeHVLEVADEVIVMDKGKILKTG 258
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
484-695 |
7.10e-16 |
|
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: 75.18 E-value: 7.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQqnLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqidvselRHNIGYV 563
Cdd:cd03221 2 ELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQdiqllagtlrdnlvsgaryvddemvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNPPILL 643
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 644 LDEPTSAMDNTGEERLKQRLQSviENKTVILVTHRASLLSLV-DRLLVIDRGQ 695
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKE--YPGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
499-691 |
7.49e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 76.50 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqidvselRHNIGYVAQDIQL---LAGTLR 575
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DnLVSGARY----------VDDEMVLQAA-ELAGVHEFARLhpqgyelQVGErgqnLSGGQRQNVALARALLLNPPILLL 644
Cdd:NF040873 76 D-LVAMGRWarrglwrrltRDDRAAVDDAlERVGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 814585811 645 DEPTSAMDNTGEERLKQRL-QSVIENKTVILVTHRASLLSLVDRLLVI 691
Cdd:NF040873 144 DEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
171-451 |
1.01e-15 |
|
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: 78.24 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVvpnQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18551 4 ALLLSLLGTAASLAQPLLVKNLIDAL---SAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAMKV----RP----ARVGSFAQNIHEF--QGMRDFLT-------SLTLASLIDLPFTLIILVVIAMLGghlvwipIIA 313
Cdd:cd18551 81 RLPVSFfdrrRSgdlvSRVTNDTTLLRELitSGLPQLVTgvltvvgAVVLMFLLDWVLTLVTLAVVPLAF-------LII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 314 FPlalgIGHMLQKPLTATLERTMALGAErqssLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNI 393
Cdd:cd18551 154 LP----LGRRIRKASKRAQDALGELSAA----LERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 394 TLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAK 451
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKAL 283
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
500-706 |
1.04e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQdiQLLAG---TLRD 576
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ--HHLTPegiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 nLVSGAR--YV---------DDEMVLQAAELAGVHEFARlhpqgyelqvgERGQNLSGGQRQNVALARALLLNPPILLLD 645
Cdd:PRK11231 96 -LVAYGRspWLslwgrlsaeDNARVNQAMEQTRINHLAD-----------RRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 646 EPTSAMD-NTGEE--RLKQRLQSviENKTVILVTH---RASllSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK11231 164 EPTTYLDiNHQVElmRLMRELNT--QGKTVVTVLHdlnQAS--RYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
500-696 |
1.10e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.97 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRhnIGYVAQDIQLLAG-TLRDNL 578
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSG----------ARYVDDEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:PRK10851 96 AFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPA-----------QLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 814585811 649 SAMDNTGEERLKQRLQSVIENK--TVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNI 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
488-700 |
1.23e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.98 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG--------VDIRQIdvSELRHN 559
Cdd:COG4161 8 INCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAI--RLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 IGYVAQDIQLLAG-TLRDNLVSGARYVDDeMVLQAAELAGVHEFARLHPQGYelqvGER-GQNLSGGQRQNVALARALLL 637
Cdd:COG4161 84 VGMVFQQYNLWPHlTVMENLIEAPCKVLG-LSKEQAREKAMKLLARLRLTDK----ADRfPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 638 NPPILLLDEPTSAMDntgEERLKQRLQSVIENK----TVILVTHRASLLSLV-DRLLVIDRGQILADG 700
Cdd:COG4161 159 EPQVLLFDEPTAALD---PEITAQVVEIIRELSqtgiTQVIVTHEVEFARKVaSQVVYMEKGRIIEQG 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
480-705 |
1.93e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.49 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 480 QGAMTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKL---LVGLYQPD--SGSLLVDGVDIRQIDVS 554
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQ---DIQLLagTLRDNLVSGARYvdDEMVLQAAELAGVHEFARLHPQGYElQVGER----GQNLSGGQRQ 627
Cdd:PRK14247 79 ELRRRVQMVFQipnPIPNL--SIFENVALGLKL--NRLVKSKKELQERVRWALEKAQLWD-EVKDRldapAGKLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 628 NVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTH---RASLLSlvDRLLVIDRGQILADGPKAA 704
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqQAARIS--DYVAFLYKGQIVEWGPTRE 231
|
.
gi 814585811 705 V 705
Cdd:PRK14247 232 V 232
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
489-697 |
2.52e-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: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD---SGSLLVDGvdiRQIDVSELRHNIGYVAQ 565
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 566 DIQLLAG-TLRDNL---------VSGARYVDDEMVLQAAELAGVHEFARlhpqgyelqvGERGQNLSGGQRQNVALARAL 635
Cdd:cd03234 89 DDILLPGlTVRETLtytailrlpRKSSDAIRKKRVEDVLLRDLALTRIG----------GNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 636 LLNPPILLLDEPTSAMDNTGEERLKQRL-QSVIENKTVILVTH--RASLLSLVDRLLVIDRGQIL 697
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
515-715 |
3.21e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 76.67 E-value: 3.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 515 IIGRSGSGKSSLAKLL------VGLYQPdSGSLLVDGVDIRQI-DVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYvdd 587
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLnrmndkVSGYRY-SGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRA--- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 588 EMVLQAAELAGVHEfARLHPQGYELQVGERGQN----LSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRL 663
Cdd:PRK14271 128 HKLVPRKEFRGVAQ-ARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 664 QSVIENKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAVMEALKKGQIS 715
Cdd:PRK14271 207 RSLADRLTVIIVTHNlAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETA 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
481-714 |
3.88e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.59 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 481 GAMTFREVDFTYPNQQNLALRGIN---LNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG----VDIRQI-D 552
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 553 VSELRHNIGYVAQ--DIQLLAGTLRDNLVSGARYV---DDEMVLQAAELAGV----HEFARLHPqgYELqvgergqnlSG 623
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLgenKQEAYKKVPELLKLvqlpEDYVKRSP--FEL---------SG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 624 GQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN--KTVILVTHRA-SLLSLVDRLLVIDRGQILADG 700
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVISIG 233
|
250
....*....|....*..
gi 814585811 701 PKAAV---MEALKKGQI 714
Cdd:PRK13645 234 SPFEIfsnQELLTKIEI 250
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
500-677 |
4.49e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 75.14 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLV 579
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 580 --SGARYVDDEMVLQAAELAgvhEFarlhpqGYELQVGERGQN-LSGGQRQNVALARALLLNPPILLLDEPTSAMDntge 656
Cdd:PRK10247 103 fpWQIRNQQPDPAIFLDDLE---RF------ALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITSALD---- 169
|
170 180
....*....|....*....|....*..
gi 814585811 657 ERLKQRLQSVI------ENKTVILVTH 677
Cdd:PRK10247 170 ESNKHNVNEIIhryvreQNIAVLWVTH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
474-696 |
4.67e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 474 LSRKALQGAMTFREVDFTYPNQ-----------QNL----ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDS 538
Cdd:COG1129 227 LTEDELVRLMVGRELEDLFPKRaaapgevvlevEGLsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADS 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 539 GSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQ----LLAGTLRDNL-------VSGARYVDDEMVLQAAElagvHEFARLH 606
Cdd:COG1129 307 GEIRLDGKPVRIRSPRDaIRAGIAYVPEDRKgeglVLDLSIRENItlasldrLSRGGLLDRRRERALAE----EYIKRLR 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 607 --PQGYELQVGergqNLSGGQRQNVALARALLLNPPILLLDEPT-----SAmdntgeerlKQRLQSVI-----ENKTVIL 674
Cdd:COG1129 383 ikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTrgidvGA---------KAEIYRLIrelaaEGKAVIV 449
|
250 260
....*....|....*....|....*.
gi 814585811 675 VThraS----LLSLVDRLLVIDRGQI 696
Cdd:COG1129 450 IS---SelpeLLGLSDRILVMREGRI 472
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
503-706 |
5.34e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.32 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQLLAG-TLRDNLVS 580
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYDNLMA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 581 GARYVDDEMVLQAAELAG--VHEFARLHPQGyelqvgERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEER 658
Cdd:PRK10895 102 VLQIRDDLSAEQREDRANelMEEFHIEHLRD------SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 814585811 659 LKQRLQSVIENKTVILVT-HRA-SLLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
505-708 |
6.09e-15 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 74.50 E-value: 6.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 505 LNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQidvseLRHNIGYVAQDIQL--------------- 569
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK-----GWRHIGYVPQRHEFawdfpisvahtvmsg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 570 ---LAGTLRDNLVSGARYVDDemvlqAAELAGVHEFARLhpqgyelQVGErgqnLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:TIGR03771 76 rtgHIGWLRRPCVADFAAVRD-----ALRRVGLTELADR-------PVGE----LSGGQRQRVLVARALATRPSVLLLDE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814585811 647 PTSAMDNTGEERLKQRLQSVI-ENKTVILVTHR-ASLLSLVDRLLVIDrGQILADGPKAAVMEA 708
Cdd:TIGR03771 140 PFTGLDMPTQELLTELFIELAgAGTAILMTTHDlAQAMATCDRVVLLN-GRVIADGTPQQLQDP 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
500-696 |
6.95e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.43 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDV---SELR-HNIGYVAQDIQLLAgTL- 574
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSFMLIP-TLn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 -RDN-----LVSGARyvDDEMVLQAAELAGvhefarlhpqgyELQVGER----GQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:PRK10584 105 aLENvelpaLLRGES--SRQSRNGAKALLE------------QLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 645 DEPTSAMDNTGEERLKQRLQSVIEN--KTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQL 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
500-677 |
7.93e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.75 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYvaQDIQLLAGTLRDNLV 579
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 580 SGARYV--DDEMVLQAAELAGVHEFARLhpqgyelqvgeRGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEE 657
Cdd:PRK13539 96 FWAAFLggEELDIAAALEAVGLAPLAHL-----------PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|.
gi 814585811 658 RLKQRLQSVIE-NKTVILVTH 677
Cdd:PRK13539 165 LFAELIRAHLAqGGIVIAATH 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
497-677 |
9.49e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 9.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKL------LVGLYQPDsGSLLVDGVDI--RQIDVSELRHNIGYVAQDIQ 568
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFRVE-GKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 569 LLAGTLRDNLVSGARY----VD-DEMV----LQAAELAGVHEFARlhpqgyelqvgERGQNLSGGQRQNVALARALLLNP 639
Cdd:PRK14243 102 PFPKSIYDNIAYGARIngykGDmDELVerslRQAALWDEVKDKLK-----------QSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 814585811 640 PILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVTH 677
Cdd:PRK14243 171 EVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTH 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
499-700 |
1.24e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.13 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQID---VSELrhNIGYVAQDIQLLAG-TL 574
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQL--GIGIIYQELSVIDElTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNL---------VSGARYVD-DEMVLQAAELagvhefarLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:PRK09700 98 LENLyigrhltkkVCGVNIIDwREMRVRAAMM--------LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 645 DEPTSAMDNTGEERL---KQRLQSviENKTVILVTHR-ASLLSLVDRLLVIDRGQILADG 700
Cdd:PRK09700 170 DEPTSSLTNKEVDYLfliMNQLRK--EGTAIVYISHKlAEIRRICDRYTVMKDGSSVCSG 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
485-709 |
1.30e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYV 563
Cdd:PRK11288 7 FDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLLAG-TLRDNLVSG-----ARYVDD-EMVLQAAElagvhEFARLhpqGYELQVGERGQNLSGGQRQNVALARALL 636
Cdd:PRK11288 85 YQELHLVPEmTVAENLYLGqlphkGGIVNRrLLNYEARE-----QLEHL---GVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 637 LNPPILLLDEPTSAMdntgEERLKQRLQSVI-----ENKTVILVTHRaslLSLVDRLlvIDRGQILADGPKAAVMEAL 709
Cdd:PRK11288 157 RNARVIAFDEPTSSL----SAREIEQLFRVIrelraEGRVILYVSHR---MEEIFAL--CDAITVFKDGRYVATFDDM 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
498-705 |
1.34e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 498 LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELR-HNIGYVAQDIQ----LLAG 572
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRLgrglVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 573 TLRDNLVSGARYVD----------DEMVLQAAELagVHEFaRLHPQGYELQVGergqNLSGGQRQNVALARALLLNPPIL 642
Cdd:COG3845 352 SVAENLILGRYRRPpfsrggfldrKAIRAFAEEL--IEEF-DVRTPGPDTPAR----SLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 643 LLDEPTSAMDNTGEERLKQRLqsvIE----NKTVILVthraS-----LLSLVDRLLVIDRGQILADGPKAAV 705
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRL---LElrdaGAAVLLI----SedldeILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
483-703 |
1.89e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.43 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQ---QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI----RQIDVSE 555
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 556 LRHNIGYVAQ--DIQLLAGTLRDNLVSGARY--VDDEMVLQAAelagvheFARLHPQGYELQVGERGQ-NLSGGQRQNVA 630
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNfkMNLDEVKNYA-------HRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 631 LARALLLNPPILLLDEPTSAMDNTGEE---RLKQRLQsVIENKTVILVTHRAS-LLSLVDRLLVIDRGQILADG-PKA 703
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRqvmRLLKSLQ-TDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTsPKE 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
501-696 |
1.94e-14 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.45 E-value: 1.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 501 RGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDgvDIRQIDVSELRHNIGYVAQDIQLLAG-TLRDNL- 578
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVFQSYALYPHlSVAENMs 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 ----VSGARYVD-DEMVLQAAELagvhefarlhpqgyeLQVGE----RGQNLSGGQRQNVALARALLLNPPILLLDEPTS 649
Cdd:PRK11000 98 fglkLAGAKKEEiNQRVNQVAEV---------------LQLAHlldrKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 650 AMDNTGE-------ERLKQRLQSvienkTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:PRK11000 163 NLDAALRvqmrieiSRLHKRLGR-----TMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
497-700 |
2.28e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.84 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRH----NIGYVAQDIQLLAG 572
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 573 -TLRDNLVSGARYVD------DEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPILLLD 645
Cdd:PRK10070 121 mTVLDNTAFGMELAGinaeerREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 646 EPTSAMDNTGEERLKQRLQSV--IENKTVILVTHRA-SLLSLVDRLLVIDRGQILADG 700
Cdd:PRK10070 190 EAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVG 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
500-699 |
3.99e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.54 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVS---ELR-HNIGYVAQDIQLLAG-TL 574
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNlvsgaryVDDEMVLQAAELAGVHEFAR--LHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMD 652
Cdd:PRK11629 105 LEN-------VAMPLLIGKKKPAEINSRALemLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 814585811 653 NTGEERLKQRLQ--SVIENKTVILVTHRASLLSLVDRLLVIDRGQILAD 699
Cdd:PRK11629 178 ARNADSIFQLLGelNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
484-708 |
4.98e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.90 E-value: 4.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQqnLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYV 563
Cdd:PRK10575 13 ALRNVSFRVPGR--TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDIQLLAGTLRDNLVSGARY-----------VDDEMVLQAAELAGVHEFA-RLHpqgyelqvgergQNLSGGQRQNVAL 631
Cdd:PRK10575 91 PQQLPAAEGMTVRELVAIGRYpwhgalgrfgaADREKVEEAISLVGLKPLAhRLV------------DSLSGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 632 ARALLLNPPILLLDEPTSAMDNTGEER---LKQRLqSVIENKTVILVTHRASLLS-LVDRLLVIDRGQILADGPKAAVME 707
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDvlaLVHRL-SQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMR 237
|
.
gi 814585811 708 A 708
Cdd:PRK10575 238 G 238
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
500-677 |
5.21e-14 |
|
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: 71.37 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDvSELRHNIGYVA-QDIQLLAGTLRDNL 578
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGhAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARYVDDEMVLQAAELAGVHEFARLhPQGYelqvgergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEER 658
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGFEDR-PVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 814585811 659 LKQRLQSVIE-NKTVILVTH 677
Cdd:cd03231 164 FAEAMAGHCArGGMVVLTTH 183
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-711 |
5.61e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 73.58 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI--RQIdvsELRHNIGYV-AQDIQL---Lag 572
Cdd:COG4586 37 AVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkRRK---EFARRIGVVfGQRSQLwwdL-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 573 TLRDNL--------VSGARYVD--DEMVlqaaELAGVHEFarlhpqgyeLQVGERgqNLSGGQRQNVALARALLLNPPIL 642
Cdd:COG4586 112 PAIDSFrllkaiyrIPDAEYKKrlDELV----ELLDLGEL---------LDTPVR--QLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 643 LLDEPTSAMD-NTgeerlKQRLQSVI------ENKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPkaavMEALKK 711
Cdd:COG4586 177 FLDEPTIGLDvVS-----KEAIREFLkeynreRGTTILLTSHDmDDIEALCDRVIVIDHGRIIYDGS----LEELKE 244
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
490-705 |
7.56e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 490 FTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG--VDIRQIDVSELRHNIGYVAQDI 567
Cdd:PRK13638 9 FRYQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 QL----------LAGTLRDNLVSG---ARYVDDEMVLQAAelagvhefarlhpQGYELQvgeRGQNLSGGQRQNVALARA 634
Cdd:PRK13638 87 EQqifytdidsdIAFSLRNLGVPEaeiTRRVDEALTLVDA-------------QHFRHQ---PIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 635 LLLNPPILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHRASLL-SLVDRLLVIDRGQILADGPKAAV 705
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
171-437 |
7.74e-14 |
|
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: 72.29 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGIC--GAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFER 248
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLAllLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 249 IVGMAMK---VRPA-----RVGSFAQNIHEFqgmrdflTSLTLASLIDLPFTLIILVVIAM-LGGHLVWIPIIAFPLALG 319
Cdd:pfam00664 84 ILRQPMSffdTNSVgellsRLTNDTSKIRDG-------LGEKLGLLFQSLATIVGGIIVMFyYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 320 IGHMLQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQ 399
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 814585811 400 VAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPL 437
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
482-703 |
8.65e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 72.55 E-value: 8.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTY-PNQ--QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIR----QIDVS 554
Cdd:PRK13641 2 SIKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQ--DIQLLAGTLRDNLVSGAR---YVDDEMVLQAAELagvhefarLHPQGYELQVGERGQ-NLSGGQRQN 628
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfgFSEDEAKEKALKW--------LKKVGLSEDLISKSPfELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 629 VALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSV-IENKTVILVTHRASLLS-LVDRLLVIDRGQILA-DGPKA 703
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKhASPKE 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
499-709 |
1.11e-13 |
|
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: 74.07 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLV----DGVDIRQIDVSE---LRHNIGYVAQDIQLLA 571
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgrAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 -GTLRDNLVsgaryvddemvlQAAELAGVHEFAR------LHPQGYELQVGERGQN-----LSGGQRQNVALARALLLNP 639
Cdd:TIGR03269 379 hRTVLDNLT------------EAIGLELPDELARmkavitLKMVGFDEEKAEEILDkypdeLSEGERHRVALAQVLIKEP 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 640 PILLLDEPTSAMDNTGEERLKQR-LQSVIE-NKTVILVTHRAS-LLSLVDRLLVIDRGQILADGPKAAVMEAL 709
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSiLKAREEmEQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
496-707 |
2.12e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 70.64 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD-----SGSLLVDGVDIRQIDVS--ELRHNIGYVAQDIQ 568
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 569 LLAG-TLRDNLVSGARYvdDEMVLQAAELAGVHEFARLHPQGYElQVGER----GQNLSGGQRQNVALARALLLNPPILL 643
Cdd:PRK14267 96 PFPHlTIYDNVAIGVKL--NGLVKSKKELDERVEWALKKAALWD-EVKDRlndyPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 644 LDEPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAVME 707
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVsDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
483-706 |
2.27e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 70.29 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIG 561
Cdd:PRK11614 6 LSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG-TLRDNLVSGARYVDDEMVLQaaELAGVHEfarLHPQGYELQVgERGQNLSGGQRQNVALARALLLNPP 640
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYE---LFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 641 ILLLDEPTSAMDNTGEERLKQRLQSV-IENKTVILVTHRAS-LLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
499-679 |
2.67e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 69.31 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELR--HNIGYVAQDIQLLagTLRD 576
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEniLYLGHLPGLKPEL--SALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGARYVDDE--MVLQAAELAGVHEFARLhPQGYelqvgergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNT 654
Cdd:TIGR01189 93 NLHFWAAIHGGAqrTIEDALAAVGLTGFEDL-PAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*.
gi 814585811 655 GEERLKQRLQSVIENK-TVILVTHRA 679
Cdd:TIGR01189 162 GVALLAGLLRAHLARGgIVLLTTHQD 187
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
480-701 |
4.03e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.30 E-value: 4.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 480 QGAMTFREVDFTYPNQQNlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQidvsELRHN 559
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 -IGYVAQ--DIQLLAGTLRDNLVSGARY-----------VDDEMVLQAAELAGVHEFArlhpqgyELQVGErgqnLSGGQ 625
Cdd:PRK15056 79 lVAYVPQseEVDWSFPVLVEDVVMMGRYghmgwlrrakkRDRQIVTAALARVDMVEFR-------HRQIGE----LSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 626 RQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSV-IENKTVILVTHRASLLSLVDRLLVIDRGQILADGP 701
Cdd:PRK15056 148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGP 224
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
499-677 |
7.60e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.96 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRqiDVSELRhniGYVAQDIQLLA-GTLRDN 577
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAER---GVVFQNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGAryvddemvlqaaELAGVHEFARLHPQGYEL-QVGERGQ------NLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:PRK11248 91 VAFGL------------QLAGVEKMQRLEIAHQMLkKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180
....*....|....*....|....*....
gi 814585811 651 MDNTGEERLKQRLQSVIEN--KTVILVTH 677
Cdd:PRK11248 159 LDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
499-707 |
1.22e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 70.99 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGL--YQPDSGSLL---------------------------------V 543
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepeeV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 544 DGVDIRQIDVSELRHNIGYVAQDIQLLAG--TLRDNLVSG---ARYVDDEMVLQAAELAGvhefarlhpqgyELQVGER- 617
Cdd:TIGR03269 95 DFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEAleeIGYEGKEAVGRAVDLIE------------MVQLSHRi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 618 ---GQNLSGGQRQNVALARALLLNPPILLLDEPTSAMD-NTGEERLKQRLQSVIENK-TVILVTHRASLLS-LVDRLLVI 691
Cdd:TIGR03269 163 thiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpQTAKLVHNALEEAVKASGiSMVLTSHWPEVIEdLSDKAIWL 242
|
250
....*....|....*.
gi 814585811 692 DRGQILADGPKAAVME 707
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVA 258
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
499-652 |
1.33e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.61 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQID---VSELRHNIGYVAQDI-------- 567
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNPygslnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 ---QLLAGTLRDN--LVSGARyvdDEMVLQAAELAGVH-EFARLHPQGYelqvgergqnlSGGQRQNVALARALLLNPPI 641
Cdd:PRK11308 110 kvgQILEEPLLINtsLSAAER---REKALAMMAKVGLRpEHYDRYPHMF-----------SGGQRQRIAIARALMLDPDV 175
|
170
....*....|.
gi 814585811 642 LLLDEPTSAMD 652
Cdd:PRK11308 176 VVADEPVSALD 186
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
500-677 |
1.64e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 67.12 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD---SGSLLVDGVDIRQIDVsELRHnIGYVAQDIQL------- 569
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA-EQRR-IGILFQDDLLfphlsvg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 570 --LAGTLRDNLVSGARyvdDEMVLQAAELAGVHEFARLHPQgyelqvgergqNLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:COG4136 95 enLAFALPPTIGRAQR---RARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 814585811 648 TSAMD-----NTGE---ERLKQRlqsvieNKTVILVTH 677
Cdd:COG4136 161 FSKLDaalraQFREfvfEQIRQR------GIPALLVTH 192
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
498-705 |
1.69e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 498 LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG--VDIRQIDVSeLRHNIGYVAQDIQLLAG-TL 574
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDA-IALGIGMVHQHFMLVPNlTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGARYVDDEMVLQAAELAGVHEFArlhpQGYELQV--GERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMd 652
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIRELS----ERYGLDVdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 653 nTGEErlKQRLQSVI-----ENKTVILVTHRasL---LSLVDRLLVIDRGQILADGPKAAV 705
Cdd:COG3845 173 -TPQE--ADELFEILrrlaaEGKSIIFITHK--LrevMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-692 |
1.91e-12 |
|
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: 67.82 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 506 NVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqidvselrhniGYVAQDIQL-LAGTLRDNLVSgary 584
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV------------SYKPQYIKAdYEGTVRDLLSS---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 585 VDDEMVLQA---AELAGVHEFARLhpqgYELQVGErgqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNtgEERLkq 661
Cdd:cd03237 85 ITKDFYTHPyfkTEIAKPLQIEQI----LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRL-- 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 814585811 662 RLQSVI------ENKTVILVTH---RASLLSlvDRLLVID 692
Cdd:cd03237 153 MASKVIrrfaenNEKTAFVVEHdiiMIDYLA--DRLIVFE 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
503-709 |
3.82e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGA 582
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 583 RYV-----------DDEMVLQAAELAGVHEFArlhpqgyelqvGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAM 651
Cdd:PRK10253 106 RYPhqplftrwrkeDEEAVTKAMQATGITHLA-----------DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 652 DNTGEERLKQRLQSVIENK--TVILVTHRAS-LLSLVDRLLVIDRGQILADG-PKAAVMEAL 709
Cdd:PRK10253 175 DISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGaPKEIVTAEL 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-708 |
3.87e-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: 69.33 E-value: 3.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKS----SLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRH----N 559
Cdd:COG4172 14 VAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 IGYVAQD------------------IQLLAGTLRDNlvsgARyvddEMVLQAAELAGVHEFARlHPQGYELQvgergqnL 621
Cdd:COG4172 94 IAMIFQEpmtslnplhtigkqiaevLRLHRGLSGAA----AR----ARALELLERVGIPDPER-RLDAYPHQ-------L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 622 SGGQRQNVALARALLLNPPILLLDEPTSAMDNTGE-------ERLKQRLqsvieNKTVILVTHRaslLSLV----DRLLV 690
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQaqildllKDLQREL-----GMALLLITHD---LGVVrrfaDRVAV 229
|
250
....*....|....*...
gi 814585811 691 IDRGQILADGPKAAVMEA 708
Cdd:COG4172 230 MRQGEIVEQGPTAELFAA 247
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
500-715 |
3.93e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.99 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLL---VGLYQPD---SGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAG- 572
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPHl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 573 TLRDNLvsgARYVDDEMVLQAAELAGVHEfARLHPQGYELQVGER----GQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:PRK14246 106 SIYDNI---AYPLKSHGIKEKREIKKIVE-ECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 649 SAMDNTGEERLKQRLQSVIENKTVILVTHRASLLSLV-DRLLVIDRGQILADG--------PKAAVMEALKKGQIS 715
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVaDYVAFLYNGELVEWGssneiftsPKNELTEKYVIGRIS 257
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
500-707 |
4.61e-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: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrqidvSEL------RHNIGYVAQDIQLLAG- 572
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-----THLpmhkraRLGIGYLPQEASIFRKl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 573 TLRDNLvsgaryvddEMVLQAAELAGVHEFARLHPQGYELQVGE----RGQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:COG1137 94 TVEDNI---------LAVLELRKLSKKEREERLEELLEEFGITHlrksKAYSLSGGERRRVEIARALATNPKFILLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 649 SAMD--NTGE-----ERLKQRLQSVienktviLVT-H--RASlLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:COG1137 165 AGVDpiAVADiqkiiRHLKERGIGV-------LITdHnvRET-LGICDRAYIISEGKVLAEGTPEEILN 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
499-700 |
5.93e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 5.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---------RHNIGYVAQDIql 569
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQHP-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 570 lAGTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYELQVG---ERGQNLSGGQRQNVALARALLLNPPILLLDE 646
Cdd:PRK11701 99 -RDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAAridDLPTTFSGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 647 PTSAMDNTGEERLKQRLQSVIE--NKTVILVTHR---ASLLSlvDRLLVIDRGQILADG 700
Cdd:PRK11701 178 PTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDlavARLLA--HRLLVMKQGRVVESG 234
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
171-450 |
5.97e-12 |
|
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: 67.06 E-value: 5.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAM----KVRPARVGS-FAQNIhefQGMRDFLTSlTLASLIDLPFTLIILVVIAM-LGGHLVWIPIIAFPLALGIGHML 324
Cdd:cd18552 84 RLPLsffdRNSSGDLISrITNDV---NQVQNALTS-ALTVLVRDPLTVIGLLGVLFyLDWKLTLIALVVLPLAALPIRRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 325 QKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVA 404
Cdd:cd18552 160 GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 814585811 405 MIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQA 450
Cdd:cd18552 240 VLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRG 285
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
499-691 |
8.03e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 8.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHnigyVAQDIQLLagtLRDNL 578
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA----VRSDIQMI---FQDPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VS-GARYVDDEMVlqaAELAGVHefarlHPQGYELQVGERGQNL------------------SGGQRQNVALARALLLNP 639
Cdd:PRK15079 109 ASlNPRMTIGEII---AEPLRTY-----HPKLSRQEVKDRVKAMmlkvgllpnlinryphefSGGQCQRIGIARALILEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 640 PILLLDEPTSAMDNTGEERLKQRLQSVIENK--TVILVTHRaslLSLV----DRLLVI 691
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHD---LAVVkhisDRVLVM 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
499-700 |
8.92e-12 |
|
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: 68.89 E-value: 8.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIrQIDVSELRHNIGYVAQ-DIQLLAGTLRDN 577
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQhNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGAryvddEMVLQAAELAGVHEFARLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEE 657
Cdd:TIGR01257 1024 ILFYA-----QLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 814585811 658 RLKQRLQSVIENKTVILVTHRASLLSLV-DRLLVIDRGQILADG 700
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSG 1142
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
496-708 |
1.22e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYqPDSGSLLVDGVDIRQIDVSEL---RHNIGYVAQD------ 566
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnssln 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 -----IQLLAGTLR---DNLVSGARyvdDEMVLQAAELAGvhefarLHPQGYELQVGErgqnLSGGQRQNVALARALLLN 638
Cdd:PRK15134 377 prlnvLQIIEEGLRvhqPTLSAAQR---EQQVIAVMEEVG------LDPETRHRYPAE----FSGGQRQRIAIARALILK 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 639 PPILLLDEPTSAMDNTGEERLKQRLQSVIENKTV--ILVTHRASLL-SLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK15134 444 PSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVrALCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
482-696 |
1.63e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.41 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQqNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSElrHNIG 561
Cdd:PRK11650 3 GLKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 562 YVAQDIQLLAG-TLRDNLVSG--ARYVD----DEMVLQAAELAGVHEFarlhpqgyeLQvgERGQNLSGGQRQNVALARA 634
Cdd:PRK11650 80 MVFQNYALYPHmSVRENMAYGlkIRGMPkaeiEERVAEAARILELEPL---------LD--RKPRELSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 635 LLLNPPILLLDEPTSAMDntgeerLKQRLQSVIE--------NKTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD------AKLRVQMRLEiqrlhrrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
488-700 |
1.82e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD---SGSLLVDGVDIRQIDVSELR----HNI 560
Cdd:PRK09473 20 VTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNklraEQI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 561 GYVAQDI------------QLLAGTLRDNLVSGARYVDDEM-VLQAAELAGVHEFARLHPQGYelqvgergqnlSGGQRQ 627
Cdd:PRK09473 100 SMIFQDPmtslnpymrvgeQLMEVLMLHKGMSKAEAFEESVrMLDAVKMPEARKRMKMYPHEF-----------SGGMRQ 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 628 NVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLS-LVDRLLVIDRGQILADG 700
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYG 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
497-701 |
2.22e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVD-----IRQIDVS------------ELRHN 559
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDvthrsIQQRDICmvfqsyalfphmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 560 IGYvAQDIQLLAGTLRDNLVSGAryvddemvLQAAELAGVHEfaRLHPQgyelqvgergqnLSGGQRQNVALARALLLNP 639
Cdd:PRK11432 99 VGY-GLKMLGVPKEERKQRVKEA--------LELVDLAGFED--RYVDQ------------ISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 640 PILLLDEPTSAMD-----NTGEE--RLKQRLqsvieNKTVILVTHRAS-LLSLVDRLLVIDRGQILADGP 701
Cdd:PRK11432 156 KVLLFDEPLSNLDanlrrSMREKirELQQQF-----NITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGS 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
484-708 |
2.32e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 64.81 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 484 TFREVDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYV 563
Cdd:PRK15112 13 TFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 564 AQDI-----------QLLAGTLRDN--LVSGARyvdDEMVLQAAELAGV-HEFARLHPQGyelqvgergqnLSGGQRQNV 629
Cdd:PRK15112 93 FQDPstslnprqrisQILDFPLRLNtdLEPEQR---EKQIIETLRQVGLlPDHASYYPHM-----------LAPGQKQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 630 ALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTV--ILVT-HRASLLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK15112 159 GLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTqHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
..
gi 814585811 707 EA 708
Cdd:PRK15112 239 AS 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
498-705 |
2.41e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 64.63 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 498 LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDI-----------------------RQIDVS 554
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvrtfqhvrlfREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ElrhNIgYVAQDIQLLAGTLRDNLVSGA-RYVDDEMVLQAA---ELAGVHEFARlHPQGyelqvgergqNLSGGQRQNVA 630
Cdd:PRK11300 99 E---NL-LVAQHQQLKTGLFSGLLKTPAfRRAESEALDRAAtwlERVGLLEHAN-RQAG----------NLAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 631 LARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASL-LSLVDRLLVIDRGQILADGPKAAV 705
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLvMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
500-701 |
2.86e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.61 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD---SGSLLVDGvdiRQIDVSELRHNIGYVAQDiQLLAGTL-- 574
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNG---MPIDAKEMRAISAYVQQD-DLFIPTLtv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGARYVDDEMVLQAAELAGVHEFAR----LHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQalglRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 651 MDNTGEERLKQRLQSVIEN-KTVILVTHRAS--LLSLVDRLLVIDRGQILADGP 701
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKgKTIICTIHQPSseLFELFDKIILMAEGRVAYLGS 250
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
507-692 |
3.01e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDgvdirqIDVSelrhnigYVAQDIQL-LAGTLRDNLVSGARYV 585
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIS-------YKPQYIKPdYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 586 DDEMVLqaaelagvHEFAR---LHPQgYELQVGErgqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNtgEERLK-- 660
Cdd:PRK13409 429 GSSYYK--------SEIIKplqLERL-LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAva 493
|
170 180 190
....*....|....*....|....*....|....*
gi 814585811 661 QRLQSVIEN--KTVILVTHRASLLSLV-DRLLVID 692
Cdd:PRK13409 494 KAIRRIAEEreATALVVDHDIYMIDYIsDRLMVFE 528
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
491-695 |
3.12e-11 |
|
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: 66.50 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 491 TYPNQQNLaLRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSG-SLLVDGVdirqidvselrhNIGYVAQDIQL 569
Cdd:TIGR03719 13 VVPPKKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGeARPQPGI------------KVGYLPQEPQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 570 -LAGTLRDNLVSG--------ARY---------VDDEMVLQAAELA---------GVHEFA----------RLHPqgYEL 612
Cdd:TIGR03719 80 dPTKTVRENVEEGvaeikdalDRFneisakyaePDADFDKLAAEQAelqeiidaaDAWDLDsqleiamdalRCPP--WDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 613 QVGergqNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVieNKTVILVTH-RASLLSLVDRLLVI 691
Cdd:TIGR03719 158 DVT----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY--PGTVVAVTHdRYFLDNVAGWILEL 231
|
....
gi 814585811 692 DRGQ 695
Cdd:TIGR03719 232 DRGR 235
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
483-706 |
3.65e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.95 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGY 562
Cdd:COG4604 2 IEIKNVSKRYGGKV--VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAG-TLRDnLVSGARY---------VDDEMVLQAAELAGVHEFARLHpqgyelqVGErgqnLSGGQRQNVALA 632
Cdd:COG4604 80 LRQENHINSRlTVRE-LVAFGRFpyskgrltaEDREIIDEAIAYLDLEDLADRY-------LDE----LSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 633 RALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHR---ASLLSlvDRLLVIDRGQILADGPKAAVM 706
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLHDinfASCYA--DHIVAMKDGRVVAQGTPEEII 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
482-677 |
3.84e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.29 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 482 AMTFREVDFTYPNQQnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDS-----GSLLVDGVDI--RQIDVS 554
Cdd:PRK14258 7 AIKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 555 ELRHNIGYVAQDIQLLAGTLRDNLVSGARYV--------DD--EMVLQAAELAGVHEfARLHPQGYELqvgergqnlSGG 624
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpkleiDDivESALKDADLWDEIK-HKIHKSALDL---------SGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 625 QRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVI--ENKTVILVTH 677
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSH 209
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
507-692 |
3.98e-11 |
|
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: 66.35 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDgvdirqIDVSelrHNIGYVAQDIQllaGTLRDNL--VSGARY 584
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKIS---YKPQYISPDYD---GTVEEFLrsANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 585 vdDEMVLQaaelagvHEFAR---LHPQgYELQVGErgqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNtgEERLK- 660
Cdd:COG1245 431 --GSSYYK-------TEIIKplgLEKL-LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAv 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 814585811 661 -QRLQSVIEN--KTVILVTHRASLLSLV-DRLLVID 692
Cdd:COG1245 495 aKAIRRFAENrgKTAMVVDHDIYLIDYIsDRLMVFE 530
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
499-707 |
4.96e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 65.62 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDS--GSLLVDGVDIRQIDVSEL-RHNIGYVAQDIQLLAG-TL 574
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNL-------VSGARYVDDEMVLQAAELAgvhEFARLHPQGYELQVGERGqnlsGGQRQNVALARALLLNPPILLLDEP 647
Cdd:TIGR02633 96 AENIflgneitLPGGRMAYNAMYLRAKNLL---RELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 648 TSAMDNTGEERLKQRLQSV-IENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAVME 707
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVKAVcDTICVIRDGQHVATKDMSTMSE 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
501-705 |
5.37e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.46 E-value: 5.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 501 RGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQ----LLAGTLR 575
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDRQssglYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNlVSGARYVDDEMVLQAAELAGVHEfaRLHPQ-GYELQVGERG-QNLSGGQRQNVALARALLLNPPILLLDEPTSAMDN 653
Cdd:PRK15439 360 WN-VCALTHNRRGFWIKPARENAVLE--RYRRAlNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 654 TGEERLKQRLQSVIENKTVILVThrASLLS----LVDRLLVIDRGQILADGPKAAV 705
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFI--SSDLEeieqMADRVLVMHQGEISGALTGAAI 490
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
500-712 |
5.97e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.16 E-value: 5.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGL--YQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQD---------- 566
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDErARAGIFLAFQYpveipgvsvs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 --IQLLAGTLRDNLVSGARYVDdeMVLQAAELAGV-HEFArlhpqgyelqvgERGQN--LSGGQRQNVALARALLLNPPI 641
Cdd:COG0396 96 nfLRTALNARRGEELSAREFLK--LLKEKMKELGLdEDFL------------DRYVNegFSGGEKKRNEILQMLLLEPKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 642 LLLDEPTSAMD-------NTGEERLKQrlqsviENKTVILVTHRASLLSLV--DRLLVIDRGQILADGPKAAVMEALKKG 712
Cdd:COG0396 162 AILDETDSGLDidalrivAEGVNKLRS------PDRGILIITHYQRILDYIkpDFVHVLVDGRIVKSGGKELALELEEEG 235
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-450 |
6.41e-11 |
|
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: 64.07 E-value: 6.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVV----PNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLF 246
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDDVLiqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 247 ERIVGMAM----KVRP----ARVGSFAQNIHEF--QGMRDFLTSLtlaslidlpFTLI-ILVVIAMLGGHLVWIPIIAFP 315
Cdd:cd18563 84 EHLQRLSLsffdKRQTgslmSRVTSDTDRLQDFlsDGLPDFLTNI---------LMIIgIGVVLFSLNWKLALLVLIPVP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 316 LALGIGHMLQKPLTATLERTMALGAERQSSLIETLAGLDAVKV---NNAESERqyqWEQTIGTLSRLELRVKVLSGLAMN 392
Cdd:cd18563 155 LVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAfgqEKREIKR---FDEANQELLDANIRAEKLWATFFP 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 393 ITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQA 450
Cdd:cd18563 232 LLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRA 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
417-694 |
7.11e-11 |
|
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: 66.19 E-value: 7.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 417 ALSMGGLVacYMLsgraLGPLAQLSGLLTRYQQAKVTMVSVDQMMELPQERnydERPLSRKALQGAMTFREVDFTYPNQQ 496
Cdd:TIGR01257 1881 AMAVEGVV--YFL----LTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEER---QRIISGGNKTDILRLNELTKVYSGTS 1951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYVAQ-DI--QLLAGt 573
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQfDAidDLLTG- 2029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 lRDNLVSGARYVDdemvLQAAELAGVHEFArLHPQGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDN 653
Cdd:TIGR01257 2030 -REHLYLYARLRG----VPAEEIEKVANWS-IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 814585811 654 TGEERLKQRLQSVI-ENKTVILVTHR-ASLLSLVDRLLVIDRG 694
Cdd:TIGR01257 2104 QARRMLWNTIVSIIrEGRAVVLTSHSmEECEALCTRLAIMVKG 2146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
499-651 |
7.72e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.95 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYqPD---SGSLLVDGVDIRQIDVSELRHN-IGYVAQDIQLLAG-T 573
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQELALVKElS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDN------LVSGARYVDDEMVLQAAELagvheFARLhpqGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:PRK13549 99 VLENiflgneITPGGIMDYDAMYLRAQKL-----LAQL---KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
....
gi 814585811 648 TSAM 651
Cdd:PRK13549 171 TASL 174
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
500-709 |
1.19e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQllagtlRDNL 578
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRK------RDGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARyVDDEMVLQA--------------AELAGVHEFARLhpqgYELQVGERGQ---NLSGGQRQNVALARALLLNPPI 641
Cdd:PRK10762 342 VLGMS-VKENMSLTAlryfsraggslkhaDEQQAVSDFIRL----FNIKTPSMEQaigLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 642 LLLDEPTSAMDNTGEERLKQRL-QSVIENKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKA-AVMEAL 709
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLInQFKAEGLSIILVSSEmPEVLGMSDRILVMHEGRISGEFTREqATQEKL 487
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
261-454 |
1.37e-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: 62.85 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 261 VGSFAQNIHEFQGMRDFLTSLTLASLIDLpFTLIILVVIAM----------LGG---HLVWIpiiafplalgighMLQKP 327
Cdd:cd18571 98 TGDILQRINDHSRIESFLTSSSLSILFSL-LNLIVFSIVLAyynltiflifLIGsvlYILWI-------------LLFLK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 328 LTATLE-RTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMI 406
Cdd:cd18571 164 KRKKLDyKRFDLSSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKNILIT 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 814585811 407 IFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTM 454
Cdd:cd18571 244 FLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFIQSLQDAKISL 291
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
168-452 |
2.19e-10 |
|
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: 62.06 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 168 YADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFE 247
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 248 RIVGMAM----KVRP----ARVGSFAQNIHEF--QGMRDFLTSLTLASL-------IDLPFTLIILVViamlgghlvwIP 310
Cdd:cd18542 81 HLQRLSFsfhdKARTgdlmSRCTSDVDTIRRFlaFGLVELVRAVLLFIGaliimfsINWKLTLISLAI----------IP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 311 IIAFpLALGIGHMLQKPLTATLERTMALGAERQssliETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLA 390
Cdd:cd18542 151 FIAL-FSYVFFKKVRPAFEEIREQEGELNTVLQ----ENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKY 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 391 MNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKV 452
Cdd:cd18542 226 WPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASA 287
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
171-456 |
4.57e-10 |
|
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: 61.25 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDR--VVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFER 248
Cdd:cd18544 4 ALLLLLLATALELLGPLLIKRAIDDyiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 249 IVGMAMKV---RPA-----RVGSFAQNIhefqgmRDFLTSLTLASLIDLpFTLI-ILVVIAMLGGHLVWIPIIAFPLALG 319
Cdd:cd18544 84 IQRLPLSFfdrTPVgrlvtRVTNDTEAL------NELFTSGLVTLIGDL-LLLIgILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 320 IGHMLQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQ 399
Cdd:cd18544 157 ATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 400 VAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAkvtMVS 456
Cdd:cd18544 237 LALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSA---MAS 290
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
499-707 |
6.73e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdiRQIDVSELRHN----IGYVAQDIQLLAG-T 573
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELNLIPQlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGARYVD-------DEMVLQAAELagvheFARLH-PQGYELQVGErgqnLSGGQRQNVALARALLLNPPILLLD 645
Cdd:PRK10762 96 IAENIFLGREFVNrfgridwKKMYAEADKL-----LARLNlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 646 EPTSAMDNTGEERLKqrlqSVI-----ENKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAVME 707
Cdd:PRK10762 167 EPTDALTDTETESLF----RVIrelksQGRGIVYISHRlKEIFEICDDVTVFRDGQFIAEREVADLTE 230
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
171-450 |
7.73e-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: 350020 [Multi-domain] Cd Length: 289 Bit Score: 60.58 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAMKV-RPARVGSFAQNI-HEFQGMRDFLTSlTLASLIDLPFTLIILVVIA----------MLGGhlvwIPIIAFpLAL 318
Cdd:cd18576 81 RLPLSFfHERRVGELTSRLsNDVTQIQDTLTT-TLAEFLRQILTLIGGVVLLffiswkltllMLAT----VPVVVL-VAV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 319 GIGHMLQKPLTATLERTmalgAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQ 398
Cdd:cd18576 155 LFGRRIRKLSKKVQDEL----AEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 814585811 399 QVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQA 450
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKA 282
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
499-651 |
9.35e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 61.67 E-value: 9.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDI-QLLAGTLRD 576
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELnLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGaRY------VDDEMVLQAAELAgvheFARLhpqGYELQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:PRK10982 93 NMWLG-RYptkgmfVDQDKMYRDTKAI----FDEL---DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSS 164
|
.
gi 814585811 651 M 651
Cdd:PRK10982 165 L 165
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
487-681 |
1.18e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 487 EVDFTYPNQqnLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQiDVSELRHNIGYVAQD 566
Cdd:PRK13540 6 ELDFDYHDQ--PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQLLAG-TLRDNLVSGARYVDDEMvlqaaelaGVHEFARLHPQGYELQVgeRGQNLSGGQRQNVALARALLLNPPILLLD 645
Cdd:PRK13540 83 SGINPYlTLRENCLYDIHFSPGAV--------GITELCRLFSLEHLIDY--PCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 814585811 646 EPTSAMDNTGEERLKQRLQSVIENKTVILVTHRASL 681
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDL 188
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
168-454 |
1.24e-09 |
|
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: 60.13 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 168 YADAIAASLVINLIALAAPLFVMNVYDRVVPNQATAT---LWMLAIGICGAYLFDLLLKS----LRSLCLDLAGKKTDLI 240
Cdd:cd18554 1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLdekVYKLFTIIGIMFFIFLILRPpveyYRQYFAQWIANKILYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 241 ISATLFERIVGMAMKV----RPARVGSfaQNIHEFQGMRDFLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPL 316
Cdd:cd18554 81 IRKDLFDHLQKLSLRYyannRSGEIIS--RVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 317 ALGIGHMLQKPL-TATLERTMALgAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITL 395
Cdd:cd18554 159 YILAVKYFFGRLrKLTKERSQAL-AEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 396 LIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAKVTM 454
Cdd:cd18554 238 TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASM 296
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
500-696 |
1.48e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.06 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSllvdgvdirqIDVSElRHNIGYVAQD------------- 566
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT----------VKWSE-NANIGYYAQDhaydfendltlfd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 -----------IQLLAGTLRDNLVSGaryvdDEMVLQAAELAGvhefarlhpqgyelqvGERGQNLSGG---QRQNVALa 632
Cdd:PRK15064 404 wmsqwrqegddEQAVRGTLGRLLFSQ-----DDIKKSVKVLSG----------------GEKGRMLFGKlmmQKPNVLV- 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 633 ralllnppillLDEPTSAMDNTGEERLKQRLqsviEN--KTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:PRK15064 462 -----------MDEPTNHMDMESIESLNMAL----EKyeGTLIFVSHdREFVSSLATRIIEITPDGV 513
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-443 |
2.60e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 59.03 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18550 4 VLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAMK--VRpARVGSFAQNIH-EFQGMRDFLTSlTLASLIDLPFTLIiLVVIAMLGghLVW----IPIIAFPLALGIGHM 323
Cdd:cd18550 84 RMSLAffTR-TRTGEIQSRLNnDVGGAQSVVTG-TLTSVVSNVVTLV-ATLVAMLA--LDWrlalLSLVLLPLFVLPTRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 324 LQKPLTATLERTMALGAERQSSLIETL--AGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVA 401
Cdd:cd18550 159 VGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIG 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 814585811 402 GVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGL 443
Cdd:cd18550 239 PALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNI 280
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
501-708 |
4.26e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 501 RGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD----SGSLLVDGV-----DIRQIDVSELRHNIGYVAQDIQLLA 571
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKpvapcALRGRKIATIMQNPRSAFNPLHTMH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 GTLRDNLVSGARYVDDEMVLQAAELAGVHEFARLhPQGYELQvgergqnLSGGQRQNVALARALLLNPPILLLDEPTSAM 651
Cdd:PRK10418 100 THARETCLALGKPADDATLTAALEAVGLENAARV-LKLYPFE-------MSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 652 DNTGEERLKQRLQSVIENKT--VILVTHRASLLS-LVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRAlgMLLVTHDMGVVArLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
497-561 |
4.62e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 4.62e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVG--LYQPDSGSLLVDGVDIRQIDvSELRHNIG 561
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE-PEERAHLG 85
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
489-706 |
5.24e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDS--GSLLVDGvdiRQIDVSELRHnIGYVAQD 566
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN---RKPTKQILKR-TGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQLLAG-TLRDNLV-----------------SGARYVDDEMVLQAAELAGV-HEFARlhpqgyelqvgergqNLSGGQRQ 627
Cdd:PLN03211 149 DILYPHlTVRETLVfcsllrlpksltkqekiLVAESVISELGLTKCENTIIgNSFIR---------------GISGGERK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 628 NVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIEN-KTVILVTHRAS--LLSLVDRLLVIDRGQILADGPKAA 704
Cdd:PLN03211 214 RVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKgKTIVTSMHQPSsrVYQMFDSVLVLSEGRCLFFGKGSD 293
|
..
gi 814585811 705 VM 706
Cdd:PLN03211 294 AM 295
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
503-699 |
6.71e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDS-GSLLVDG--VDIRQIDVSeLRHNIGYVAQD-----IQLLAGTL 574
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGkpVKIRNPQQA-IAQGIAMVPEDrkrdgIVPVMGVG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RD-NLVSGARYVDDEMVLQAAELAGVHEF-ARL-----HPqgyELQVGergqNLSGGQRQNVALARALLLNPPILLLDEP 647
Cdd:PRK13549 360 KNiTLAALDRFTGGSRIDDAAELKTILESiQRLkvktaSP---ELAIA----RLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 648 TSAMD-NTGEERLKQRLQSVIENKTVILVTHR-ASLLSLVDRLLVIDRGQILAD 699
Cdd:PRK13549 433 TRGIDvGAKYEIYKLINQLVQQGVAIIVISSElPEVLGLSDRVLVMHEGKLKGD 486
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
485-693 |
7.49e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 58.99 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 485 FREVDFTYPNQQNLALRgINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqidvselRHNIGYVA 564
Cdd:TIGR00954 454 FENIPLVTPNGDVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVP 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 QDIQLLAGTLRDNLVsgarYVD--DEMV---LQAAELAGVHEFARLHpqgYELQ-------VGERGQNLSGGQRQNVALA 632
Cdd:TIGR00954 522 QRPYMTLGTLRDQII----YPDssEDMKrrgLSDKDLEQILDNVQLT---HILEreggwsaVQDWMDVLSGGEKQRIAMA 594
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 633 RALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVieNKTVILVTHRASLLSLVDRLLVIDR 693
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
500-656 |
1.65e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 55.89 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqidvsELRhnIGYVAQDIQL---LAGTLRD 576
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------KLR--IGYVPQKLYLdttLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 --NLVSGARYVDDEMVLQAAELAGVHEFARlhpqgyelqvgergQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDNT 654
Cdd:PRK09544 89 flRLRPGTKKEDILPALKRVQAGHLIDAPM--------------QKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVN 154
|
..
gi 814585811 655 GE 656
Cdd:PRK09544 155 GQ 156
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
500-703 |
3.58e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 3.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVdiRQIDVSELR-HNIG--YVAQDIQLLAG-TLR 575
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKaHQLGiyLVPQEPLLFPNlSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSG-ARYVDDEMVLQA--AELaGVHefARLHPQGYELQVGErgqnlsggqRQNVALARALLLNPPILLLDEPTSAMD 652
Cdd:PRK15439 105 ENILFGlPKRQASMQKMKQllAAL-GCQ--LDLDSSAGSLEVAD---------RQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 653 NTGEERLKQRLQSVIENKT-VILVTHRAS-LLSLVDRLLVIDRGQILADGPKA 703
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVgIVFISHKLPeIRQLADRISVMRDGTIALSGKTA 225
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
494-709 |
3.80e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 494 NQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVG-LY-QPDSGSLLVDGVDIRQIDVSE-LRHNIGYVAQDIQ-- 568
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYgRNISGTVFKDGKEVDVSTVSDaIDAGLAYVTEDRKgy 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 569 --LLAGTLRDNL-------VSGARYVDDEMVLQAAElagvhEF-ARLH---PQGYElQVGergqNLSGGQRQNVALARAL 635
Cdd:NF040905 350 glNLIDDIKRNItlanlgkVSRRGVIDENEEIKVAE-----EYrKKMNiktPSVFQ-KVG----NLSGGNQQKVVLSKWL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 636 LLNPPILLLDEPTSAMDnTGEerlKQRLQSVI-----ENKTVILVThraS----LLSLVDRLLVIDRGQILADGPKA-AV 705
Cdd:NF040905 420 FTDPDVLILDEPTRGID-VGA---KYEIYTIInelaaEGKGVIVIS---SelpeLLGMCDRIYVMNEGRITGELPREeAS 492
|
....
gi 814585811 706 MEAL 709
Cdd:NF040905 493 QERI 496
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
344-452 |
4.08e-08 |
|
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: 55.19 E-value: 4.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 344 SSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGL 423
Cdd:cd18546 179 ADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVL 258
|
90 100
....*....|....*....|....*....
gi 814585811 424 VACYMLSGRALGPLAQLSGLLTRYQQAKV 452
Cdd:cd18546 259 VAFLLYLRRFFAPIQQLSQVFDSYQQARA 287
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
488-700 |
6.65e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG----------VDIRQIDVSELR 557
Cdd:PRK10261 20 IAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 558 HNIG----------------------YVAQDIQLLAGTLRDNLVSGARYVDDEMVLQAAELAgvheFARLHPQgyelqvg 615
Cdd:PRK10261 100 HVRGadmamifqepmtslnpvftvgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTI----LSRYPHQ------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 616 ergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQrLQSVIENKT---VILVTHRASLLS-LVDRLLVI 691
Cdd:PRK10261 169 -----LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQ-LIKVLQKEMsmgVIFITHDMGVVAeIADRVLVM 242
|
....*....
gi 814585811 692 DRGQILADG 700
Cdd:PRK10261 243 YQGEAVETG 251
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
500-706 |
6.69e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 6.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVG-LYQPD-------SGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLA 571
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 GTLRDNLVSGARY-----------VDDEMVLQAAELAGVhefarlhpqgyELQVGERGQNLSGGQRQNVALARA------ 634
Cdd:PRK13547 97 AFSAREIVLLGRYpharragalthRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVlaqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 635 ---LLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLSL-VDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK13547 166 phdAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
497-652 |
6.71e-08 |
|
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: 55.71 E-value: 6.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 497 NLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLV-DGVDirqidvselrhnIGYVAQDiqllagtlR 575
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVK------------LAYVDQS--------R 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNL---------VSGAryvDDEMVLQAAELAGVHEFARLHPQGYELQ--VGErgqnLSGGQRQNVALARALLLNPPILLL 644
Cdd:TIGR03719 395 DALdpnktvweeISGG---LDIIKLGKREIPSRAYVGRFNFKGSDQQkkVGQ----LSGGERNRVHLAKTLKSGGNVLLL 467
|
....*...
gi 814585811 645 DEPTSAMD 652
Cdd:TIGR03719 468 DEPTNDLD 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
503-699 |
7.63e-08 |
|
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: 55.60 E-value: 7.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD-SGSLLVDG--VDIRQIdVSELRHNIGYVAQD------IQLLAGT 573
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNP-AQAIRAGIAMVPEDrkrhgiVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGARYVDDEMVLQAAELAGV-HEFARLHPQGY--ELQVGergqNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRIDAAAELQIIgSAIQRLKVKTAspFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 814585811 651 MDNTGE-ERLKQRLQSVIENKTVILVTHR-ASLLSLVDRLLVIDRGQILAD 699
Cdd:TIGR02633 434 VDVGAKyEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKGD 484
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
20-133 |
8.79e-08 |
|
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: 51.23 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 20 DPLLDGLLTLCSLHYKPASRAMLTTGLPLAAQRLSAELLPRAAARAGLQGRLLQRKLEQIPSIALPAMLLLKEGRSAVLL 99
Cdd:cd02259 6 DCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLPALLLWKQGHFVILY 85
|
90 100 110
....*....|....*....|....*....|....
gi 814585811 100 GWEGDTaRLLLSESDGGEVQVSRETLSQDYSGRV 133
Cdd:cd02259 86 GADKGQ-VLIADPLEEGPVTLSESELEERWTGHW 118
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
500-696 |
9.74e-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: 53.04 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGL---YQPDSGSLLVDGVDIRQIDvSELRHNIGYVAQD---IQLLagT 573
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFA-EKYPGEIIYVSEEdvhFPTL--T 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGARYVDDEMVlqaaelagvhefarlhpqgyelqvgeRGqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDN 653
Cdd:cd03233 100 VRETLDFALRCKGNEFV--------------------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 814585811 654 TGEERLKQRLQSV--IENKTVILVTHRAS--LLSLVDRLLVIDRGQI 696
Cdd:cd03233 152 STALEILKCIRTMadVLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQ 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
503-708 |
1.05e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.92 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdiRQIDVSELRHNI--GYV-------AQDIQLLAgT 573
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIMlcpedrkAEGIIPVH-S 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 574 LRDNLVSGAR--YVDDEMVLQAAELAgvhEFARLHPQGYELQVGERGQ---NLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:PRK11288 348 VADNINISARrhHLRAGCLINNRWEA---ENADRFIRSLNIKTPSREQlimNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 649 SAMDnTGEerlKQRLQSVIEN-----KTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK11288 425 RGID-VGA---KHEIYNVIYElaaqgVAVLFVSSDlPEVLGVADRIVVMREGRIAGELAREQATER 486
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
171-450 |
1.19e-07 |
|
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: 53.72 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 G--MAM--KVRP----ARVGSFAQNIHEF------QGMRDFLTslTLASLIDLPF-----TLIILVViamlgghlvwIPI 311
Cdd:cd18557 81 RqeIAFfdKHKTgeltSRLSSDTSVLQSAvtdnlsQLLRNILQ--VIGGLIILFIlswklTLVLLLV----------IPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 312 IAfplalgIGHMLQKPLTATLERTMALGAERQSSLI-ETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLA 390
Cdd:cd18557 149 LL------IASKIYGRYIRKLSKEVQDALAKAGQVAeESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALF 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 391 MNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQA 450
Cdd:cd18557 223 QGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKA 282
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
500-695 |
1.27e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSG-SLLVDGVdirqidvselrhNIGYVAQDIQL-LAGTLRDN 577
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGI------------KVGYLPQEPQLdPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSG--------ARY---------VDDEM--------VLQAA-ELAGVH------EFA----RLHPqgYELQVGergqNL 621
Cdd:PRK11819 91 VEEGvaevkaalDRFneiyaayaePDADFdalaaeqgELQEIiDAADAWdldsqlEIAmdalRCPP--WDAKVT----KL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 622 SGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVieNKTVILVTHrasllslvDR---------LLVID 692
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY--PGTVVAVTH--------DRyfldnvagwILELD 234
|
...
gi 814585811 693 RGQ 695
Cdd:PRK11819 235 RGR 237
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
496-696 |
1.76e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 496 QNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSL-LVDGVdirqidvselrhNIGYVAQDiQLlaGTL 574
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------------KLGYFAQH-QL--EFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RdnlvsgaryvDDEMVLQaaelagvhEFARLHPQGYELQ--------------VGERGQNLSGGQRQNVALARALLLNPP 640
Cdd:PRK10636 389 R----------ADESPLQ--------HLARLAPQELEQKlrdylggfgfqgdkVTEETRRFSGGEKARLVLALIVWQRPN 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 814585811 641 ILLLDEPTSAMDNTGEERLKQRLQSvIENKTVILVTHRASLLSLVDRLLVIDRGQI 696
Cdd:PRK10636 451 LLLLDEPTNHLDLDMRQALTEALID-FEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
473-694 |
1.86e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 473 PLSRKALQGAMTF---REVDFTYpnqqnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLY--QPDSGSllvdgVD 547
Cdd:COG2401 22 DLSERVAIVLEAFgveLRVVERY------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGC-----VD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 548 IRQIDVSELRhnigyvaqdiqllagTLRDNLVSGARYVDDEMVLQAAELAGVHEFARlhpqgyelqvgeRGQNLSGGQRQ 627
Cdd:COG2401 91 VPDNQFGREA---------------SLIDAIGRKGDFKDAVELLNAVGLSDAVLWLR------------RFKELSTGQKF 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 628 NVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLLSLV--DRLLVIDRG 694
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARraGITLVVATHHYDVIDDLqpDLLIFVGYG 214
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
505-696 |
2.01e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 505 LNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDgvdiRQIDVSEL-----RHNIG----YVAQDIQLLAGTLR 575
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLqqdppRNVEGtvydFVAEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 D-----NLVsgARYVDDEMVLQAAELAGVHEfarlHPQGYEL---------QVGERGQ----NLSGGQRQNVALARALLL 637
Cdd:PRK11147 100 RyhdisHLV--ETDPSEKNLNELAKLQEQLD----HHNLWQLenrinevlaQLGLDPDaalsSLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 638 NPPILLLDEPTSAMDNTGEERLKQRLQSVieNKTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLEGFLKTF--QGSIIFISHdRSFIRNMATRIVDLDRGKL 231
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
171-450 |
2.72e-07 |
|
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: 52.86 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFE--- 247
Cdd:cd18545 5 ALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFShlq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 248 ---------RIVGMAMkvrpARVgsfaqnIHEFQGMRDFLTSLTLASLIDLpFTLIILVVIaMLGGH-------LVWIPI 311
Cdd:cd18545 85 klsfsffdsRPVGKIL----SRV------INDVNSLSDLLSNGLINLIPDL-LTLVGIVII-MFSLNvrlalvtLAVLPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 312 IAFpLALGIGHMLQKPLTATLERTMALGAerqsSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAM 391
Cdd:cd18545 153 LVL-VVFLLRRRARKAWQRVRKKISNLNA----YLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFW 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 392 NITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQA 450
Cdd:cd18545 228 PLVELISALGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSA 286
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
165-449 |
4.19e-07 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 52.07 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 165 RWLYADaIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKK--TDLiiS 242
Cdd:cd18549 2 KLFFLD-LFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARieTDM--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 243 ATLFERI------------VGMAMkvrpARVGSFAQNIHEF--QGMRDFLTS-LTLA------SLIDLPFTLIILVVIam 301
Cdd:cd18549 79 RDLFEHLqklsfsffdnnkTGQLM----SRITNDLFDISELahHGPEDLFISiITIIgsfiilLTINVPLTLIVFALL-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 302 lgghlvwipiiafPLALGIGHMLQKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLEL 381
Cdd:cd18549 153 -------------PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKK 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 382 RV-KVLSGLAMNITLLIQqVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQ 449
Cdd:cd18549 220 KAyKAMAYFFSGMNFFTN-LLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
499-708 |
6.29e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.05 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKS--SLAklLVGLY----QPDSGSLLVDGVDIRQIDVSELRHNIGY-VAQDIQLLA 571
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsSLA--IMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLVGAeVAMIFQDPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 GTLRDNLVSGaryvddemvLQAAELAGVHE---FARLHPQGYEL--QVG-----ER----GQNLSGGQRQNVALARALLL 637
Cdd:PRK11022 100 TSLNPCYTVG---------FQIMEAIKVHQggnKKTRRQRAIDLlnQVGipdpaSRldvyPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 638 NPPILLLDEPTSAMDNTGEER-------LKQRlqsviENKTVILVTHRASLLSLV-DRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQiiellleLQQK-----ENMALVLITHDLALVAEAaHKIIVMYAGQVVETGKAHDIFRA 244
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
503-700 |
7.23e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RHNIGYVAQDIQLLAG-TLRDNL 578
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGALFTDmNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 579 VSGARY-------VDDEMVLQAAELAGVHEFARLHPqgyelqvgergQNLSGGQRQNVALARALLLNPPILLLDEPTSAM 651
Cdd:PRK11831 106 AYPLREhtqlpapLLHSTVMMKLEAVGLRGAAKLMP-----------SELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 652 DNTGEE---RLKQRLQSVIeNKTVILVTHRA-SLLSLVDRLLVIDRGQILADG 700
Cdd:PRK11831 175 DPITMGvlvKLISELNSAL-GVTCVVVSHDVpEVLSIADHAYIVADKKIVAHG 226
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
291-450 |
7.76e-07 |
|
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: 51.64 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 291 FTLIILVVIAMLG--GHLVWIPIIAFPLALGIGHMLQKpLTATL--ERTMALGaeRQSSLI-ETLAGLDAVKVNNAESER 365
Cdd:cd18547 130 ILTIVGTLIMMLYisPLLTLIVLVTVPLSLLVTKFIAK-RSQKYfrKQQKALG--ELNGYIeEMISGQKVVKAFNREEEA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 366 QYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLT 445
Cdd:cd18547 207 IEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQIN 286
|
....*
gi 814585811 446 RYQQA 450
Cdd:cd18547 287 SLQSA 291
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
277-452 |
1.00e-06 |
|
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: 51.25 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 277 FLTSLTLASLIDLPFTLIILVVIAMLGGHLVWIPIIAFPLAlgigHMLQKPLtatlertmalgaERQSSLI-ETLAGLDA 355
Cdd:cd18548 127 LIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLF----KKVQKKL------------DRLNRVVrENLTGIRV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 356 VKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALG 435
Cdd:cd18548 191 IRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILM 270
|
170
....*....|....*..
gi 814585811 436 PLAQLSGLLTRYQQAKV 452
Cdd:cd18548 271 SLMMLSMVFVMLPRASA 287
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
277-419 |
1.22e-06 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 50.94 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 277 FLTSLTLASLIDLPFTLIILVVIAMLGghlVWIPIIAFPLALGIGHMLQKpltatlertmaLGAERQSSLIETLAGLDAV 356
Cdd:cd18585 123 ILATILFLAFFSPALALILLAGLLLAG---VVIPLLFYRLGKKIGQQLVQ-----------LRAELRTELVDGLQGMAEL 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 357 KVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALS 419
Cdd:cd18585 189 LIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD 251
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
345-454 |
1.50e-06 |
|
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: 50.55 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 345 SLIETLagldavKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLAMNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLV 424
Cdd:cd18569 188 QMIETL------KASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLV 261
|
90 100 110
....*....|....*....|....*....|
gi 814585811 425 ACYMLSGRALGPLAQLSGLLTRYQQAKVTM 454
Cdd:cd18569 262 AFQSLMASFLAPVNSLVGLGGTLQEMRGDM 291
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
171-451 |
1.70e-06 |
|
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: 50.23 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATAT-LWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERI 249
Cdd:cd18778 4 TLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGlLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 250 VGMAMKV---RP-----ARVGSFAQNIHEF--QGMRDFLTSLtlaslidlpftLIILVVIAMLGGH------LVWIPIia 313
Cdd:cd18778 84 QRLSLRYfddRQtgdlmSRVINDVANVERLiaDGIPQGITNV-----------LTLVGVAIILFSInpklalLTLIPI-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 314 fPLALGIGHMLQK---PLTATLERTMAlgaERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELRVKVLSGLA 390
Cdd:cd18778 151 -PFLALGAWLYSKkvrPRYRKVREALG---ELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIF 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 814585811 391 MNITLLIQQVAGVAMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAK 451
Cdd:cd18778 227 HPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRAL 287
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
499-707 |
1.92e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSEL---RHNIGYVAQDIQllaGTLR 575
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDPY---ASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 576 DNLVSGARYVDDEMV---LQ----AAELAGVHEFARLHPQgyelQVGERGQNLSGGQRQNVALARALLLNPPILLLDEPT 648
Cdd:PRK10261 416 PRQTVGDSIMEPLRVhglLPgkaaAARVAWLLERVGLLPE----HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 649 SAMDNTGEERLKQRLQSVIENKTV--ILVTHRASLLSLVD-RLLVIDRGQILADGPKAAVME 707
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
483-696 |
2.10e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTYPNQQNLaLRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLL--------------VDGVDI 548
Cdd:PLN03073 509 ISFSDASFGYPGGPLL-FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDL 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 549 RQIDVSELRHNIGYVAQDiqllagTLRDNLvsGARYVDDEMVLQAAelagvhefarlhpqgyelqvgergQNLSGGQRQN 628
Cdd:PLN03073 588 SSNPLLYMMRCFPGVPEQ------KLRAHL--GSFGVTGNLALQPM------------------------YTLSGGQKSR 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 629 VALARALLLNPPILLLDEPTSAMDNTGEERLKQRLqsVIENKTVILVTHRASLLS-LVDRLLVIDRGQI 696
Cdd:PLN03073 636 VAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
171-451 |
4.71e-06 |
|
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: 49.02 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 171 AIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFERIV 250
Cdd:cd18543 4 ALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 251 GMAM----KVRPARVGSFAqnIHEFQGMRDFLT--SLTLASLIDLPFTLIILVVIAMLGGHLVwipIIAFPLALGIGHML 324
Cdd:cd18543 84 RLDGafhdRWQSGQLLSRA--TSDLSLVQRFLAfgPFLLGNLLTLVVGLVVMLVLSPPLALVA---LASLPPLVLVARRF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 325 QKPLTATLERTMALGAERQSSLIETLAGLDAVKVNNAESERQYQWEQTIGTLSRLELR-VKVLSGLAMNITLLiQQVAGV 403
Cdd:cd18543 159 RRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRaARLRARFWPLLEAL-PELGLA 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 814585811 404 AMIIFGVYQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAK 451
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRAR 285
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
507-677 |
5.32e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSL------------------------LVDGvdirQIDVSelrHNIGY 562
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkrfrgtelqnyfkkLYNG----EIKVV---HKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQDIQLLAGTLRDnLVSGA--RYVDDEmVLQAAELAGVhefarlhpqgyelqVGERGQNLSGGQRQNVALARALLLNPP 640
Cdd:PRK13409 169 VDLIPKVFKGKVRE-LLKKVdeRGKLDE-VVERLGLENI--------------LDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 814585811 641 ILLLDEPTSAMDntgeerLKQRL------QSVIENKTVILVTH 677
Cdd:PRK13409 233 FYFFDEPTSYLD------IRQRLnvarliRELAEGKYVLVVEH 269
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
507-706 |
6.59e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.01 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYqPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDI---------QLLagtlrdn 577
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQtppfampvfQYL------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 lvsgARYVDDEMVLQAAELAgVHEFARLhpqgyeLQVGER----GQNLSGGQRQNVALA-------RALLLNPPILLLDE 646
Cdd:PRK03695 91 ----TLHQPDKTRTEAVASA-LNEVAEA------LGLDDKlgrsVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 814585811 647 PTSAMDNTGEERLKQRLQSVIENKTVILVT--------HRAsllslvDRLLVIDRGQILADGPKAAVM 706
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSshdlnhtlRHA------DRVWLLKQGKLLASGRRDEVL 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
510-591 |
8.80e-06 |
|
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: 46.21 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 510 GEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDVSELRHNIGYVAQDIQLLAGTLRDNLVSGARYVDDEM 589
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
..
gi 814585811 590 VL 591
Cdd:smart00382 82 LI 83
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
495-555 |
1.33e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.09 E-value: 1.33e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 495 QQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGL--YQPDSGSLLVDGVDIRQIDVSE 555
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPED 74
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
507-694 |
1.57e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLL-----VGLYQpdSGSLLVDGvdiRQIDVSELRhNIGYVAQ-DIQLLAGTLRDNLVS 580
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLaervtTGVIT--GGDRLVNG---RPLDSSFQR-SIGYVQQqDLHLPTSTVRESLRF 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 581 GAR---------YVDDEMVLQAAELAGVHEFArlhpqgyELQVGERGQNLSGGQRQNVALA-RALLLNPPILLLDEPTSA 650
Cdd:TIGR00956 860 SAYlrqpksvskSEKMEYVEEVIKLLEMESYA-------DAVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSG 932
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 814585811 651 MDNTGEERLKQRLQSVIENKTVILVT-HRAS--LLSLVDRLLVIDRG 694
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTiHQPSaiLFEEFDRLLLLQKG 979
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
488-695 |
1.64e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 488 VDFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLA-KLLVGLYQPD----SGSLLVDGVDIRQIDVSELRHnigy 562
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRG---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 vaqdiqllagtLRDNLVsgARYVDDEMVL---------QAAELAGVHEFARLHPQGYEL-----QVGERG---------Q 619
Cdd:PRK15134 89 -----------VRGNKI--AMIFQEPMVSlnplhtlekQLYEVLSLHRGMRREAARGEIlncldRVGIRQaakrltdypH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 620 NLSGGQRQNVALARALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIE--NKTVILVTHRASLL-SLVDRLLVIDRGQ 695
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGR 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
515-633 |
1.81e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 515 IIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQIDvselRHNIGYVAQDIQL-LAGTLRDNLVSGARYVDDEMVLQA 593
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIGHNLGLkLEMTVFENLKFWSEIYNSAETLYA 106
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 814585811 594 AelagVHEFaRLHPqgyelQVGERGQNLSGGQRQNVALAR 633
Cdd:PRK13541 107 A----IHYF-KLHD-----LLDEKCYSLSSGMQKIVAIAR 136
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
513-652 |
2.16e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.81 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 513 IGIIGRSGSGKSSLAKLLVGLYQPDSGSLLV-DGVDirqidvselrhnIGYVAQDiqllagtlRDNL---------VSGA 582
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVK------------LAYVDQS--------RDALdpnktvweeISGG 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 814585811 583 ryvDDEMVLQAAELAGVHEFARLHPQGYELQ--VGergqNLSGGQRQNVALARALLLNPPILLLDEPTSAMD 652
Cdd:PRK11819 413 ---LDIIKVGNREIPSRAYVGRFNFKGGDQQkkVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
169-451 |
2.29e-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: 47.18 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 169 ADAIAASLVINLIALAAPLFVMNVYDRVVPNQATATLWMLAIGICGAYLFDLLLKSLRSLCLDLAGKKTDLIISATLFER 248
Cdd:cd18565 17 APPLLIGVAIDAVFNGEASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 249 IVGMAMkvrparvGSFAQN------------IHEfqgMRDFLTSlTLASLIDLPFTLI-ILVVIAMLGGHLVWIPIIAFP 315
Cdd:cd18565 97 VQRLDM-------AFFEDRqtgdlmsvlnndVNQ---LERFLDD-GANSIIRVVVTVLgIGAILFYLNWQLALVALLPVP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 316 LALGIGHMLQKPL----TATLERTMALgaerqSSLIET-LAGLDAVKVNNAE----------SE--RQYQWEqTIGTLSR 378
Cdd:cd18565 166 LIIAGTYWFQRRIepryRAVREAVGDL-----NARLENnLSGIAVIKAFTAEdferervadaSEeyRDANWR-AIRLRAA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 379 LELRVKVLSGLAMNITLLIqqvaGVAMIIFGVyQIIDGALSMGGLVACYMLSGRALGPLAQLSGLLTRYQQAK 451
Cdd:cd18565 240 FFPVIRLVAGAGFVATFVV----GGYWVLDGP-PLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAM 307
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
499-708 |
2.34e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 47.21 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLyQPDSGSLLVD-----GVDIRQIDVSELRHNIGyvaQDIQLL--- 570
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLSPRERRKIIG---REIAMIfqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 571 -------AGTLRDNLvsgaryvddEMVLQAAELAGV--HEFARLHPQGYEL--QVGERGQN---------LSGGQRQNVA 630
Cdd:COG4170 98 psscldpSAKIGDQL---------IEAIPSWTFKGKwwQRFKWRKKRAIELlhRVGIKDHKdimnsypheLTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 631 LARALLLNPPILLLDEPTSAMDNTGEE---RLKQRLqSVIENKTVILVTHR-ASLLSLVDRLLVIDRGQILADGPKAAVM 706
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQAqifRLLARL-NQLQGTSILLISHDlESISQWADTITVLYCGQTVESGPTEQIL 247
|
..
gi 814585811 707 EA 708
Cdd:COG4170 248 KS 249
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
20-133 |
2.59e-05 |
|
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The cysteine peptidases in family C39 cleave the "double-glycine" leader peptides from the precursors of various bacteriocins (mostly non-lantibiotic). The cleavage is mediated by the transporter as part of the secretion process. Bacteriocins are antibiotic proteins secreted by some species of bacteria that inhibit the growth of other bacterial species. The bacteriocin is synthesized as a precursor with an N-terminal leader peptide, and processing involves removal of the leader peptide by cleavage at a Gly-Gly bond, followed by translocation of the mature bacteriocin across the cytoplasmic membrane. Most endopeptidases of family C39 are N-terminal domains in larger proteins (ABC transporters) that serve both functions. The proposed protease active site is not conserved in this sub-family.
Pssm-ID: 239098 [Multi-domain] Cd Length: 121 Bit Score: 44.16 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 20 DPLLDGLLTLCSLHYKPASRAMLTTGLPLAAQRLSAELLPRAAARAGLQGRLLQRKLEQIPSIALPAMLLLKEGRSAVLL 99
Cdd:cd02417 6 DSGLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPLPALAWDDDGGHFILA 85
|
90 100 110
....*....|....*....|....*....|....
gi 814585811 100 GWEGDTARLLLSESDGGEVqVSRETLSQDYSGRV 133
Cdd:cd02417 86 KLDGQKYLIQDPISQRPEV-LSREEFEARWSGEL 118
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
507-682 |
3.81e-05 |
|
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: 45.82 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLlVDGVDIRQIdvseLRHNIGYVAQDI--QLLAGTLRdnLVSGARY 584
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKF-DDPPDWDEI----LDEFRGSELQNYftKLLEGDVK--VIVKPQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 585 VD------DEMVLQAAELAGVHEFARLHPQGYEL-QVGERG-QNLSGGQRQNVALARALLLNPPILLLDEPTSAMDntge 656
Cdd:cd03236 96 VDlipkavKGKVGELLKKKDERGKLDELVDQLELrHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD---- 171
|
170 180 190
....*....|....*....|....*....|...
gi 814585811 657 erLKQRLQSVI-------ENKTVILVTHRASLL 682
Cdd:cd03236 172 --IKQRLNAARlirelaeDDNYVLVVEHDLAVL 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
452-696 |
4.29e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.70 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 452 VTMVSVDQMMELPQERNYDERPLSRKALQGAMTfREVDFTYPN---QQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAK 528
Cdd:PRK09700 229 VSDVSNDDIVRLMVGRELQNRFNAMKENVSNLA-HETVFEVRNvtsRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 529 LLVGLYQPDSGSLLVDGVDIR---QID--------VSELRHNIGY-----VAQDIQLlAGTLRDNLVSGAR-YVDDEMVL 591
Cdd:PRK09700 308 CLFGVDKRAGGEIRLNGKDISprsPLDavkkgmayITESRRDNGFfpnfsIAQNMAI-SRSLKDGGYKGAMgLFHEVDEQ 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 592 QAAELAgvHEFARLHPQGYELQVGErgqnLSGGQRQNVALARALLLNPPILLLDEPTSAMD-NTGEERLKQRLQSVIENK 670
Cdd:PRK09700 387 RTAENQ--RELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDvGAKAEIYKVMRQLADDGK 460
|
250 260
....*....|....*....|....*..
gi 814585811 671 TVILVTHR-ASLLSLVDRLLVIDRGQI 696
Cdd:PRK09700 461 VILMVSSElPEIITVCDRIAVFCEGRL 487
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
499-700 |
4.37e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAkLLVGLYQPDSGSLLVDgVDIRQIDVSELRHNIGY--VAQDIQLLAGTLRD 576
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWR-F*TWCANRRALRRTIG*hrPVR*GRRESFSGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 577 NLVSGARYVD---DEMVLQAAELagVHEFARLHPqgyelqVGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMDN 653
Cdd:NF000106 106 NLYMIGR*LDlsrKDARARADEL--LERFSLTEA------AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 814585811 654 TGEERLKQRLQSVIENKTVILVT--HRASLLSLVDRLLVIDRGQILADG 700
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTtqYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
463-652 |
5.61e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 463 LPQERNYDERPLS---RKALQGA--------MTFREVDFTypnqqnlALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLV 531
Cdd:NF033858 241 LPEEKRRGHQPVVippRPADDDDepaieargLTMRFGDFT-------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 532 GLYQPDSGSLLVDG--VDIRQIDVselRHNIGYVAQDIQL---LagTLRDNLVSGARYVDdemvLQAAELAG-VHEFArl 605
Cdd:NF033858 314 GLLPASEGEAWLFGqpVDAGDIAT---RRRVGYMSQAFSLygeL--TVRQNLELHARLFH----LPAAEIAArVAEML-- 382
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 814585811 606 hpQGYELQ--VGERGQNLSGGQRQNVALARALLLNPPILLLDEPTSAMD 652
Cdd:NF033858 383 --ERFDLAdvADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
499-545 |
6.52e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 6.52e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDG 545
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
500-677 |
9.63e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 9.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVdGVDIrqidvselrhNIGYVAQDIQLL--AGTLRDN 577
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL----------EVAYFDQHRAELdpEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 578 LVSGAryvddemvlQAAELAGV--HEFARL-----HPQGYELQVgergQNLSGGQRQNVALARALLLNPPILLLDEPTSA 650
Cdd:PRK11147 404 LAEGK---------QEVMVNGRprHVLGYLqdflfHPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTND 470
|
170 180
....*....|....*....|....*....
gi 814585811 651 MDntgEERLkQRLQSVIEN--KTVILVTH 677
Cdd:PRK11147 471 LD---VETL-ELLEELLDSyqGTVLLVSH 495
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
507-696 |
1.21e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqidvselRHNIGYVAQDIQLLAGTLRDNLVSGAR-YV 585
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQETPALPQPALEYVIDGDReYR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 586 DDEMVLQAA-ELAGVHEFARLHPQGYELQ---VGERGQNL------------------SGGQRQNVALARALLLNPPILL 643
Cdd:PRK10636 93 QLEAQLHDAnERNDGHAIATIHGKLDAIDawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 814585811 644 LDEPTSAMDNTGEERLKQRLQSVieNKTVILVTH-RASLLSLVDRLLVIDRGQI 696
Cdd:PRK10636 173 LDEPTNHLDLDAVIWLEKWLKSY--QGTLILISHdRDFLDPIVDKIIHIEQQSL 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
483-694 |
1.37e-04 |
|
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: 43.39 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 483 MTFREVDFTY--PNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLL-----VGLYqpdSGSLLVDGvdiRQIDVSe 555
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILING---RPLDKN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 556 LRHNIGYVAQ-DIQLLAGTLRDNLvsgaryvddemvlqaaelagvhEF-ARLhpqgyelqvgeRGqnLSGGQRQNVALAR 633
Cdd:cd03232 77 FQRSTGYVEQqDVHSPNLTVREAL----------------------RFsALL-----------RG--LSVEQRKRLTIGV 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 814585811 634 ALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENKTVILVT-HR--ASLLSLVDRLLVIDRG 694
Cdd:cd03232 122 ELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
486-677 |
3.52e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 486 REVDFTYPNQQN---LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGvdirqiDVSELRHNIGY 562
Cdd:PRK13546 23 RMKDALIPKHKNktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 563 VAQdiqllagtlrdnlVSGARYVDDEMVLQAAELagvHEFARLHPQGYEL-QVGE----RGQNLSGGQRQNVALARALLL 637
Cdd:PRK13546 97 SGQ-------------LTGIENIEFKMLCMGFKR---KEIKAMTPKIIEFsELGEfiyqPVKKYSSGMRAKLGFSINITV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 814585811 638 NPPILLLDEPTSAMDNTGEERLKQRLQSVIE-NKTVILVTH 677
Cdd:PRK13546 161 NPDILVIDEALSVGDQTFAQKCLDKIYEFKEqNKTIFFVSH 201
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
508-677 |
4.04e-04 |
|
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: 43.62 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 508 RAGEKIGIIGRSGSGKSSLAKLLVGLYQPD-----------------SGSLLVD---GVDIRQIDVSelrHNIGYVAQDI 567
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNlgdydeepswdevlkrfRGTELQDyfkKLANGEIKVA---HKPQYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 568 QLLAGTLRDNLvsgaRYVDDEMVLqaAELAGvhefaRLhpqgyELQ-VGERG-QNLSGGQRQNVALARALLLNPPILLLD 645
Cdd:COG1245 174 KVFKGTVRELL----EKVDERGKL--DELAE-----KL-----GLEnILDRDiSELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*....
gi 814585811 646 EPTSAMDntgeerLKQRLQ--SVI-----ENKTVILVTH 677
Cdd:COG1245 238 EPSSYLD------IYQRLNvaRLIrelaeEGKYVLVVEH 270
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
503-708 |
4.68e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.87 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 503 INLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPD----SGSLLVDGVDIRQIDVSELR----HNIGYVAQDIQllagTL 574
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRERRklvgHNVSMIFQEPQ----SC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGARYVDDEMVLQAAELAGVHEFARLHPQGYEL--QVGERGQN---------LSGGQRQNVALARALLLNPPILL 643
Cdd:PRK15093 102 LDPSERVGRQLMQNIPGWTYKGRWWQRFGWRKRRAIELlhRVGIKDHKdamrsfpyeLTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 644 LDEPTSAMDNTGEE---RLKQRLQSViENKTVILVTHRASLLS-LVDRLLVIDRGQILADGPKAAVMEA 708
Cdd:PRK15093 182 ADEPTNAMEPTTQAqifRLLTRLNQN-NNTTILLISHDLQMLSqWADKINVLYCGQTVETAPSKELVTT 249
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
489-676 |
5.26e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 489 DFTYPNQQNLALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQID----VSELRHnIGYVA 564
Cdd:PRK13543 16 ALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrsrfMAYLGH-LPGLK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 565 QDIQLLAGTLRDNLVSGARyvDDEMVLQAAELAGVhefarlhpQGYELQVgerGQNLSGGQRQNVALARALLLNPPILLL 644
Cdd:PRK13543 95 ADLSTLENLHFLCGLHGRR--AKQMPGSALAIVGL--------AGYEDTL---VRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190
....*....|....*....|....*....|..
gi 814585811 645 DEPTSAMDNTGEERLKQRLQSVIENKTVILVT 676
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISAHLRGGGAALVT 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
499-700 |
7.33e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 7.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDS--GSLLVDGV-----DIRQidvSElRHNIGYVAQDIQLLA 571
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD---SE-ALGIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 572 G-TLRDNLVSG---ARY--VD-DEMVLQAAEL---AGVHEfarlHPQgyelqvgERGQNLSGGQRQNVALARALLLNPPI 641
Cdd:NF040905 92 YlSIAENIFLGnerAKRgvIDwNETNRRARELlakVGLDE----SPD-------TLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 814585811 642 LLLDEPTSAMDNTGEERLkqrLQSVIENK----TVILVTHRaslLSLVDRllVIDRGQILADG 700
Cdd:NF040905 161 LILDEPTAALNEEDSAAL---LDLLLELKaqgiTSIIISHK---LNEIRR--VADSITVLRDG 215
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
498-550 |
8.52e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 8.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 814585811 498 LALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQ 550
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD 67
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
500-701 |
1.17e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 500 LRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVG-LYQ---PDSGSLLVDGVDIRQIdVSELRHNIGYVAQ-DIQLLAGTL 574
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGfhiGVEGVITYDGITPEEI-KKHYRGDVVYNAEtDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 575 RDNLVSGAR---------------YVDDEMVLQAAELAGVHEfarlhpqgYELQVGE---RGqnLSGGQRQNVALARALL 636
Cdd:TIGR00956 156 GETLDFAARcktpqnrpdgvsreeYAKHIADVYMATYGLSHT--------RNTKVGNdfvRG--VSGGERKRVSIAEASL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 814585811 637 LNPPILLLDEPTSAMDN-TGEERLKQ-RLQSVIENKTVILVTHRAS--LLSLVDRLLVIDRGQILADGP 701
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSaTALEFIRAlKTSANILDTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGP 294
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
499-696 |
2.17e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 499 ALRGINLNVRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVDIRQID-----------VSELRHNIG-YVAQD 566
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGiYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 567 IQ---LLA---------GTLRDN-LVSGARYVDDEMvlqaaelagvhefaRLHPQGYELQVGergqNLSGGQRQNVALAR 633
Cdd:PRK10982 343 IGfnsLISnirnyknkvGLLDNSrMKSDTQWVIDSM--------------RVKTPGHRTQIG----SLSGGNQQKVIIGR 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 814585811 634 ALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVI-ENKTVILVTHR-ASLLSLVDRLLVIDRGQI 696
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEmPELLGITDRILVMSNGLV 469
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
609-695 |
6.08e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.46 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 609 GYeLQVGERGQNLSGGQRQNVALAR--ALLLNPPILLLDEPTSAMDNTGEERLKQRLQSVIENK-TVILVTHRASLLSLV 685
Cdd:cd03238 77 GY-LTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGnTVILIEHNLDVLSSA 155
|
90
....*....|
gi 814585811 686 DRLLVIDRGQ 695
Cdd:cd03238 156 DWIIDFGPGS 165
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
507-692 |
7.79e-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: 37.94 E-value: 7.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 507 VRAGEKIGIIGRSGSGKSSLAKLLVGLYQPDSGSLLVDGVdirqidvselrhNIGYVAQdiqllagtlrdnlvsgarYVD 586
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI------------TPVYKPQ------------------YID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 814585811 587 demvlqaaelagvhefarlhpqgyelqvgergqnLSGGQRQNVALARALLLNPPILLLDEPTSAMDNtgEERLK--QRLQ 664
Cdd:cd03222 72 ----------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNaaRAIR 115
|
170 180 190
....*....|....*....|....*....|.
gi 814585811 665 SVIEN--KTVILVTHRASLLS-LVDRLLVID 692
Cdd:cd03222 116 RLSEEgkKTALVVEHDLAVLDyLSDRIHVFE 146
|
|
| |
