|
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 ... |
25-717 |
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: 960.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 25 LLDSLVLLTEYFGSPCSSESLAAGLPLSSAVLSPELVPQAAARAGLTAKLSRKGLNQVTAIQLPCILLLKDKKACILREL 104
Cdd:TIGR03375 1 LLDCLLLLARHYGRPVSREALVAGLPLEDGRLTPELLPRAARRAGLSARLVKRSLDDISPLLLPAILLLKDGRACVLLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 105 DLEQQYAVIqLPETG-GEQRLSIEELETLYVGYLFLVKQQYRGDMGFDVYHHDHSKHWLLQTIKDSAPIYRDALIASILV 183
Cdd:TIGR03375 81 DEDGKARVL-LPETGdGEQELSLDALEALYSGYAIFVRPQFRFDARADELISPRPKHWFWSTLKESWPLYRDVLIASLLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 184 NLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAIGIPLENRS 263
Cdd:TIGR03375 160 NLLALASPLFVMNVYDRVVPNQAFETLWVLAIGVALAIVFDFVLKTLRSYFLDVAGKKADLILSAKLFERVLGLRMEARP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 264 ASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPRLKTAIEESNKF 343
Cdd:TIGR03375 240 ASVGSFANQLREFESVRDFFTSATLTALIDLPFALLFLLVIAIIGGPLVWVPLVAIPLILLPGLLLQRPLSRLAEESMRE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 344 ASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVILGVYRVADNDI 423
Cdd:TIGR03375 320 SAQRNAVLVESLSGLETIKALNAEGRFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISDGEL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 424 SMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQRLMGKIEADDLSFSYPGSEKP 503
Cdd:TIGR03375 400 TMGGLIACVMLSGRALAPLGQLAGLLTRYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQGEIEFRNVSFAYPGQETP 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 504 VLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNI 583
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNI 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 LFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQ 663
Cdd:TIGR03375 560 ALGAPYADDEEILRAAELAGVTEFVRRHPDGLDMQIGERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEER 639
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 664 FMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEKLNQG 717
Cdd:TIGR03375 640 FKDRLKRWLAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLEALRKG 693
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
18-713 |
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: 696.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 18 QRVTVDPLLDSLVLLTEYFGSPCSSESLAAGLPLSSAVLSPELVPQAAARAGLTAKLSRKGLNQVTAIQLPCILLLKDKK 97
Cdd:COG2274 9 QMEAADCGLACLAMIARYYGRPVSLEELREALGVSRDGLSLLGLLRAARRLGLRARGVRLDLEELAELPLPAILHWDGNH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 98 ACILRELDLEQqyAVIQLPETGgEQRLSIEELETLYVGYLFLVKQQYRGDMGFDvyhHDHSKHWLLQTIKDSAPIYRDAL 177
Cdd:COG2274 89 FVVLEGVDGDK--VTIADPATG-RRKLSLEEFAESWTGVALLLEPTPEFDKRGE---KPFGLRWFLRLLRRYRRLLLQVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 178 IASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAIGI 257
Cdd:COG2274 163 LASLLINLLALATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 258 PLENR-SASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPRLKTA 336
Cdd:COG2274 243 PLSFFeSRSVGDLASRFRDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 337 IEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVILGVY 416
Cdd:COG2274 323 SREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAY 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 417 RVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQRLMGKIEADDLSFS 496
Cdd:COG2274 403 LVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 497 YPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFH 576
Cdd:COG2274 483 YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFS 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 577 GSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASL 656
Cdd:COG2274 563 GTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 657 DARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:COG2274 643 DAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR 699
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
171-462 |
1.10e-151 |
|
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: 442.26 E-value: 1.10e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 171 PIYRDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRL 250
Cdd:cd18587 2 RIYRDVLLAALLINLFALASPLFVMNVYDRVVPNNAIETLWVLAIGVLIALLFDFILKLLRAYFIDVAGKRADVILSSRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 251 FYKAIGIPLENRSASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQ 330
Cdd:cd18587 82 FERVLGLRLEARPASVGSFANNLREFESVRDFFTSATLTALIDLPFVLLFLAVIALIGGPLALVPLVAIPLVLLYGLLLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 331 PRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSV 410
Cdd:cd18587 162 KPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAI 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 411 VILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQL 462
Cdd:cd18587 242 VIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
176-713 |
2.11e-120 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 372.58 E-value: 2.11e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:COG1132 26 ALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL----ENRSASVggMARQLGEFDSIREILTSaTITTLVDLPFALLFVLIIyLVAGD--LALIPLVASLIIIGYTLIV 329
Cdd:COG1132 106 RLPLsffdRRRTGDL--LSRLTNDVDAVEQFLAH-GLPQLVRSVVTLIGALVV-LFVIDwrLALIVLLVLPLLLLVLRLF 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 330 QPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVS 409
Cdd:COG1132 182 GRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLAL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 410 VVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQRLMGKIE 489
Cdd:COG1132 262 VLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 490 ADDLSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLP 569
Cdd:COG1132 342 FENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 QDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLM 649
Cdd:COG1132 421 QDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 650 DEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:COG1132 501 DEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
162-716 |
4.91e-116 |
|
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: 360.60 E-value: 4.91e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 162 LLQTIKDSAPIYRDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKK 241
Cdd:COG4618 11 LRAALRACRRAFLSVGLFSFFINLLMLTPPLYMLQVYDRVLTSRSVDTLLMLTLLALGLYAVMGLLDAVRSRILVRVGAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 242 VDIIVSSRLFYKAIGIPLENRSASVggmARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLI 321
Cdd:COG4618 91 LDRRLGPRVFDAAFRAALRGGGGAA---AQALRDLDTLRQFLTGPGLFALFDLPWAPIFLAVLFLFHPLLGLLALVGALV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 322 IIGYTLIVQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANF 401
Cdd:COG4618 168 LVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 402 VVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLvsk 481
Cdd:COG4618 248 LRLLLQSAVLGLGAYLVIQGEITPGAMIAASILMGRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPL--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 482 QRLMGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL 561
Cdd:COG4618 325 PRPKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 RRNFGYLPQDVTLFHGSVRDNI-LFGtrQVTEHQLIRAVQLSGVN-LFTDLEsEGLDQQVGEGGHSLSRGQRQTVALARA 639
Cdd:COG4618 405 GRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHeMILRLP-DGYDTRIGEGGARLSGGQRQRIGLARA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNV-SRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEKLNQ 716
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLARLAR 559
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
486-705 |
9.29e-105 |
|
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: 318.76 E-value: 9.29e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPP 645
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADG 705
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 ... |
178-714 |
1.16e-95 |
|
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: 306.97 E-value: 1.16e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 178 IASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAIGI 257
Cdd:TIGR01842 13 LFSFVINILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFAASFSA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 258 PLENRSasvGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPRLKTAI 337
Cdd:TIGR01842 93 TLRRGS---GDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAVVLVGLALLNNRATKKPL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 338 EESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVILGVYR 417
Cdd:TIGR01842 170 KEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 418 VADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMtqeDEFENKGHLVSKQRLMGKIEADDLSFSY 497
Cdd:TIGR01842 250 AIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELL---ANYPSRDPAMPLPEPEGHLSVENVTIVP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 498 PGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHG 577
Cdd:TIGR01842 327 PGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 578 SVRDNILFGTRQVTEHQLIRAVQLSGVN-LFTDLEsEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASL 656
Cdd:TIGR01842 407 TVAENIARFGENADPEKIIEAAKLAGVHeLILRLP-DGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 657 DARAEKQFMRSMHNV-SRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEKL 714
Cdd:TIGR01842 486 DEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAKL 544
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
282-706 |
6.57e-89 |
|
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: 289.74 E-value: 6.57e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 282 ILTSATITTLVDLPFALLfVLIIYLVAGdlALIPLVASLIiigytlivqpRLKTAIEESNKFASLkHGHLIESLASLESI 361
Cdd:COG4987 143 ILAAVAFLAFFSPALALV-LALGLLLAG--LLLPLLAARL----------GRRAGRRLAAARAAL-RARLTDLLQGAAEL 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 362 KSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVILGVYRVADNDISmGGIIAAVMLASRAVA- 440
Cdd:COG4987 209 AAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFe 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 441 PMAQLANLMTRANQTASALRQLDQIMTQEDE--FENKGHLVSKQrlmGKIEADDLSFSYPGSEKPVLHPFALRIRPGERI 518
Cdd:COG4987 288 ALAPLPAAAQHLGRVRAAARRLNELLDAPPAvtEPAEPAPAPGG---PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERV 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 519 AIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRA 598
Cdd:COG4987 365 AIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAA 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 599 VQLsgVNLFTDLES--EGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRT 676
Cdd:COG4987 445 LER--VGLGDWLAAlpDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT 522
|
410 420 430
....*....|....*....|....*....|
gi 1310934957 677 LLIITHKMHLLNLVDRIIVMDRGHIIADGP 706
Cdd:COG4987 523 VLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
159-713 |
1.01e-87 |
|
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: 286.27 E-value: 1.01e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 159 KHWLLQTIKDSAPIYRDALIASILVNLFALVSPLFIMNVYDKVV-PNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDV 237
Cdd:COG4988 5 DKRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 238 AGKKVDIIVSSRLFYKAIGI-PLENRSASVGGMARQLGE----FDS-IREILTSATITTLVdlPFALL-FVLIIYLVAGd 310
Cdd:COG4988 85 AAARVKRRLRRRLLEKLLALgPAWLRGKSTGELATLLTEgveaLDGyFARYLPQLFLAALV--PLLILvAVFPLDWLSG- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 311 laLIPLV-ASLIIIGYTLIvqpRLKTAIEESNKFASLKH--GHLIESLASLESIKSYGAEglvqKAWQQMIGHTANwQLR 387
Cdd:COG4988 162 --LILLVtAPLIPLFMILV---GKGAAKASRRQWRALARlsGHFLDRLRGLTTLKLFGRA----KAEAERIAEASE-DFR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 388 SKK--------LSN---------SVANVAnfvvqltvvsvvILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLM- 449
Cdd:COG4988 232 KRTmkvlrvafLSSavleffaslSIALVA------------VYIGFRLLGGSLTLFAALFVLLLAPEFFLPLRDLGSFYh 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 450 TRANQTAsALRQLDQIMTQEDEFENKGHLVSKQRLMGKIEADDLSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKS 529
Cdd:COG4988 300 ARANGIA-AAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPG-GRPALDGLSLTIPPGERVALVGPSGAGKS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 530 TLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTD 609
Cdd:COG4988 378 TLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 610 LESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNL 689
Cdd:COG4988 458 ALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQ 537
|
570 580
....*....|....*....|....
gi 1310934957 690 VDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
63-713 |
1.31e-75 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 257.95 E-value: 1.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 63 QAAARAGLTAKLSRKGLNQVTAIQLPCILLLKDKKACILRelDLEQQYAVIQLPETGgEQRLSIEELETLYVGYLfLVKQ 142
Cdd:TIGR03796 52 KAARSYGLEAKGFRKELDALAELPLPYIVFWNFNHFVVVE--GFRGGRVYLNDPALG-PRTVSLEEFDESFTGVV-LTFE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 143 -----QYRGdmgfdvyhhdhSKHWLLQTIKDSAPIYRDALIASILVNLFALVSPLFIMN---VY-DKVVPNLAFESLWVL 213
Cdd:TIGR03796 128 pgpefQKGG-----------RKPSLLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAfsqIFvDEILVQGRQDWLRPL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 214 AIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAIGIPLE---NRSAsvGGMARQLGEFDSIREILTSATITT 290
Cdd:TIGR03796 197 LLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRffaQRHA--GDIASRVQLNDQVAEFLSGQLATT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 291 LVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLV 370
Cdd:TIGR03796 275 ALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDF 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 371 QKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMT 450
Cdd:TIGR03796 355 FSRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 451 RANQTASALRQLDQIMTQ------EDEFENKGHLVSKQRLMGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRN 524
Cdd:TIGR03796 435 TLQELEGDLNRLDDVLRNpvdpllEEPEGSAATSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGS 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 525 GSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGV 604
Cdd:TIGR03796 515 GSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAI 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 605 NLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMhnvsRDR--TLLIITH 682
Cdd:TIGR03796 595 HDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL----RRRgcTCIIVAH 670
|
650 660 670
....*....|....*....|....*....|.
gi 1310934957 683 KMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:TIGR03796 671 RLSTIRDCDEIIVLERGKVVQRGTHEELWAV 701
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
170-462 |
1.84e-73 |
|
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: 239.79 E-value: 1.84e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 170 APIYRDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSR 249
Cdd:cd18566 1 RPLLPQVLLASLFINILALATPLFILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 250 LFYKAIGIPL-ENRSASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLI 328
Cdd:cd18566 81 AFEHLLSLPLsFFEREPSGAHLERLNSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 329 VQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVV 408
Cdd:cd18566 161 LGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 409 SVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQL 462
Cdd:cd18566 241 AVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
488-700 |
2.15e-70 |
|
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: 227.27 E-value: 2.15e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNIlfgtrqvtehqliravqLSGvnlftdlesegldqqvgegghslsrGQRQTVALARAILNDPPVL 647
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------LSG-------------------------GQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGH 700
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
488-713 |
2.47e-65 |
|
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: 216.33 E-value: 2.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVL 647
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
486-713 |
5.38e-65 |
|
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: 215.17 E-value: 5.38e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYpGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPP 645
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
232-721 |
1.95e-63 |
|
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: 221.51 E-value: 1.95e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 232 SYLIDVAGKKVDIIVSSRLFYKAIGIPleNRSASVGGMARQLGEFDSIREILTSAT---ITTLVDLPFALLFVLIIYL-V 307
Cdd:TIGR02203 75 TYLLSWVSNKVVRDIRVRMFEKLLGLP--VSFFDRQPTGTLLSRITFDSEQVASAAtdaFIVLVRETLTVIGLFIVLLyY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 308 AGDLALIPLVASLIIIGYTLIVQPRLKTAIEES-NKFASLKHGhLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQL 386
Cdd:TIGR02203 153 SWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIqNSMGQVTTV-AEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 387 RSKKLSNSVANVANFVVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIM 466
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 467 TQEDEfENKGHLVsKQRLMGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSL 546
Cdd:TIGR02203 312 DSPPE-KDTGTRA-IERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 547 RYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFG-TRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHS 625
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 626 LSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADG 705
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
490
....*....|....*.
gi 1310934957 706 PKDKVLEKlnQGLMAG 721
Cdd:TIGR02203 550 THNELLAR--NGLYAQ 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
488-713 |
4.09e-62 |
|
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: 207.72 E-value: 4.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVL 647
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
488-713 |
1.40e-61 |
|
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: 206.03 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVT--LFHGSVRDNILFGTRQ--VTEHQLIRAVQ--LSGVNLfTDLesegLDQQVgeggHSLSRGQRQTVALARAIL 641
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGPENlgLPREEIRERVEeaLELVGL-EHL----ADRPP----HELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 642 NDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLL-NLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
486-706 |
5.74e-61 |
|
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: 203.88 E-value: 5.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNI-LFGtrQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDP 644
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLdPFG--EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGP 706
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
488-713 |
6.26e-60 |
|
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: 201.69 E-value: 6.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:cd03253 1 IEFENVTFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVL 647
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
488-696 |
7.49e-59 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 207.91 E-value: 7.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEkPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVL 647
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVM 696
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
454-713 |
9.14e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 208.91 E-value: 9.14e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 454 QTASALRQLDQIMTQEDE--FENKGHLVSKQrlmGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTL 531
Cdd:PRK11160 306 QVIASARRINEITEQKPEvtFPTTSTAAADQ---VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 532 AKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAvqLSGVNLFTDLE 611
Cdd:PRK11160 383 LQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEV--LQQVGLEKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 612 S-EGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLV 690
Cdd:PRK11160 461 DdKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF 540
|
250 260
....*....|....*....|...
gi 1310934957 691 DRIIVMDRGHIIADGPKDKVLEK 713
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
488-705 |
2.33e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 202.38 E-value: 2.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLS-FSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGlFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:PRK11174 350 IEAEDLEiLSPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPV 646
Cdd:PRK11174 427 WVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 647 LLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADG 705
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
412-713 |
1.52e-55 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 200.19 E-value: 1.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 412 ILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQRLMGKIEAD 491
Cdd:PRK13657 259 VLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 492 DLSFSYPGSeKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQD 571
Cdd:PRK13657 339 DVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 VTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDE 651
Cdd:PRK13657 418 AGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 652 PTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
488-713 |
3.70e-55 |
|
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: 188.90 E-value: 3.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPG-SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:cd03249 1 IEFKNVSFRYPSrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPV 646
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 647 LLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
298-720 |
1.09e-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: 195.42 E-value: 1.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 298 LLFVLIIYLVAGDL--ALIPLVASLIIIGYTLIVQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQ 375
Cdd:COG5265 166 IALVAGILLVKYDWwfALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYD 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 376 QMIGHTANWQLRSKkLSNSVANVA-NFVVQLTVVSVVILGVYRVADNDISMGGI--IAAVML-----------ASR---- 437
Cdd:COG5265 246 EALARYERAAVKSQ-TSLALLNFGqALIIALGLTAMMLMAAQGVVAGTMTVGDFvlVNAYLIqlyiplnflgfVYReirq 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 438 AVAPMAQLANLMTRANQTASAlrqldqimtqedefENKGHLVSKQrlmGKIEADDLSFSYpGSEKPVLHPFALRIRPGER 517
Cdd:COG5265 325 ALADMERMFDLLDQPPEVADA--------------PDAPPLVVGG---GEVRFENVSFGY-DPERPILKGVSFEVPAGKT 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 518 IAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIR 597
Cdd:COG5265 387 VAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEA 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 598 AVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTL 677
Cdd:COG5265 467 AARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTT 546
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1310934957 678 LIITHKmhlLNLV---DRIIVMDRGHIIADGPKDKVLEKlnQGLMA 720
Cdd:COG5265 547 LVIAHR---LSTIvdaDEILVLEAGRIVERGTHAELLAQ--GGLYA 587
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
489-700 |
2.94e-53 |
|
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: 182.67 E-value: 2.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYL 568
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 569 PQ--DVTLFHGSVRDNILFG--TRQVTEHQLIRAVQ--LSGVNLftdleSEGLDQQVgeggHSLSRGQRQTVALARAILN 642
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEeaLELVGL-----EGLRDRSP----FTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 643 DPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLL-NLVDRIIVMDRGH 700
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEgKTIIIVTHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
174-462 |
3.61e-52 |
|
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: 182.70 E-value: 3.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 174 RDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYK 253
Cdd:cd18588 5 GEVLLASLFLQLFALVTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 254 AIGIPL---ENRSasVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQ 330
Cdd:cd18588 85 LLRLPLsyfESRQ--VGDTVARVRELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 331 PRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSV 410
Cdd:cd18588 163 PILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 411 VILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQL 462
Cdd:cd18588 243 LWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
171-445 |
1.33e-51 |
|
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: 181.26 E-value: 1.33e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 171 PIYRDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRL 250
Cdd:cd18586 2 RVFVEVGLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 251 FYKAIGIPLENRSASVGGMA-RQLgefDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIV 329
Cdd:cd18586 82 FRAVLELPLESRPSGYWQQLlRDL---DTLRNFLTGPSLFAFFDLPWAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 330 QPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVS 409
Cdd:cd18586 159 HRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSL 238
|
250 260 270
....*....|....*....|....*....|....*.
gi 1310934957 410 VVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQL 445
Cdd:cd18586 239 ILGVGAYLVIDGELTIGALIAASILSGRALAPIDQL 274
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
332-713 |
5.26e-51 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 189.55 E-value: 5.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 332 RLKTAIEESNKFAslkhghlIESLASLESIKSYGAEGLVQKAWQQMIGHTAnwQLRSKKLSNSVANVANFVVQLTVVSVV 411
Cdd:TIGR00958 331 ELQEAVAKANQVA-------EEALSGMRTVRSFAAEEGEASRFKEALEETL--QLNKRKALAYAGYLWTTSVLGMLIQVL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 412 IL--GVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKqRLMGKIE 489
Cdd:TIGR00958 402 VLyyGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPL-NLEGLIE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 490 ADDLSFSYPG-SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYL 568
Cdd:TIGR00958 481 FQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALV 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 569 PQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLL 648
Cdd:TIGR00958 561 GQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLI 640
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 649 MDEPTASLDARAEKQFMRSMHnvSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:TIGR00958 641 LDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMED 703
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
488-701 |
5.89e-51 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 175.10 E-value: 5.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNIlfgtrqvtehqliravqlsgvnlftdlesegldqqvgegghsLSRGQRQTVALARAILNDPPVL 647
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVS-RDRTLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
488-714 |
2.29e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.64 E-value: 2.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQiHPSDLRRNFGY 567
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHG-SVRDNI-----LFGTRQVTEHQLIRAVqLSGVNLftdleSEGLDQQVGegghSLSRGQRQTVALARAIL 641
Cdd:COG1131 78 VPQEPALYPDlTVRENLrffarLYGLPRKEARERIDEL-LELFGL-----TDAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 642 NDPPVLLMDEPTASLDARAEKQFMRSMHN-VSRDRTLLIITHKMHLL-NLVDRIIVMDRGHIIADGPKDKVLEKL 714
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
413-682 |
4.87e-50 |
|
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: 183.33 E-value: 4.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 413 LGVYRVADNDISmGGIIAAVML----ASRAVAPMAQLANLMTRANQTASALRQL--DQIMTQEDEFENKGHLVSKQrlmG 486
Cdd:TIGR02868 258 AGGPAVADGRLA-PVTLAVLVLlplaAFEAFAALPAAAQQLTRVRAAAERIVEVldAAGPVAEGSAPAAGAVGLGK---P 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYPGSEkPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:TIGR02868 334 TLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAvqLSGVNLFTDLES--EGLDQQVGEGGHSLSRGQRQTVALARAILNDP 644
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPDATDEELWAA--LERVGLADWLRAlpDGLDTVLGEGGARLSGGERQRLALARALLADA 490
|
250 260 270
....*....|....*....|....*....|....*...
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITH 682
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
488-711 |
5.46e-49 |
|
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: 172.54 E-value: 5.46e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTL-FHGSVRDNILFG-------TRQVTE--HQLIRAVqLSGVNLfTDLEseglDQQVGEgghsLSRGQRQTVALA 637
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGryphlglFGRPSAedREAVEEA-LERTGL-EHLA----DRPVDE----LSGGERQRVLIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 638 RAILNDPPVLLMDEPTASLDARAEKQFMRSMH--NVSRDRTLLIITHKmhlLNLV----DRIIVMDRGHIIADGPKDKVL 711
Cdd:COG1120 150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHD---LNLAaryaDRLVLLKDGRIVAQGPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
488-701 |
1.55e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 169.61 E-value: 1.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNILFG----TRQVTEHQLIRAVQLSGvnlftdLESEGLDQQVGEgghsLSRGQRQTVALARAILND 643
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlrERKFDRERALELLERLG------LPPDILDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 644 PPVLLMDEPTASLDA----RAEKQFMRSMHNvsRDRTLLIITHKMHLLNLV-DRIIVMDRGHI 701
Cdd:COG4619 149 PDVLLLDEPTSALDPentrRVEELLREYLAE--EGRAVLWVSHDPEQIERVaDRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
488-716 |
2.08e-48 |
|
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: 170.81 E-value: 2.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAqIHPSDLRRNFGY 567
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNI-LFGT-RQVTEHQLIRAVQlsgvNLFTDLE-SEGLDQQVGEgghsLSRGQRQTVALARAILND 643
Cdd:COG4555 79 LPDERGLYdRLTVRENIrYFAElYGLFDEELKKRIE----ELIELLGlEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 644 PPVLLMDEPTASLDARAEKQFMRSMHNV-SRDRTLLIITHKMHLL-NLVDRIIVMDRGHIIADGPKDKVLEKLNQ 716
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
488-705 |
3.29e-48 |
|
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: 167.88 E-value: 3.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsAQIHPSDLRRNFGY 567
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-VSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNIlfGTRqvtehqliravqlsgvnlftdlesegldqqvgegghsLSRGQRQTVALARAILNDPPVL 647
Cdd:cd03247 80 LNQRPYLFDTTLRNNL--GRR-------------------------------------FSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADG 705
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
486-702 |
3.98e-48 |
|
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: 168.74 E-value: 3.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNilfgtrqvtehqLIRAVQLSGVNLFTDLEsegldqqVGEGGHSLSRGQRQTVALARAILNDPP 645
Cdd:cd03369 85 TIIPQDPTLFSGTIRSN------------LDPFDEYSDEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHII 702
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVK 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
488-711 |
4.76e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 169.88 E-value: 4.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsaqihPSDLRRNFGY 567
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTL---FHGSVRDNILFG-TRQV--------TEHQLIRAVqLSGVNLfTDLEseglDQQVGEgghsLSRGQRQTVA 635
Cdd:COG1121 80 VPQRAEVdwdFPITVRDVVLMGrYGRRglfrrpsrADREAVDEA-LERVGL-EDLA----DRPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHN-VSRDRTLLIITHKMH-LLNLVDRIIVMDRGhIIADGPKDKVL 711
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGaVREYFDRVLLLNRG-LVAHGPPEEVL 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
488-708 |
1.11e-47 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 169.53 E-value: 1.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSA---QIHpsDLRRN 564
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeeNLW--EIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQ--DVTLFHGSVRDNILFG--TRQVTEHQLIRAVQLSgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAI 640
Cdd:TIGR04520 79 VGMVFQnpDNQFVGATVEDDVAFGleNLGVPREEMRKRVDEA-------LKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHIIADG-PKD 708
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGtPRE 222
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
172-462 |
2.76e-47 |
|
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: 169.23 E-value: 2.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 172 IYRDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLF 251
Cdd:cd18783 3 LFRDVAIASLILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 252 YKAIGIPLEN-RSASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQ 330
Cdd:cd18783 83 DRLLSLPIDFfERTPAGVLTKHMQQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 331 PRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSV 410
Cdd:cd18783 163 PPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGV 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 411 VILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQL 462
Cdd:cd18783 243 IWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
441-713 |
3.21e-47 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 176.36 E-value: 3.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 441 PMAQLANLMTRANQTASALRQLDQIMTQEDEfENKGHLVSKqRLMGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAI 520
Cdd:PRK11176 297 PLKSLTNVNAQFQRGMAACQTLFAILDLEQE-KDEGKRVIE-RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVAL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 521 IGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFG-TRQVTEHQLIRAV 599
Cdd:PRK11176 375 VGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAA 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 600 QLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLI 679
Cdd:PRK11176 455 RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV 534
|
250 260 270
....*....|....*....|....*....|....
gi 1310934957 680 ITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:PRK11176 535 IAHRLSTIEKADEILVVEDGEIVERGTHAELLAQ 568
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
482-701 |
2.52e-46 |
|
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: 164.57 E-value: 2.52e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 482 QRLMGKIEADDLSFSYPG-SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD 560
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 LRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAI 640
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
488-712 |
2.01e-45 |
|
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: 170.08 E-value: 2.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGS---EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD---L 561
Cdd:COG1123 261 LEVRNLSKRYPVRgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlreL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 RRNFGYLPQDVT--LFHG-SVRDNILFGTRQvteHQLI-------RAVQLsgvnlftdLESEGLDQQVGEG-GHSLSRGQ 630
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIAEPLRL---HGLLsraerreRVAEL--------LERVGLPPDLADRyPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLV-DRIIVMDRGHIIADGPK 707
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYIaDRVAVMYDGRIVEDGPT 489
|
....*
gi 1310934957 708 DKVLE 712
Cdd:COG1123 490 EEVFA 494
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
488-704 |
6.51e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.59 E-value: 6.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP--GSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---- 561
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 RRNFGYLPQDVTLFHG-SVRDNILF-----GTRQVTEHQLIRAVqLSGVNLftdleSEGLDQQVGEgghsLSRGQRQTVA 635
Cdd:COG1136 85 RRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRERAREL-LERVGL-----GDRLDHRPSQ----LSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITHKMHLLNLVDRIIVMDRGHIIAD 704
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
488-701 |
3.52e-44 |
|
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: 156.40 E-value: 3.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQiHPSDLRRNFGY 567
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHG-SVRDNIlfgtrqvtehqliravqlsgvnlftdlesegldqqvgegghSLSRGQRQTVALARAILNDPPV 646
Cdd:cd03230 78 LPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 647 LLMDEPTASLDARAEKQFMRSMHN-VSRDRTLLIITHKMHLL-NLVDRIIVMDRGHI 701
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
488-712 |
6.09e-44 |
|
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: 158.22 E-value: 6.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---RRN 564
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLFHG-SVRDNILFGTRQVTE--HQLIR--------AVQLSGV-NLFTdleSEgldqqvgegghsLSRGQRQ 632
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPLREHTDlsEAEIRelvlekleLVGLPGAaDKMP---SE------------LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 633 TVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDK 709
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDsAFAIADRVAVLADGKIIAEGTPEE 228
|
...
gi 1310934957 710 VLE 712
Cdd:COG1127 229 LLA 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
488-701 |
2.25e-43 |
|
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: 155.73 E-value: 2.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGS--EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---- 561
Cdd:cd03255 1 IELKNLSKTYGGGgeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 RRNFGYLPQDVTLF-HGSVRDNI---LFGTRQVTEHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALA 637
Cdd:cd03255 81 RRHIGFVFQSFNLLpDLTALENVelpLLLAGVPKKERRERAEEL--------LERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 638 RAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
488-712 |
1.22e-42 |
|
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: 161.99 E-value: 1.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPS---NGSLRYDGIDSAQIHPSDLRRN 564
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQD--VTLFHGSVRDNILFG--TRQVTEHQLI-RAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARA 639
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEARaRVLEL--------LEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHL-LNLVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
488-710 |
1.53e-42 |
|
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: 154.20 E-value: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---RRN 564
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLFHG-SVRDNILFGTRQVTE--HQLIRAV---QLSGVNLftdleSEGLDQQVGEgghsLSRGQRQTVALAR 638
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPLREHTRlsEEEIREIvleKLEAVGL-----RGAEDLYPAE----LSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSR--DRTLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDKV 710
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
489-705 |
3.59e-42 |
|
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: 151.05 E-value: 3.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYL 568
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 569 PqdvtlfhgsvrdnilfgtrqvtehQLIRAVQLsgvnlfTDLesegLDQQVGEgghsLSRGQRQTVALARAILNDPPVLL 648
Cdd:cd03214 79 P------------------------QALELLGL------AHL----ADRPFNE----LSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 649 MDEPTASLDARAEKQFMRSMHNVSRDRTLLIIThKMHLLNLV----DRIIVMDRGHIIADG 705
Cdd:cd03214 121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVM-VLHDLNLAaryaDRVILLKDGRIVAQG 180
|
|
| Peptidase_C39_likeD |
cd02421 |
A sub-family of peptidase family C39. Peptidase family C39 mostly contains ... |
18-142 |
4.22e-42 |
|
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: 148.93 E-value: 4.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 18 QRVTVDPLLDSLVLLTEYFGSPCSSESLAAGLPLSSAVLSPELVPQAAARAGLTAKLSRKGLNQVTAIQLPCILLLKDKK 97
Cdd:cd02421 1 DLTRDDPLLDCLVLLARQFGKPASRDSLVAGLPLDDGRLSPALFPRAAARAGLSARVVRRPLDAIPTLLLPAILLLKNGR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1310934957 98 ACILRELDLEQqyAVIQLPET-GGEQRLSIEELETLYVGYLFLVKQ 142
Cdd:cd02421 81 ACVLLGVDDGH--ARILDPESgGGEVEISLEELEEEYSGYAIFVKP 124
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
489-705 |
5.45e-42 |
|
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: 151.92 E-value: 5.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIdsaqiHPSDLRRNFGYL 568
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 569 PQ----DVTlFHGSVRDNILFG-TRQVTEHQLIRAVQLSGVNlfTDLESEGL----DQQVGEgghsLSRGQRQTVALARA 639
Cdd:cd03235 74 PQrrsiDRD-FPISVRDVVLMGlYGHKGLFRRLSKADKAKVD--EALERVGLselaDRQIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMH-LLNLVDRIIVMDRgHIIADG 705
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGlVLEYFDRVLLLNR-TVVASG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
485-704 |
9.51e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 152.55 E-value: 9.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYP--GSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsAQIHPSDLR 562
Cdd:COG1116 5 APALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG---KPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RnfGYLPQDVTLF-HGSVRDNILFGTRQVTE---------HQLIRAVQLSGV-NLFTdlesegldqqvgeggHSLSRGQR 631
Cdd:COG1116 82 R--GVVFQEPALLpWLTVLDNVALGLELRGVpkaerreraRELLELVGLAGFeDAYP---------------HQLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 632 QTVALARAILNDPPVLLMDEPTASLDAraekqFMR-SMHNV------SRDRTLLIITHKMH--LLnLVDRIIVMDR--GH 700
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDA-----LTReRLQDEllrlwqETGKTVLFVTHDVDeaVF-LADRVVVLSArpGR 218
|
....
gi 1310934957 701 IIAD 704
Cdd:COG1116 219 IVEE 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
488-708 |
1.75e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 152.45 E-value: 1.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQ--DVTLFHGSVRDNILFG------TRQVTEHQLIRAVQLSGVNLFTDLESegldqqvgeggHSLSRGQRQTVALARA 639
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAE---KQFMRSMHNVsRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADG-PKD 708
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKreiKKIMVDLRKT-RKKTLISITHDMDEAILADKVIVFSEGKLIAQGkPKE 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
488-705 |
7.10e-41 |
|
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: 148.82 E-value: 7.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRNFGY 567
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGTRQ--VTEHQLIRAVQLSgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDP 644
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGLKLrgVPKAEIRARVREL-------LELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 645 PVLLMDEPTASLDARAeKQFMRS----MHNvSRDRTLLIITHKM-HLLNLVDRIIVMDRGHIIADG 705
Cdd:cd03259 150 SLLLLDEPLSALDAKL-REELREelkeLQR-ELGITTIYVTHDQeEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
489-700 |
1.05e-40 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 146.24 E-value: 1.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYL 568
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 569 PQdvtlfhgsvrdnilfgtrqvtehqliravqlsgvnlftdlesegldqqvgegghsLSRGQRQTVALARAILNDPPVLL 648
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 649 MDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLL-NLVDRIIVMDRGH 700
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
488-710 |
1.70e-40 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 148.10 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGL-----FKPSNGSLRYDG--IDSAQIHPSD 560
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGkdIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 LRRNFGYLPQDVTLFHGSVRDNILFGTRQvteHQLIRAVQLSGVNLFTdLESEGLDQQVGE--GGHSLSRGQRQTVALAR 638
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRL---HGIKLKEELDERVEEA-LRKAALWDEVKDrlHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDKV 710
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
488-699 |
6.65e-40 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 145.69 E-value: 6.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSE---KPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsaqihpsdlrrN 564
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLFHGSVRDNILFGT-------RQVtehqlIRAVQLSgvnlfTDLES-EGLDQ-QVGEGGHSLSRGQRQTVA 635
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpfdeeryEKV-----IKACALE-----PDLEIlPDGDLtEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRS--MHNVSRDRTLLIITHKMHLLNLVDRIIVMDRG 699
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
488-712 |
1.90e-39 |
|
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: 145.72 E-value: 1.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP--GSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTL-FH--GSVRDNI-----LFGTRQVTEhqliRAVQLsgvnlftdLESEGLDQQVGEG-GHSLSRGQRQTVAL 636
Cdd:COG1124 82 QMVFQDPYAsLHprHTVDRILaeplrIHGLPDREE----RIAEL--------LEQVGLPPSFLDRyPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLN-LVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAhLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
488-704 |
2.31e-39 |
|
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: 144.54 E-value: 2.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP--GSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlrrnF 565
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLF-HGSVRDNILFG-------TRQVTEH--QLIRAVQLSGV-NLFTdlesegldqqvgeggHSLSRGQRQTV 634
Cdd:cd03293 76 GYVFQQDALLpWLTVLDNVALGlelqgvpKAEARERaeELLELVGLSGFeNAYP---------------HQLSGGMRQRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDAraekqFMR-SMHNV------SRDRTLLIITHKMH-LLNLVDRIIVMDR--GHIIAD 704
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDA-----LTReQLQEElldiwrETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
488-711 |
4.71e-39 |
|
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: 144.75 E-value: 4.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHpFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNN-LNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNI-----LFGtrqVTEHQLI-RAVQLSGVnlfTDLESEGLDQQVgegGHSLSRGQRQTVALARAI 640
Cdd:cd03295 80 VIQQIGLFpHMTVEENIalvpkLLK---WPKEKIReRADELLAL---VGLDPAEFADRY---PHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
505-654 |
6.21e-39 |
|
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: 140.86 E-value: 6.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 505 LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLF-HGSVRDNI 583
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 584 LFGTRQVTEHQLIRAVQ----LSGVNLftdleSEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTA 654
Cdd:pfam00005 81 RLGLLLKGLSKREKDARaeeaLEKLGL-----GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
488-700 |
8.10e-39 |
|
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: 141.56 E-value: 8.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPgsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDSAQIHPSDLRRNF 565
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLF-HGSVRDNILFGtrqvtehqliravqLSGvnlftdlesegldqqvgegghslsrGQRQTVALARAILNDP 644
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG--------------LSG-------------------------GQQQRVALARALAMDP 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMHNVsRDR---TLLIITHKMH-LLNLVDRIIVMDRGH 700
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSL-QAQlgiTVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
311-712 |
1.86e-38 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 151.02 E-value: 1.86e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 311 LALIPL-VASLIIIGYTLIVQPRLKTAieeSNKFASLkHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRsk 389
Cdd:PRK10789 142 LALLPMpVMAIMIKRYGDQLHERFKLA---QAAFSSL-NDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMR-- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 390 klsnsVANV-ANF--VVQLTVVSVVIL----GVYRVADNDISMGGIIAAVMLASRAVAPMAQLA---NLMTRANQTASAL 459
Cdd:PRK10789 216 -----VARIdARFdpTIYIAIGMANLLaiggGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAwmfNIVERGSAAYSRI 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 460 RQldqiMTQEDEFENKGHL-VSKQRlmGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGL 538
Cdd:PRK10789 291 RA----MLAEAPVVKDGSEpVPEGR--GELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 539 FKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQ 618
Cdd:PRK10789 365 FDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 619 VGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDR 698
Cdd:PRK10789 445 VGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQH 524
|
410
....*....|....
gi 1310934957 699 GHIIADGPKDKVLE 712
Cdd:PRK10789 525 GHIAQRGNHDQLAQ 538
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
488-707 |
2.09e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.11 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSeKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD---LRRN 564
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTL-FHGSVRDNILF-----GTRQVTEHQLIRAVqlsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALAR 638
Cdd:COG2884 81 IGVVFQDFRLlPDRTVYENVALplrvtGKSRKEIRRRVREV----------LDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR-TLLIITHKMHLLNLVD-RIIVMDRGHIIADGPK 707
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGtTVLIATHDLELVDRMPkRVLELEDGRLVRDEAR 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
485-701 |
8.16e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.45 E-value: 8.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRN 564
Cdd:COG3839 1 MASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD--RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLF-HGSVRDNILFG-----------TRQVTEhqLIRAVQLSGVnlftdlesegLDQQVGEgghsLSRGQRQ 632
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrkvpkaeiDRRVRE--AAELLGLEDL----------LDRKPKQ----LSGGQRQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 633 TVALARAILNDPPVLLMDEPTASLDA--RAEkqfMRS----MHNvSRDRTLLIITHKMH-LLNLVDRIIVMDRGHI 701
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAklRVE---MRAeikrLHR-RLGTTTIYVTHDQVeAMTLADRIAVMNDGRI 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
488-712 |
1.03e-37 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 144.13 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGID-SAQIHPSDlrRNFG 566
Cdd:COG1118 3 IEVRNISKRFGS--FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRE--RRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLF-HGSVRDNILFG-----------TRQVTEhqLIRAVQLsgvnlftdlesEGLDQ----QvgegghsLSRGQ 630
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlrvrppskaeiRARVEE--LLELVQL-----------EGLADrypsQ-------LSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITHKMHL-LNLVDRIIVMDRGHIIADGPK 707
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDElgGTTVFVTHDQEEaLELADRVVVMNQGRIEQVGTP 218
|
....*
gi 1310934957 708 DKVLE 712
Cdd:COG1118 219 DEVYD 223
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
486-713 |
2.22e-37 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 147.94 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYpGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:PRK10790 339 GRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNILFGtRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPP 645
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
488-705 |
5.80e-37 |
|
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: 138.02 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP--GSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---R 562
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQD--------VTLFHgSVRDNILFGTRQVTEHQLIRAVQLSGVNLftDLESEGLDQQVgeggHSLSRGQRQTV 634
Cdd:cd03257 82 KEIQMVFQDpmsslnprMTIGE-QIAEPLRIHGKLSKKEARKEAVLLLLVGV--GLPEEVLNRYP----HELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLL-NLVDRIIVMDRGHIIADG 705
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVaKIADRVAVMYAGKIVEEG 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
485-706 |
1.07e-36 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 141.39 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRN 564
Cdd:COG3842 3 MPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLF-HGSVRDNILFG--TRQVTEHQLIRAVQlsgvnlftdlesEGLDqQVGEGG------HSLSRGQRQTVA 635
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlrMRGVPKAEIRARVA------------ELLE-LVGLEGladrypHQLSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMH-LLNLVDRIIVMDRGHIIADGP 706
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEeALALADRIAVMNDGRIEQVGT 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
488-705 |
1.75e-36 |
|
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: 136.17 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGeRIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsAQIHPSDLRRNFGY 567
Cdd:cd03264 1 LQLENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRD-----NILFGTRQVTEHQLIRAVqLSGVNLFtdlesEGLDQQVGegghSLSRGQRQTVALARAIL 641
Cdd:cd03264 77 LPQEFGVYpNFTVREfldyiAWLKGIPSKEVKARVDEV-LELVNLG-----DRAKKKIG----SLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 642 NDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADG 705
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
487-722 |
1.79e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 138.61 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQ--DVTLFHGSVRDNILFG--TRQVTEHQLIR----AVQLSGVNLFTDLESegldqqvgeggHSLSRGQRQTVALAR 638
Cdd:PRK13635 85 MVFQnpDNQFVGATVQDDVAFGleNIGVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLeKLNQ 716
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF-KSGH 232
|
....*.
gi 1310934957 717 GLMAGG 722
Cdd:PRK13635 233 MLQEIG 238
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
171-448 |
2.89e-36 |
|
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: 138.49 E-value: 2.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 171 PIYRDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRL 250
Cdd:cd18782 2 RALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 251 FYKAIGIPLEN-RSASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIV 329
Cdd:cd18782 82 IDHLLRLPLGFfDKRPVGELSTRISELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 330 QPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVS 409
Cdd:cd18782 162 GPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLL 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 1310934957 410 VVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANL 448
Cdd:cd18782 242 VLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTL 280
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
488-711 |
3.77e-36 |
|
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: 136.75 E-value: 3.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVG-LFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLF---HGSVRDNIL---FGT----RQVTEHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVAL 636
Cdd:COG1119 82 LVSPALQLRfprDETVLDVVLsgfFDSiglyREPTDEQRERAREL--------LELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITHkmHL---LNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTH--HVeeiPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
488-711 |
1.19e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 135.28 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:PRK13548 3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTL-FHGSVRDNILFG-----TRQVTEHQLIRAVqlsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAIL 641
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGraphgLSRAEDDALVAAA----------LAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 642 ------NDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIIthkMHLLNLV----DRIIVMDRGHIIADGPKDK 709
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVV---LHDLNLAaryaDRIVLLHQGRLVADGTPAE 227
|
..
gi 1310934957 710 VL 711
Cdd:PRK13548 228 VL 229
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
172-448 |
1.37e-35 |
|
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: 136.54 E-value: 1.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 172 IYRDALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLF 251
Cdd:cd18568 3 LLAEILLASLLLQLLGLALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 252 YKAIGIPL---ENRSasVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLI 328
Cdd:cd18568 83 KHLLSLPLsffASRK--VGDIITRFQENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 329 VQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVV 408
Cdd:cd18568 161 SSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1310934957 409 SVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANL 448
Cdd:cd18568 241 AVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
488-682 |
1.64e-35 |
|
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: 133.37 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQiHPSDLRRNFGY 567
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHG-SVRDNILF-----GTRQVTE--HQLIRAVQLSGVnlftdlesegLDQQVGEgghsLSRGQRQTVALARA 639
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaalyGLRADREaiDEALEAVGLAGL----------ADLPVRQ----LSAGQKRRVALARL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHN-VSRDRTLLIITH 682
Cdd:COG4133 146 LLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
445-708 |
2.18e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 144.73 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 445 LANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQR------LMGKIEADDLSFSYPGSEKPVLHPFALRIRPGERI 518
Cdd:PLN03232 1186 LSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRpvsgwpSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKV 1265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 519 AIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNIlfgtRQVTEHQ---L 595
Cdd:PLN03232 1266 GVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI----DPFSEHNdadL 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 596 IRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR 675
Cdd:PLN03232 1342 WEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC 1421
|
250 260 270
....*....|....*....|....*....|....
gi 1310934957 676 TLLIITHKMHLLNLVDRIIVMDRGHIIA-DGPKD 708
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLSSGQVLEyDSPQE 1455
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
488-712 |
3.18e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 133.58 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDSAQIHPSDLRRNF 565
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGedLTDSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLF-HGSVRDNILFGTRQV----TEHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAI 640
Cdd:COG1126 80 GMVFQQFNLFpHLTVLENVTLAPIKVkkmsKAEAEERAMEL--------LERVGLADKADAYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLNLV-DRIIVMDRGHIIADGPKDKVLE 712
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEgMTMVVVTHEMGFAREVaDRVVFMDGGRIVEEGPPEEFFE 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
510-711 |
3.21e-35 |
|
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: 134.01 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-----LRRNFgylpQDVTLFHG-SVRDNI 583
Cdd:COG0411 25 LEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRiarlgIARTF----QNPRLFPElTVLENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 LFGTRQVTEHQLIRAVqlsgVNLFTDLESE--------------GLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLM 649
Cdd:COG0411 101 LVAAHARLGRGLLAAL----LRLPRARREEreareraeellervGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 650 DEPTASLDArAEKQ-FMRSMHNVSRDR--TLLIITHKMHLL-NLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:COG0411 177 DEPAAGLNP-EETEeLAELIRRLRDERgiTILLIEHDMDLVmGLADRIVVLDFGRVIAEGTPAEVR 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
488-712 |
3.49e-35 |
|
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: 132.94 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSekPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-LRRNFG 566
Cdd:cd03224 1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFHG-SVRDNILFGTRQVTEHQliRAVQLSGV-NLFTDLEsEGLDQQVGegghSLSRGQRQTVALARAILNDP 644
Cdd:cd03224 79 YVPEGRRIFPElTVEENLLLGAYARRRAK--RKARLERVyELFPRLK-ERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHL-LNLVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEgVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
488-713 |
9.16e-35 |
|
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: 132.46 E-value: 9.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSekPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRNFGY 567
Cdd:cd03296 3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGTR-----------QVTE--HQLIRAVQLSGvnlftdLESEGLDQqvgegghsLSRGQRQT 633
Cdd:cd03296 79 VFQHYALFrHMTVFDNVAFGLRvkprserppeaEIRAkvHELLKLVQLDW------LADRYPAQ--------LSGGQRQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 634 VALARAILNDPPVLLMDEPTASLDARAEKQ---FMRSMHnvsrDR---TLLIITH-KMHLLNLVDRIIVMDRGHIIADGP 706
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKElrrWLRRLH----DElhvTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
|
....*..
gi 1310934957 707 KDKVLEK 713
Cdd:cd03296 221 PDEVYDH 227
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
484-715 |
1.11e-34 |
|
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: 132.73 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 484 LMGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRR 563
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 564 NFGYLPQDVTLFHGSVRDNiLFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILND 643
Cdd:cd03288 96 RLSIILQDPILFSGSIRFN-LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 644 PPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEKLN 715
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQED 246
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
510-711 |
1.16e-34 |
|
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: 131.79 E-value: 1.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-----LRRNFgylpQDVTLFHG-SVRDNI 583
Cdd:cd03219 21 FSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEiarlgIGRTF----QIPRLFPElTVLENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 LFGTRQVTEH-------------------QLIRAVQLSGVnlftdlesegLDQQVGEgghsLSRGQRQTVALARAILNDP 644
Cdd:cd03219 97 MVAAQARTGSglllararreereareraeELLERVGLADL----------ADRPAGE----LSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 645 PVLLMDEPTASLdARAEKQFM----RSMHnvSRDRTLLIITHKMHL-LNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:cd03219 163 KLLLLDEPAAGL-NPEETEELaeliRELR--ERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
488-706 |
1.43e-34 |
|
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: 131.55 E-value: 1.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLS--FSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---R 562
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQDVTLFHG-SVRDNILF-----GTRQvtEHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVAL 636
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiaGVPK--AEIEERVLEL--------LELVGLEDKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLL-NLVDRIIVMDRGHIIADGP 706
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVkRICDRVAVMEKGEVVEEGT 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
488-713 |
2.02e-34 |
|
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: 131.54 E-value: 2.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSeKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---RRN 564
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLF-HGSVRDNILFGT-----------RQVTEHQLIRAVQLsgvnlftdLESEGLD----QQVGEgghsLSR 628
Cdd:cd03256 80 IGMIFQQFNLIeRLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAA--------LERVGLLdkayQRADQ----LSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 629 GQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMH--NVSRDRTLLIITHKMHL-LNLVDRIIVMDRGHIIADG 705
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDG 227
|
....*...
gi 1310934957 706 PKDKVLEK 713
Cdd:cd03256 228 PPAELTDE 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
488-701 |
5.03e-34 |
|
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: 129.19 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGI----DSAQIHpsDLRR 563
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLkltdDKKNIN--ELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 564 NFGYLPQDVTLF-HGSVRDNILFGTRQV---TEHQLI-RAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALAR 638
Cdd:cd03262 77 KVGMVFQQFNLFpHLTVLENITLAPIKVkgmSKAEAEeRALEL--------LEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLNLV-DRIIVMDRGHI 701
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREVaDRVIFMDDGRI 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
488-705 |
5.05e-34 |
|
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: 129.55 E-value: 5.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQiHPSDLRRNFGY 567
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHG-SVRDNILFGTRqvtehqliravqLSGVNLFT-DLESEGLDQQVGEGGH------SLSRGQRQTVALARA 639
Cdd:cd03263 80 CPQFDALFDElTVREHLRFYAR------------LKGLPKSEiKEEVELLLRVLGLTDKankrarTLSGGMKRKLSLAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLN-LVDRIIVMDRGHIIADG 705
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEaLCDRIAIMSDGKLRCIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
488-711 |
5.36e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.87 E-value: 5.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEkpvLHpFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRNFGY 567
Cdd:COG3840 2 LRLDDLTYRYGDFP---LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE--RPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGTR-----QVTEHQLIRAVqLSGVNLfTDLESEGLDQqvgegghsLSRGQRQTVALARAIL 641
Cdd:COG3840 76 LFQENNLFpHLTVAQNIGLGLRpglklTAEQRAQVEQA-LERVGL-AGLLDRLPGQ--------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 642 NDPPVLLMDEPTASLDArAEKQFM----RSMHNvSRDRTLLIITHkmHL---LNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:COG3840 146 RKRPILLLDEPFSALDP-ALRQEMldlvDELCR-ERGLTVLMVTH--DPedaARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
488-705 |
9.48e-34 |
|
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: 128.64 E-value: 9.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPV--LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQiHPSDLRRNF 565
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHG-SVRDNILFGTRQvteHQLIRAVQLSGVN-LFTDLE-SEGLDQQVGEgghsLSRGQRQTVALARAILN 642
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEYFAGL---YGLKGDELTARLEeLADRLGmEELLDRRVGG----FSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 643 DPPVLLMDEPTASLD---ARAEKQFMRsmHNVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADG 705
Cdd:cd03266 154 DPPVLLLDEPTTGLDvmaTRALREFIR--QLRALGKCILFSTHIMQeVERLCDRVVVLHRGRVVYEG 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
486-701 |
4.03e-33 |
|
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: 137.38 E-value: 4.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:TIGR00957 1283 GRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNI-LFGtrQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDP 644
Cdd:TIGR00957 1363 TIIPQDPVLFSGSLRMNLdPFS--QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:TIGR00957 1441 KILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
486-702 |
1.53e-32 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 135.64 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRdnilFGTRQVTEHqliravqlSGVNLFTDLE-----------SEGLDQQVGEGGHSLSRGQRQTV 634
Cdd:PLN03130 1316 GIIPQAPVLFSGTVR----FNLDPFNEH--------NDADLWESLErahlkdvirrnSLGLDAEVSEAGENFSVGQRQLL 1383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHII 702
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVV 1451
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
488-701 |
2.09e-32 |
|
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: 125.43 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRNFGY 567
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGTR-----------QVTEhqLIRAVQLSGvnlftdLESEGLDQqvgegghsLSRGQRQTVA 635
Cdd:cd03300 77 VFQNYALFpHLTVFENIAFGLRlkklpkaeikeRVAE--ALDLVQLEG------YANRKPSQ--------LSGGQQQRVA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITH-KMHLLNLVDRIIVMDRGHI 701
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHdQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
510-720 |
4.35e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 124.76 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRNFGYLPQDVTLF-HGSVRDNILFGTR 588
Cdd:cd03299 20 LEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAYGLK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 589 QVTEHQLIRAVQLSGVNlftdlESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSM 668
Cdd:cd03299 98 KRKVDKKEIERKVLEIA-----EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 669 HNVSR--DRTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVLEKLNQGLMA 720
Cdd:cd03299 173 KKIRKefGVTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVA 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
490-702 |
9.23e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 130.18 E-value: 9.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 490 ADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLrydgidsaqIHPSDLRrnFGYLP 569
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV---------SIPKGLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 QDVTLF-HGSVRDNILFGTRQVTE-----HQLIRAVQLSGVN------LFTDLESEG---------------------LD 616
Cdd:COG0488 68 QEPPLDdDLTVLDTVLDGDAELRAleaelEELEAKLAEPDEDlerlaeLQEEFEALGgweaearaeeilsglgfpeedLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 617 QQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPTASLDARA----EkQFMRsmhnvSRDRTLLIITHKMHLLN-LVD 691
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlE-EFLK-----NYPGTVLVVSHDRYFLDrVAT 217
|
250
....*....|.
gi 1310934957 692 RIIVMDRGHII 702
Cdd:COG0488 218 RILELDRGKLT 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
504-711 |
1.03e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 132.98 E-value: 1.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 504 VLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNI 583
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 -LFgtRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILN-DPPVLLMDEPTASLDARAE 661
Cdd:PTZ00243 1405 dPF--LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALD 1482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 662 KQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADG-PKDKVL 711
Cdd:PTZ00243 1483 RQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGsPRELVM 1533
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
514-705 |
1.04e-31 |
|
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: 122.79 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 514 PGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG---IDSAQ-IHPSDLRRNFGYLPQDVTLF-HGSVRDNILFGTR 588
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkINLPPQQRKIGLVFQQYALFpHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 589 QVTEHQL-IRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRS 667
Cdd:cd03297 102 RKRNREDrISVDEL--------LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1310934957 668 MHNVSRD--RTLLIITHKM-HLLNLVDRIIVMDRGHIIADG 705
Cdd:cd03297 174 LKQIKKNlnIPVIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
488-706 |
1.42e-31 |
|
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: 122.93 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPV--LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsaqIHPSD----- 560
Cdd:COG4181 9 IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD---LFALDedara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 --LRRNFGYLPQDVTLF-HGSVRDNI-----LFGTRQVTEhqliRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQ 632
Cdd:COG4181 86 rlRARHVGFVFQSFQLLpTLTALENVmlpleLAGRRDARA----RARAL--------LERVGLGHRLDHYPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 633 TVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHIIADGP 706
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
488-713 |
2.01e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.14 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKP---SNGSLRYDGIDSAQIHPSDLRRN 564
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQ--DVTLFHGSVRDNILFG--TRQVTEHQLIRAVQ--LSGVNLFTDLESEgldqqvgegGHSLSRGQRQTVALAR 638
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEMIKIVRdvLADVGMLDYIDSE---------PANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLI--ITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVisITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
489-712 |
2.26e-31 |
|
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: 122.40 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFSYPGSekPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL-RRNFGY 567
Cdd:COG0410 5 EVENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHG-SVRDNILFGTRQVTEHQLIRAVqLSGV-NLFTDLEsEGLDQQVGegghSLSRGQRQTVALARAILNDPP 645
Cdd:COG0410 83 VPEGRRIFPSlTVEENLLLGAYARRDRAEVRAD-LERVyELFPRLK-ERRRQRAG----TLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHL-LNLVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREgVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
450-702 |
4.25e-31 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 128.26 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 450 TRANQTASALRQLDQIMTQEDEFENKG---HLVSKQRLmGK--IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRN 524
Cdd:COG0488 274 RKAKQAQSRIKALEKLEREEPPRRDKTveiRFPPPERL-GKkvLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 525 GSGKSTLAKLLVGLFKPSNGSLRY-DGIdsaqihpsdlrrNFGYLPQDVTLFHG--SVRDNILFGTRQVTEhqlIRAVQL 601
Cdd:COG0488 351 GAGKSTLLKLLAGELEPDSGTVKLgETV------------KIGYFDQHQEELDPdkTVLDELRDGAPGGTE---QEVRGY 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 602 SGVNLFTdleSEGLDQQVGegghSLSRGQRQTVALARAILNDPPVLLMDEPT-----ASLDARAE--KQFmrsmhnvsrD 674
Cdd:COG0488 416 LGRFLFS---GDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTnhldiETLEALEEalDDF---------P 479
|
250 260
....*....|....*....|....*....
gi 1310934957 675 RTLLIITHKMHLLN-LVDRIIVMDRGHII 702
Cdd:COG0488 480 GTVLLVSHDRYFLDrVATRILEFEDGGVR 508
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
488-701 |
4.95e-31 |
|
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: 120.82 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPgsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRNFGY 567
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFG------TRQVTEHQLIRAVQLSGVnlftdleSEGLDQQVgeggHSLSRGQRQTVALARAI 640
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELLQI-------EHLLDRKP----KQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQfMRS----MHNvSRDRTLLIITH-KMHLLNLVDRIIVMDRGHI 701
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQ-MRAelkrLQQ-RLGTTTIYVTHdQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
488-704 |
8.04e-31 |
|
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: 118.30 E-value: 8.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSekPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRnfgy 567
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARR---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 lpqdvtlfHGsvrdnilfgtrqvtehqlIRAVqlsgvnlftdlesegldqqvgeggHSLSRGQRQTVALARAILNDPPVL 647
Cdd:cd03216 75 --------AG------------------IAMV------------------------YQLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNV-SRDRTLLIITHKM-HLLNLVDRIIVMDRGHIIAD 704
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLrAQGVAVIFISHRLdEVFEIADRVTVLRDGRVVGT 163
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
505-711 |
8.44e-31 |
|
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: 124.44 E-value: 8.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 505 LHPFALRIR---PGERI-AIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG---IDSAQIHpsDL---RRNFGYLPQDVTL 574
Cdd:COG4148 11 RGGFTLDVDftlPGRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGI--FLpphRRRIGYVFQEARL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 F-HGSVRDNILFGTRQVTEHQliRAVQLSG-VNLF--TDLesegLDQQVgeggHSLSRGQRQTVALARAILNDPPVLLMD 650
Cdd:COG4148 89 FpHLSVRGNLLYGRKRAPRAE--RRISFDEvVELLgiGHL----LDRRP----ATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 651 EPTASLDARAeKQ----FMRSMHnvsrDRT---LLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:COG4148 159 EPLAALDLAR-KAeilpYLERLR----DELdipILYVSHSLDeVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
509-720 |
2.16e-30 |
|
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: 122.91 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 509 ALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGI---DSAQ-IHPSDLRRNFGYLPQDVTLF-HGSVRDNI 583
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKgIFLPPEKRRIGYVFQEARLFpHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 LFGTRQVTEHQliRAVQLSGVnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQ 663
Cdd:TIGR02142 97 RYGMKRARPSE--RRISFERV-----IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 664 FMRSMHNVSR--DRTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVLEKLNQGLMA 720
Cdd:TIGR02142 170 ILPYLERLHAefGIPILYVSHSLqEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLA 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
488-706 |
2.43e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.52 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSekPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRN-FG 566
Cdd:COG1129 5 LEMRGISKSFGGV--KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLF-HGSVRDNILFGtRQVTEHQLI-------RAVQLsgvnlftdLESEGLD----QQVGEgghsLSRGQRQTV 634
Cdd:COG1129 83 IIHQELNLVpNLSVAENIFLG-REPRRGGLIdwramrrRAREL--------LARLGLDidpdTPVGD----LSVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNV-SRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADGP 706
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkAQGVAIIYISHRLDeVFEIADRVTVLRDGRLVGTGP 223
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
488-708 |
9.16e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 119.42 E-value: 9.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSY----PGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQI-HPSDLR 562
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQ--DVTLFHGSVRDNILFGTRQV-TEHQLIRA-VQLSgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALAR 638
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGPENLgIPPEEIRErVDES-------LKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHIIADG-PKD 708
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGtPKE 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
503-712 |
9.25e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.89 E-value: 9.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 503 PVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGID----SAQIHpsDLRRNFGYLPQDVTLF-HG 577
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvndpKVDER--LIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 578 SVRDNILFGTRQV------TEHQLIRAVqlsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDE 651
Cdd:PRK09493 93 TALENVMFGPLRVrgaskeEAEKQAREL----------LAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 652 PTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLNLV-DRIIVMDRGHIIADGPKDKVLE 712
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVaSRLIFIDKGRIAEDGDPQVLIK 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
488-710 |
1.08e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.38 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSY-PGS--EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGID--SAQIHPSDLR 562
Cdd:PRK13637 3 IKIENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQ--DVTLFHGSVRDNILFGTRQV------TEHQLIRAVQLSGvnlftdLESEGL-DQQVGEgghsLSRGQRQT 633
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGPINLglseeeIENRVKRAMNIVG------LDYEDYkDKSPFE----LSGGQKRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 634 VALARAILNDPPVLLMDEPTASLDARAEKQFM---RSMHNvSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDK 709
Cdd:PRK13637 153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILnkiKELHK-EYNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGTPRE 231
|
.
gi 1310934957 710 V 710
Cdd:PRK13637 232 V 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
250-705 |
2.68e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 125.47 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 250 LFYKAIGIPLENRSASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIiyLVAGDLALIPLVASLII---IGYT 326
Cdd:PLN03232 380 IFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMV--LLYQQLGVASLFGSLILfllIPLQ 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 327 LIVQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLS-------NSVANVA 399
Cdd:PLN03232 458 TLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSafnsfilNSIPVVV 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 400 NFVVqltvvsvviLGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFenkghLV 479
Cdd:PLN03232 538 TLVS---------FGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERI-----LA 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 480 SKQRLMGKIEADDLS---FSYPG-SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPsngslrydgidsAQ 555
Cdd:PLN03232 604 QNPPLQPGAPAISIKngyFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH------------AE 671
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 556 IHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEhQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVA 635
Cdd:PLN03232 672 TSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESE-RYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVS 750
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRS-MHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADG 705
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG 821
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
177-462 |
3.05e-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: 118.00 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 177 LIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAIG 256
Cdd:cd18555 8 LLLSLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 257 IPL---ENRsaSVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPRL 333
Cdd:cd18555 88 LPYsffENR--SSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 334 KTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVIL 413
Cdd:cd18555 166 KKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1310934957 414 GVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQL 462
Cdd:cd18555 246 GAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
488-715 |
4.63e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 117.01 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSeKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQihPSDL---RRN 564
Cdd:PRK13644 2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGD--FSKLqgiRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDV-TLFHG-SVRDNILFGTRQVT--EHQLIRAVQLSgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAI 640
Cdd:PRK13644 79 VGIVFQNPeTQFVGrTVEEDLAFGPENLClpPIEIRKRVDRA-------LAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEKLN 715
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
488-705 |
6.41e-29 |
|
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: 114.90 E-value: 6.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPvLHpFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRNFGY 567
Cdd:cd03298 1 VRLDKIRFSY--GEQP-MH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD--RPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGtrqVTEHQLIRAVQLSGVnlftdlesEGLDQQVGEGG------HSLSRGQRQTVALARAI 640
Cdd:cd03298 75 LFQENNLFaHLTVEQNVGLG---LSPGLKLTAEDRQAI--------EVALARVGLAGlekrlpGELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 641 LNDPPVLLMDEPTASLDA--RAEKQFMRSMHNVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADG 705
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPalRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
488-701 |
7.71e-29 |
|
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: 114.43 E-value: 7.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSeKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD---LRRN 564
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLF-HGSVRDNILFGTRQVTE-HQLIRAvQLSGVnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILN 642
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFALEVTGVpPREIRK-RVPAA-----LELVGLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 643 DPPVLLMDEPTASLDARAEKQFMRSMHNVS-RDRTLLIITHKMHLLNLVD-RIIVMDRGHI 701
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINkAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
508-711 |
9.09e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 115.06 E-value: 9.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 508 FALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRNFGYLPQDVTLF-HGSVRDNI--- 583
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFsHLTVAQNIglg 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 ------LFGTRQVTEHQLIRAVQLSgvNLFTDLESEgldqqvgegghsLSRGQRQTVALARAILNDPPVLLMDEPTASLD 657
Cdd:PRK10771 96 lnpglkLNAAQREKLHAIARQMGIE--DLLARLPGQ------------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 658 ARAEKQFMRSMHNVSRDR--TLLIITHkmhllNLVD------RIIVMDRGHIIADGPKDKVL 711
Cdd:PRK10771 162 PALRQEMLTLVSQVCQERqlTLLMVSH-----SLEDaariapRSLVVADGRIAWDGPTDELL 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
488-712 |
1.03e-28 |
|
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: 117.08 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVlhpFALR-----IRPGERIAIIGRNGSGKSTLAKLLVGLFKP---SNGSLRYDGIDSAQIHPS 559
Cdd:COG0444 2 LEVRNLKVYFPTRRGVV---KAVDgvsfdVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 560 DLR----RNFGYLPQD--------VTlfhgsVRDnilfgtrQVTE----HQLI-------RAVQLsgvnlftdLESEGLD 616
Cdd:COG0444 79 ELRkirgREIQMIFQDpmtslnpvMT-----VGD-------QIAEplriHGGLskaeareRAIEL--------LERVGLP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 617 QQVGEGG---HSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLL-NLV 690
Cdd:COG0444 139 DPERRLDrypHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVaEIA 218
|
250 260
....*....|....*....|..
gi 1310934957 691 DRIIVMDRGHIIADGPKDKVLE 712
Cdd:COG0444 219 DRVAVMYAGRIVEEGPVEELFE 240
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
488-710 |
1.49e-28 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 117.49 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRNFGY 567
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGTRQVTEH-------------QLIRAVQLSgvNLFTDLESEgldqqvgegghsLSRGQRQT 633
Cdd:PRK10851 79 VFQHYALFrHMTVFDNIAFGLTVLPRRerpnaaaikakvtQLLEMVQLA--HLADRYPAQ------------LSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 634 VALARAILNDPPVLLMDEPTASLDARAEKQ---FMRSMHNVSRdRTLLIITH-KMHLLNLVDRIIVMDRGHIIADGPKDK 709
Cdd:PRK10851 145 VALARALAVEPQILLLDEPFGALDAQVRKElrrWLRQLHEELK-FTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
|
.
gi 1310934957 710 V 710
Cdd:PRK10851 224 V 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
488-705 |
2.00e-28 |
|
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: 113.62 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQiHPSDLRRNFGY 567
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLfhgsvrDNILFGTRQVTEHQLIRAVQ-----------LSGVNLFtdlesEGLDQQVGegghSLSRGQRQTVAL 636
Cdd:cd03265 78 VFQDLSV------DDELTGWENLYIHARLYGVPgaerreridelLDFVGLL-----EAADRLVK----TYSGGMRRRLEI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQ---FMRSMhNVSRDRTLLIITHKMHLLN-LVDRIIVMDRGHIIADG 705
Cdd:cd03265 143 ARSLVHRPEVLFLDEPTIGLDPQTRAHvweYIEKL-KEEFGMTILLTTHYMEEAEqLCDRVAIIDHGRIIAEG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
487-710 |
3.05e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 113.98 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLvglfkpsN------------GSLRYDGID-- 552
Cdd:COG1117 11 KIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCL-------NrmndlipgarveGEILLDGEDiy 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 553 SAQIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTR---QVTEHQLIRAVQ--LSGVNLFTDLESEgLDQQvgegGHSLS 627
Cdd:COG1117 82 DPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRlhgIKSKSELDEIVEesLRKAALWDEVKDR-LKKS----ALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 628 RGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADGP 706
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFGP 236
|
....
gi 1310934957 707 KDKV 710
Cdd:COG1117 237 TEQI 240
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
488-718 |
3.98e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 113.64 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP--------------------GSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLR 547
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 548 YDGIDSAQIhpsDLrrNFGylpqdvtlFHG--SVRDNILFG------TRQVTEHQL--IRAvqlsgvnlFTDLEsEGLDQ 617
Cdd:COG1134 85 VNGRVSALL---EL--GAG--------FHPelTGRENIYLNgrllglSRKEIDEKFdeIVE--------FAELG-DFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 618 QVGegghSLSRGQRQTVALARAILNDPPVLLMDEPTASLDAR-AEK--QFMRSMhnVSRDRTLLIITHKMHLL-NLVDRI 693
Cdd:COG1134 143 PVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKclARIREL--RESGRTVIFVSHSMGAVrRLCDRA 216
|
250 260
....*....|....*....|....*
gi 1310934957 694 IVMDRGHIIADGPKDKVLEKLNQGL 718
Cdd:COG1134 217 IWLEKGRLVMDGDPEEVIAAYEALL 241
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
177-449 |
4.78e-28 |
|
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: 114.48 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 177 LIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAIG 256
Cdd:cd18567 8 LLLSLALELFALASPLYLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 257 IPL---ENRSasVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPRL 333
Cdd:cd18567 88 LPLsyfEKRH--LGDIVSRFGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 334 KTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVIL 413
Cdd:cd18567 166 RRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYL 245
|
250 260 270
....*....|....*....|....*....|....*.
gi 1310934957 414 GVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLM 449
Cdd:cd18567 246 GALLVLDGEFTVGMLFAFLAYKDQFSSRASSLIDKL 281
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
488-712 |
9.12e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 115.81 E-value: 9.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRNFGY 567
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGTR-QVTEHQLI--------RAVQLsgvnlftdlesEGLDQQvgeGGHSLSRGQRQTVALA 637
Cdd:PRK09452 91 VFQSYALFpHMTVFENVAFGLRmQKTPAAEItprvmealRMVQL-----------EEFAQR---KPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 638 RAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITH-KMHLLNLVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
497-704 |
1.70e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 497 YPGS--EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIhPSDLR-RNFGYLPQDV- 572
Cdd:COG1101 12 NPGTvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRaKYIGRVFQDPm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 573 --TLFHGSVRDNILFGTRQVTEHQLIRAV----------QLSGVNLftDLESEgLDQQVGegghSLSRGQRQTVALARAI 640
Cdd:COG1101 91 mgTAPSMTIEENLALAYRRGKRRGLRRGLtkkrrelfreLLATLGL--GLENR-LDTKVG----LLSGGQRQALSLLMAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMR-SMHNVSRDR-TLLIITHKM-HLLNLVDRIIVMDRGHIIAD 704
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTAALVLElTEKIVEENNlTTLMVTHNMeQALDYGNRLIMMHEGRIILD 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
510-713 |
1.85e-27 |
|
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: 112.35 E-value: 1.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRR-----------NFGYLPqdvtlfHGS 578
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALLP------HRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 579 VRDNILFG------TRQVTEHQLIRAVQLSGvnlftdLESEGlDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEP 652
Cdd:cd03294 119 VLENVAFGlevqgvPRAEREERAAEALELVG------LEGWE-HKYPDE----LSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 653 TASLDA--RAEKQ--FMRSMHNvsRDRTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:cd03294 188 FSALDPliRREMQdeLLRLQAE--LQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
167-711 |
2.06e-27 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 119.36 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 167 KDSAPIYRDALIASILVNLFALVSPLFIMNVYDkvVPNLAFES----LWVLAIGAGIaylfdLVMRQLRSYLIDVAGKKV 242
Cdd:PTZ00265 825 KDVTIIALSILVAGGLYPVFALLYAKYVSTLFD--FANLEANSnkysLYILVIAIAM-----FISETLKNYYNNVIGEKV 897
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 243 DIIVSSRLF----YKAIGIpLENRSASVGGMARQLGefdsiREI--LTSATITTLVdlPFALLFVLIIYLVAGDLALIPL 316
Cdd:PTZ00265 898 EKTMKRRLFenilYQEISF-FDQDKHAPGLLSAHIN-----RDVhlLKTGLVNNIV--IFTHFIVLFLVSMVMSFYFCPI 969
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 317 VASLIIIGY-----TLIVQPRLKTAIEESNKFASLKHGHLI----------------ESLASLESIKSYGAEGLVQKAWQ 375
Cdd:PTZ00265 970 VAAVLTGTYfifmrVFAIRARLTANKDVEKKEINQPGTVFAynsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCNLIE 1049
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 376 QMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQT 455
Cdd:PTZ00265 1050 KAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENA 1129
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 456 ASALRQLDQIMTQE---DEFENKG-HLVSKQRLMGKIEADDLSFSYPGSEK-PVLHPFALRIRPGERIAIIGRNGSGKST 530
Cdd:PTZ00265 1130 KLSFEKYYPLIIRKsniDVRDNGGiRIKNKNDIKGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKST 1209
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 531 LAKLLV-------------------------------------------------------GLFKpSNGSLRYDGIDSAQ 555
Cdd:PTZ00265 1210 VMSLLMrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedsTVFK-NSGKILLDGVDICD 1288
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 556 IHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVA 635
Cdd:PTZ00265 1289 YNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIA 1368
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNV--SRDRTLLIITHKMHLLNLVDRIIVM---DR--GHIIADGPKD 708
Cdd:PTZ00265 1369 IARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFnnpDRtgSFVQAHGTHE 1448
|
...
gi 1310934957 709 KVL 711
Cdd:PTZ00265 1449 ELL 1451
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
176-448 |
2.60e-27 |
|
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: 112.54 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18570 7 ILLLSLLITLLGIAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL---ENRSasVGGMARQLGEFDSIREILTSATITTLVDLpFALLFVLII-YLVAGDLALIPLVASLIIIGYTLIVQP 331
Cdd:cd18570 87 KLPLsffETRK--TGEIISRFNDANKIREAISSTTISLFLDL-LMVIISGIIlFFYNWKLFLITLLIIPLYILIILLFNK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 332 RLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVV 411
Cdd:cd18570 164 PFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLIL 243
|
250 260 270
....*....|....*....|....*....|....*..
gi 1310934957 412 ILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANL 448
Cdd:cd18570 244 WIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINL 280
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
488-706 |
6.67e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.36 E-value: 6.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKP--VLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---- 561
Cdd:PRK10535 5 LELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 RRNFGYLPQDVTLF-HGSVRDN-----ILFGTRqvTEHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVA 635
Cdd:PRK10535 85 REHFGFIFQRYHLLsHLTAAQNvevpaVYAGLE--RKQRLLRAQEL--------LQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVsRDR--TLLIITHKMHLLNLVDRIIVMDRGHIIADGP 706
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRghTVIIVTHDPQVAAQAERVIEIRDGEIVRNPP 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
485-706 |
7.79e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.84 E-value: 7.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDSA------QI 556
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitIDTArslsqqKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 557 HPSDLRRNFGYLPQDVTLF-HGSVRDNILFGTRQVTEHQLIRAVQLsGVNLftdLESEGLDQQVGEGGHSLSRGQRQTVA 635
Cdd:PRK11264 79 LIRQLRQHVGFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATAR-AREL---LAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLNLV-DRIIVMDRGHIIADGP 706
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVaDRAIFMDQGRIVEQGP 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
488-708 |
8.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDV-TLFHGS-VRDNILFG--TRQVTEHQLIRAVQ--LSGVNLFTDLESEgldqqvgegGHSLSRGQRQTVALARAIL 641
Cdd:PRK13648 88 VFQNPdNQFVGSiVKYDVAFGleNHAVPYDEMHRRVSeaLKQVDMLERADYE---------PNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 642 NDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHIIADG-PKD 708
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGtPTE 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
487-711 |
2.57e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 2.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFHG-SVRD---------NILFGTRQVTEHQLI-RAVQLSGVNLFTDLESEgldqqvgegghSLSRGQRQTVA 635
Cdd:PRK11231 80 LLPQHHLTPEGiTVRElvaygrspwLSLWGRLSAEDNARVnQAMEQTRINHLADRRLT-----------DLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIIthkMHLLN----LVDRIIVMDRGHIIADGPKDKV 710
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTV---LHDLNqasrYCDHLVVLANGHVMAQGTPEEV 225
|
.
gi 1310934957 711 L 711
Cdd:PRK11231 226 M 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
429-704 |
4.15e-26 |
|
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: 113.35 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 429 IAAVMLASRAvaPMAQLAN---LMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQRLMGKIEADDLSFSYPGSEKP-- 503
Cdd:COG4615 268 FVLVLLFLRG--PLSQLVGalpTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDeg 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 504 -VLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDSAQIHpsDLRRNFGYLPQDVTLFHGsvr 580
Cdd:COG4615 346 fTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpVTADNRE--AYRQLFSAVFSDFHLFDR--- 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 581 dniLFGTRQVTEHQLIRAvqlsgvnLFTDLEsegLDQQVG-EGGH----SLSRGQRQTVALARAILNDPPVLLMDEPTAS 655
Cdd:COG4615 421 ---LLGLDGEADPARARE-------LLERLE---LDHKVSvEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDEWAAD 487
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 656 LDARAEKQF-------MRsmhnvSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIAD 704
Cdd:COG4615 488 QDPEFRRVFytellpeLK-----ARGKTVIAISHDDRYFDLADRVLKMDYGKLVEL 538
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
486-701 |
4.20e-26 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 108.40 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKpSNGSLRYDGIDSAQIHPSDLRRNF 565
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNiLFGTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPP 645
Cdd:cd03289 80 GVIPQKVFIFSGTFRKN-LDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:cd03289 159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
488-705 |
4.90e-26 |
|
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: 105.71 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPG----SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPS--NGSLRYDGIdsaQIHPSDL 561
Cdd:cd03213 4 LSFRNLTVTVKSspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGR---PLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 RRNFGYLPQDvTLFHGS--VRDNILFgtrqvtehqlirAVQLSGvnlftdlesegldqqvgegghsLSRGQRQTVALARA 639
Cdd:cd03213 81 RKIIGYVPQD-DILHPTltVRETLMF------------AAKLRG----------------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITH--KMHLLNLVDRIIVMDRGHIIADG 705
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTgRTIICSIHqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
514-710 |
5.13e-26 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 109.96 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 514 PGERI-AIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG---IDSAQ-IHPSDLRRNFGYLPQDVTLF-HGSVRDNILFGT 587
Cdd:PRK11144 22 PAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKgICLPPEKRRIGYVFQDARLFpHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 588 RQVTEHQLIRAVQLSGVN-LFTDLEsegldqqvgeggHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMR 666
Cdd:PRK11144 102 AKSMVAQFDKIVALLGIEpLLDRYP------------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1310934957 667 SMHNVSRDRTLLII--THKM-HLLNLVDRIIVMDRGHIIADGPKDKV 710
Cdd:PRK11144 170 YLERLAREINIPILyvSHSLdEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
485-696 |
5.86e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 107.64 E-value: 5.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGS--EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsAQIHPSDLR 562
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG---VPVTGPGAD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RnfGYLPQDVTLFHG-SVRDNILFG---------TRQVTEHQLIRAVQLSGVNlftdleseglDQQVgeggHSLSRGQRQ 632
Cdd:COG4525 78 R--GVVFQKDALLPWlNVLDNVAFGlrlrgvpkaERRARAEELLALVGLADFA----------RRRI----WQLSGGMRQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 633 TVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITHKM-HLLNLVDRIIVM 696
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRtgKGVFLITHSVeEALFLATRLVVM 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
488-706 |
7.33e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 109.40 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPV--LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---R 562
Cdd:COG1135 2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQDVTLFHG-SVRDNILF-----GT------RQVTEhqLIRAVQLSgvnlftDLESEGLDQqvgegghsLSRGQ 630
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALpleiaGVpkaeirKRVAE--LLELVGLS------DKADAYPSQ--------LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHllnlV-----DRIIVMDRGHIIA 703
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMD----VvrricDRVAVLENGRIVE 221
|
...
gi 1310934957 704 DGP 706
Cdd:COG1135 222 QGP 224
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
508-701 |
2.89e-25 |
|
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: 104.17 E-value: 2.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 508 FALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRNFGYLPQDVTLF-HGSVRDNILFG 586
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY--QRPVSMLFQENNLFaHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 587 TR---QVTEHQLIRAVQLSgvnlftdlESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDA--RAE 661
Cdd:TIGR01277 95 LHpglKLNAEQQEKVVDAA--------QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPllREE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1310934957 662 KQFMRSMHNVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHI 701
Cdd:TIGR01277 167 MLALVKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
176-447 |
3.01e-25 |
|
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: 106.48 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18779 7 ILLASLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL---ENRSAsvGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPR 332
Cdd:cd18779 87 RLPYrffQQRST--GDLLMRLSSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 333 LKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVVI 412
Cdd:cd18779 165 VRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLW 244
|
250 260 270
....*....|....*....|....*....|....*
gi 1310934957 413 LGVYRVADNDISMGGIIAAVMLASRAVAPMAQLAN 447
Cdd:cd18779 245 VGAWQVLDGQLSLGTMLALNALAGAFLAPLASLVG 279
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
488-712 |
3.95e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.43 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGiDSAQIHPSDLRRNFGY 567
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTL---FhgSVRDNIL-FGTRQVTEHQLIRAvQLSGVNLFTDLESEGlDQQVGEgghsLSRGQRQTVALARAILND 643
Cdd:PRK13537 85 VPQFDNLdpdF--TVRENLLvFGRYFGLSAAAARA-LVPPLLEFAKLENKA-DAKVGE----LSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 644 PPVLLMDEPTASLDARAEK---QFMRSMhnVSRDRTLLIITHKMHLLN-LVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHlmwERLRSL--LARGKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
520-721 |
4.39e-25 |
|
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: 106.81 E-value: 4.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 520 IIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlRRNFGYLPQDVTLF-HGSVRDNILFGTRQvteHQLIRA 598
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFGLKM---RKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 599 VQLSGVNlftdlESEGLDQQVGEGG---HSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR 675
Cdd:TIGR01187 76 EIKPRVL-----EALRLVQLEEFADrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1310934957 676 --TLLIITH-KMHLLNLVDRIIVMDRGHIIADGPKDKVLEKLNQGLMAG 721
Cdd:TIGR01187 151 giTFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVAR 199
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
488-713 |
4.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.70 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP-GSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDSAQIHPSDLRRN 564
Cdd:PRK13636 6 LKVEELNYNYSdGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQ--DVTLFHGSVRDNILFG--TRQVTEHQLIRAVQLSgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAI 640
Cdd:PRK13636 84 VGMVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNA-------LKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSR--DRTLLIITHKMHLLNL-VDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
441-713 |
5.58e-25 |
|
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: 111.58 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 441 PMAQLANLMTRANQTASALRQLDQIMTQE----DEFENKghlVSKQRLMGKIEADDLSFSYPGSEKPVLHPFALRIRPGE 516
Cdd:TIGR00957 589 PLNILPMVISSIVQASVSLKRLRIFLSHEelepDSIERR---TIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGA 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 517 RIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsaqihpsdlrrNFGYLPQDVTLFHGSVRDNILFGtrQVTEHQLI 596
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFG--KALNEKYY 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 597 RAVqLSGVNLFTDLE--SEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSM---HNV 671
Cdd:TIGR00957 731 QQV-LEACALLPDLEilPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGV 809
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1310934957 672 SRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:TIGR00957 810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
488-700 |
1.50e-24 |
|
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: 99.83 E-value: 1.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRydgidsaqiHPSDLRrnFGY 567
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT---------WGSTVK--IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPqdvtlfhgsvrdnilfgtrqvtehqliravQLSGvnlftdlesegldqqvgegghslsrGQRQTVALARAILNDPPVL 647
Cdd:cd03221 68 FE------------------------------QLSG-------------------------GEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVsrDRTLLIITHKMHLLNLV-DRIIVMDRGH 700
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEY--PGTVILVSHDRYFLDQVaTKIIELEDGK 144
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
488-705 |
1.63e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSY-PGS--EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRydgIDSAQIHPS----- 559
Cdd:PRK13634 3 ITFQKVEHRYqYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT---IGERVITAGkknkk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 560 --DLRRNFGYLPQ--DVTLFHGSVRDNILFGTRQ--VTEHQLIR----AVQLSGvnlftdLESEGLDQQVGEgghsLSRG 629
Cdd:PRK13634 80 lkPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQkareMIELVG------LPEELLARSPFE----LSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 630 QRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLII--THKMH-LLNLVDRIIVMDRGHIIADG 705
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVlvTHSMEdAARYADQIVVMHKGTVFLQG 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
448-714 |
1.72e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.30 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 448 LMTRANQTASALRQLDQIMTQEDEfenkGHLVSKQRLMGK-----IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIG 522
Cdd:PRK13536 1 LLTRAVAEEAPRRLELSPIERKHQ----GISEAKASIPGSmstvaIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 523 RNGSGKSTLAKLLVGLFKPSNGSLRYDGID-SAQIHPSdlRRNFGYLPQDVTL-FHGSVRDNIL-FGTRQVTEHQLIRAV 599
Cdd:PRK13536 75 PNGAGKSTIARMILGMTSPDAGKITVLGVPvPARARLA--RARIGVVPQFDNLdLEFTVRENLLvFGRYFGMSTREIEAV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 600 qLSGVNLFTDLESEGlDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEK---QFMRSMhnVSRDRT 676
Cdd:PRK13536 153 -IPSLLEFARLESKA-DARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHliwERLRSL--LARGKT 224
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1310934957 677 LLIITHKMHLLN-LVDRIIVMDRGHIIADG-PKDKVLEKL 714
Cdd:PRK13536 225 ILLTTHFMEEAErLCDRLCVLEAGRKIAEGrPHALIDEHI 264
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
488-711 |
1.77e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 106.46 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTL-FHgsvrdnilFGTRQVTEhqLIRAVQLSGVNLFTDLESEGLDQQVGEGG---------HSLSRGQRQTVALA 637
Cdd:PRK09536 82 VPQDTSLsFE--------FDVRQVVE--MGRTPHRSRFDTWTETDRAAVERAMERTGvaqfadrpvTSLSGGERQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 638 RAILNDPPVLLMDEPTASLDARAEKQFMRSMHN-VSRDRTLLIITHKMHL-LNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRlVDDGKTAVAAIHDLDLaARYCDELVLLADGRVRAAGPPADVL 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
244-687 |
2.30e-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: 109.61 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 244 IIVSSRLFYKAIGIPLENRSASVGGM--ARQLGEFDSIREILTSATITTLVDLPFALLFVL-IIYLVA-----GDLALIP 315
Cdd:TIGR01271 954 LTVSKRLHEQMLHSVLQAPMAVLNTMkaGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLgAIFVVSvlqpyIFIAAIP 1033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 316 LVASLIII-GYTLIVQPRLKTAIEESNkfaSLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIG-HTANW-----QLRS 388
Cdd:TIGR01271 1034 VAVIFIMLrAYFLRTSQQLKQLESEAR---SPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNlHTANWflylsTLRW 1110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 389 KKLSNSVANVANFVVQLtvvsvvILGVYRVADNDISMGGIIAAVMLASR----AVAPMAQLANLMtranQTASALRQLDQ 464
Cdd:TIGR01271 1111 FQMRIDIIFVFFFIAVT------FIAIGTNQDGEGEVGIILTLAMNILStlqwAVNSSIDVDGLM----RSVSRVFKFID 1180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 465 IMTQEDEFENKGHLVSKQRLM--------------GKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKST 530
Cdd:TIGR01271 1181 LPQEEPRPSGGGGKYQLSTVLvienphaqkcwpsgGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST 1260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 531 LAKLLVGLFKpSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFHGSVRDNiLFGTRQVTEHQLIRAVQLSGVNLFTDL 610
Cdd:TIGR01271 1261 LLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-LDPYEQWSDEEIWKVAEEVGLKSVIEQ 1338
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 611 ESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLL 687
Cdd:TIGR01271 1339 FPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEAL 1415
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
488-705 |
2.62e-24 |
|
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: 102.03 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSY------PG-------------SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRY 548
Cdd:cd03267 1 IEVSNLSKSYrvyskePGligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 549 DGIDsaqihPSDLRRNFgylpqdvtlfhgSVRDNILFGTRQ--------VTEHQLIRAV----------QLSGVNLFTDL 610
Cdd:cd03267 81 AGLV-----PWKRRKKF------------LRRIGVVFGQKTqlwwdlpvIDSFYLLAAIydlpparfkkRLDELSELLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 611 ESEgLDQQVgeggHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMH-LL 687
Cdd:cd03267 144 EEL-LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKdIE 218
|
250
....*....|....*...
gi 1310934957 688 NLVDRIIVMDRGHIIADG 705
Cdd:cd03267 219 ALARRVLVIDKGRLLYDG 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
496-696 |
3.40e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 100.39 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 496 SYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsaqihpsdlRRNFGYLPQDVTL- 574
Cdd:NF040873 1 GYGG--RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 --FHGSVRDNILFGT--------------RQVTEHQLiRAVQLsgvnlfTDLEseglDQQVGEgghsLSRGQRQTVALAR 638
Cdd:NF040873 68 dsLPLTVRDLVAMGRwarrglwrrltrddRAAVDDAL-ERVGL------ADLA----GRQLGE----LSGGQRQRALLAQ 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSM-HNVSRDRTLLIITHKMHLLNLVDRIIVM 696
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
471-708 |
4.11e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.99 E-value: 4.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 471 EFENKGHLVSKQRLMGKIEADDLSFSypgsekpvlhpfalrIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRydg 550
Cdd:PRK13641 4 KFENVDYIYSPGTPMEKKGLDNISFE---------------LEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 551 IDSAQIHPS-------DLRRNFGYLPQ--DVTLFHGSVRDNILFGTRQ--VTEHQL-IRAVQLsgvnlftdLESEGLDQQ 618
Cdd:PRK13641 66 IAGYHITPEtgnknlkKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAkEKALKW--------LKKVGLSED 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 619 VGEggHS---LSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRI 693
Cdd:PRK13641 138 LIS--KSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMdDVAEYADDV 215
|
250
....*....|....*.
gi 1310934957 694 IVMDRGHIIA-DGPKD 708
Cdd:PRK13641 216 LVLEHGKLIKhASPKE 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
422-699 |
4.88e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.20 E-value: 4.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 422 DISMGGIIAAVMLASRAVAPMAQLANLMTR-ANQTASALR--QLDQIMTQEDEfENKGHLVSKQRLMGKIEADDLSFSYP 498
Cdd:COG4178 295 EITLGGLMQAASAFGQVQGALSWFVDNYQSlAEWRATVDRlaGFEEALEAADA-LPEAASRIETSEDGALALEDLTLRTP 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 499 gSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRydgidsaqiHPSDLRRNFgyLPQDVTLFHGS 578
Cdd:COG4178 374 -DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA---------RPAGARVLF--LPQRPYLPLGT 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 579 VRDNILF--GTRQVTEHQLIRAVQLsgVNLfTDLeSEGLDQQVgEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASL 656
Cdd:COG4178 442 LREALLYpaTAEAFSDAELREALEA--VGL-GHL-AERLDEEA-DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1310934957 657 DARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRG 699
Cdd:COG4178 517 DEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
488-701 |
5.18e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 5.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSY-PGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQ--DVTLFHGSVRDNILFG-TRQVTEHQLIR-----AVQLSGVNLFTDLESEgldqqvgegghSLSRGQRQTVALAR 638
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFGlENKGIPHEEMKervneALELVGMQDFKEREPA-----------RLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
488-711 |
6.89e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 101.31 E-value: 6.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQD------VTlfhgsVRDNILFG---------TRQVTEH--QLIRAVQLsgvnlfTDLESEGLDQqvgegghsLSRGQ 630
Cdd:COG4604 80 LRQEnhinsrLT-----VRELVAFGrfpyskgrlTAEDREIidEAIAYLDL------EDLADRYLDE--------LSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIIthkMHLLNLV----DRIIVMDRGHIIAD 704
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIV---LHDINFAscyaDHIVAMKDGRVVAQ 217
|
....*..
gi 1310934957 705 GPKDKVL 711
Cdd:COG4604 218 GTPEEII 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
491-699 |
7.16e-24 |
|
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: 102.24 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 491 DDLSFS-YPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSaqihpsdlrrnfgYLP 569
Cdd:cd03291 38 NNLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS-------------FSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 QDVTLFHGSVRDNILFGTR--QVTEHQLIRAVQLS-GVNLFTDLESEGLdqqvGEGGHSLSRGQRQTVALARAILNDPPV 646
Cdd:cd03291 105 QFSWIMPGTIKENIIFGVSydEYRYKSVVKACQLEeDITKFPEKDNTVL----GEGGITLSGGQRARISLARAVYKDADL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 647 LLMDEPTASLDARAEKQ-FMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRG 699
Cdd:cd03291 181 YLLDSPFGYLDVFTEKEiFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
488-705 |
8.20e-24 |
|
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: 99.98 E-value: 8.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAqiHPSDLRRNFGY 567
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNI-----LFGTRQVTEHQLIRAVQLSGVNlftdleseglDQQVGegghSLSRGQRQTVALARAIL 641
Cdd:cd03268 77 LIEAPGFYpNLTARENLrllarLLGIRKKRIDEVLDVVGLKDSA----------KKKVK----GFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 642 NDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLNLV-DRIIVMDRGHIIADG 705
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKVaDRIGIINKGKLIEEG 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
488-714 |
1.32e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 102.47 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP---------GSEKPVLHP----------FALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRY 548
Cdd:COG4586 2 IEVENLSKTYRvyekepglkGALKGLFRReyreveavddISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 549 DGIDsaqihPSDLRRNFGYlpqdvtlfhgsvrdNI--LFGTRQvtehQLI------------RAV-QLSG------VNLF 607
Cdd:COG4586 82 LGYV-----PFKRRKEFAR--------------RIgvVFGQRS----QLWwdlpaidsfrllKAIyRIPDaeykkrLDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 608 TD-LESEG-LDQQVgeggHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEK---QFMRSMhNVSRDRTLLIITH 682
Cdd:COG4586 139 VElLDLGElLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEairEFLKEY-NRERGTTILLTSH 213
|
250 260 270
....*....|....*....|....*....|...
gi 1310934957 683 KMH-LLNLVDRIIVMDRGHIIADGPKDKVLEKL 714
Cdd:COG4586 214 DMDdIEALCDRVIVIDHGRIIYDGSLEELKERF 246
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
485-705 |
1.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.03 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGSEKpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGS--LRYDGIDSAQIHpsDLR 562
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlIRGEPITKENIR--EVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQ--DVTLFHGSVRDNILFG------TRQVTEHQLIRAVQLSGVnlftdlesEGLDQQVGeggHSLSRGQRQTV 634
Cdd:PRK13652 78 KFVGLVFQnpDDQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGL--------EELRDRVP---HHLSGGEKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLII--THKMHLL-NLVDRIIVMDRGHIIADG 705
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVpEMADYIYVMDKGRIVAYG 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
502-682 |
1.58e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 99.09 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 502 KPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKP---SNGSLRYDG--IDSAQIHpsdlRRNFGYLPQDVTLF- 575
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrLTALPAE----QRRIGILFQDDLLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 576 HGSVRDNILFGT-RQVTEHQLIRAVQlsgvnlfTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTA 654
Cdd:COG4136 90 HLSVGENLAFALpPTIGRAQRRARVE-------QALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190
....*....|....*....|....*....|
gi 1310934957 655 SLDARAEKQFMRSMHNVSRDRTL--LIITH 682
Cdd:COG4136 163 KLDAALRAQFREFVFEQIRQRGIpaLLVTH 192
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
489-701 |
2.30e-23 |
|
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: 97.89 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFsypgseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRN-FGY 567
Cdd:cd03215 6 EVRGLSV------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQD---VTLFHG-SVRDNILFGtrqvtehqliraVQLSGvnlftdlesegldqqvgegghslsrGQRQTVALARAILND 643
Cdd:cd03215 80 VPEDrkrEGLVLDlSVAENIALS------------SLLSG-------------------------GNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 644 PPVLLMDEPTASLDARAeKQFMRSMHNVSRDR--TLLIITHKMH-LLNLVDRIIVMDRGHI 701
Cdd:cd03215 123 PRVLILDEPTRGVDVGA-KAEIYRLIRELADAgkAVLLISSELDeLLGLCDRILVMYEGRI 182
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
441-719 |
2.90e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 105.98 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 441 PMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQrlMGKIEADDLSFSY-PGSEKPVLHPFALRIRPGERIA 519
Cdd:PLN03130 570 PLFMLPNLITQAVNANVSLKRLEELLLAEERVLLPNPPLEPG--LPAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 520 IIGRNGSGKSTLAKLLVGLFKP-SNGSLRydgidsaqihpsdLRRNFGYLPQDVTLFHGSVRDNILFGTrQVTEHQLIRA 598
Cdd:PLN03130 648 IVGSTGEGKTSLISAMLGELPPrSDASVV-------------IRGTVAYVPQVSWIFNATVRDNILFGS-PFDPERYERA 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 599 VQLSGvnLFTDLES-EGLDQ-QVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQ-FMRSMHNVSRDR 675
Cdd:PLN03130 714 IDVTA--LQHDLDLlPGGDLtEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQvFDKCIKDELRGK 791
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1310934957 676 TLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLE--KLNQGLM 719
Cdd:PLN03130 792 TRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNngPLFQKLM 837
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
488-712 |
2.95e-23 |
|
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: 99.15 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-LRRNFG 566
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFHG-SVRDNILFgtrqVTE-HQLIRAVQLSGVN-LFTDLESEGLDQQVgegGHSLSRGQRQTVALARAILND 643
Cdd:cd03218 79 YLPQEASIFRKlTVEENILA----VLEiRGLSKKEREEKLEeLLEEFHITHLRKSK---ASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 644 PPVLLMDEPTASLDARAEKQFMRSMHNVsRDRTL--LIITHKMH-LLNLVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIgvLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
485-705 |
3.46e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.17 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKI-EADDLSFSYPG-SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLR 562
Cdd:PRK13642 1 MNKIlEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQ--DVTLFHGSVRDNILFGTRQ--VTEHQLIRAVQ--LSGVNLftdlesegLDQQVGEGGHsLSRGQRQTVAL 636
Cdd:PRK13642 81 RKIGMVFQnpDNQFVGATVEDDVAFGMENqgIPREEMIKRVDeaLLAVNM--------LDFKTREPAR-LSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVsRDR---TLLIITHKMHLLNLVDRIIVMDRGHIIADG 705
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI-KEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
488-708 |
3.99e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.77 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP-GSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDSAQIHPSDLRRN 564
Cdd:PRK13639 2 LETRDLKYSYPdGTE--ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQ--DVTLFHGSVRDNILFG------TRQVTEHQLIRAVQLSGVnlftdlesEGLDQQVGeggHSLSRGQRQTVAL 636
Cdd:PRK13639 80 VGIVFQnpDDQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGM--------EGFENKPP---HHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLNL-VDRIIVMDRGHIIADG-PKD 708
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVyADKVYVMSDGKIIKEGtPKE 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
501-705 |
5.68e-23 |
|
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: 97.99 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIhpsdlrrNFGylpqdvTLFHG--S 578
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-------GLG------GGFNPelT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 579 VRDNILF-----GTRQVTEHQLIRAVQlsgvnLFTDLEsEGLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPT 653
Cdd:cd03220 101 GRENIYLngrllGLSRKEIDEKIDEII-----EFSELG-DFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 654 ASLDAR-AEK--QFMRSMhnVSRDRTLLIITHKMHLL-NLVDRIIVMDRGHIIADG 705
Cdd:cd03220 171 AVGDAAfQEKcqRRLREL--LKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
509-710 |
5.85e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.91 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 509 ALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYD-----GIDSAQIHPSDLRRNFgylpQDVTLFHG-SVRDN 582
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieGLPGHQIARMGVVRTF----QHVRLFREmTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 583 ILfgtrqVTEHQLIRAVQLSGV---NLFTDLESEGLDQ------QVG-------EGGhSLSRGQRQTVALARAILNDPPV 646
Cdd:PRK11300 101 LL-----VAQHQQLKTGLFSGLlktPAFRRAESEALDRaatwleRVGllehanrQAG-NLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 647 LLMDEPTASLDARAEKQF------MRSMHNVSrdrtLLIITHKMHL-LNLVDRIIVMDRGHIIADGPKDKV 710
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELdeliaeLRNEHNVT----VLLIEHDMKLvMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
488-713 |
7.13e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 99.41 E-value: 7.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsAQIHPSDlRRNFGY 567
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LP------QDVTlfhgsVRDNIL-FGT-RQVTEHQLIRAVQlsgvNLFTDLE-SEGLDQQVGEgghsLSRGQRQTVALAR 638
Cdd:COG4152 76 LPeerglyPKMK-----VGEQLVyLARlKGLSKAEAKRRAD----EWLERLGlGDRANKKVEE----LSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 639 AILNDPPVLLMDEPTASLD---ARAEKQFMRSMHNvsRDRTLLIITHKMHLL-NLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:COG4152 143 ALLHDPELLILDEPFSGLDpvnVELLKDVIRELAA--KGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
488-707 |
8.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGY 567
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDV--TLFHGSVRDNILFGTRQVtehQLIRAVQLSGVNlfTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPP 645
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGPVNM---GLDKDEVERRVE--EALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHL-LNLVDRIIVMDRGHIIADGPK 707
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDK 222
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
503-700 |
1.09e-22 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 104.22 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 503 PVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsaqihpsdlrrNFGYLPQDVTLFHGSVRDN 582
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 583 ILFGTR--QVTEHQLIRAVQLS-GVNLFTDLESEGLdqqvGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDAR 659
Cdd:TIGR01271 507 IIFGLSydEYRYTSVIKACQLEeDIALFPEKDKTVL----GEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1310934957 660 AEKQ-FMRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGH 700
Cdd:TIGR01271 583 TEKEiFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGV 624
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
501-708 |
1.54e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.44 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHpSDLRRNFgylpQDVTLFH-GSV 579
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAR-EDTRLMF----QDARLLPwKKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 580 RDNILFGTRQVTEHQLIRAvqlsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDA- 658
Cdd:PRK11247 99 IDNVGLGLKGQWRDAALQA-----------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAl 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 659 -RAEKQFMrsMHNVSRDR--TLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKD 708
Cdd:PRK11247 168 tRIEMQDL--IESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEGKIGLDLTVD 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
487-716 |
2.09e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.93 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYPGS---EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGID----SAQIHPS 559
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 560 DLRRNFGYLPQ--DVTLFHGSVRDNILFGTRQVTEHqlIRAVQLSGVNLFTDLeseGLDQQVGEGG-HSLSRGQRQTVAL 636
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVKNYAHRLLMDL---GFSRDVMSQSpFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQFMRSMH--NVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADG-PKD--KV 710
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTsPKElfKD 236
|
....*.
gi 1310934957 711 LEKLNQ 716
Cdd:PRK13646 237 KKKLAD 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
488-712 |
2.11e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 99.91 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPsdLRRNFGY 567
Cdd:PRK11607 20 LEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLF-HGSVRDNILFGTRQvteHQLIRAVQLSGVNLFTDLESegLDQQVGEGGHSLSRGQRQTVALARAILNDPPV 646
Cdd:PRK11607 96 MFQSYALFpHMTVEQNIAFGLKQ---DKLPKAEIASRVNEMLGLVH--MQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 647 LLMDEPTASLDARAEKQFMRSMHNVsRDR---TLLIITH-KMHLLNLVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDI-LERvgvTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
488-706 |
4.04e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.33 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKPV--LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---R 562
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQDVTLFHG-SVRDNILFgtrqvtehqlirAVQLSGVNLfTDLES--EGLDQQVGEGGH------SLSRGQRQT 633
Cdd:PRK11153 82 RQIGMIFQHFNLLSSrTVFDNVAL------------PLELAGTPK-AEIKArvTELLELVGLSDKadrypaQLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 634 VALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLL-NLVDRIIVMDRGHIIADGP 706
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
176-459 |
5.34e-22 |
|
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: 96.85 E-value: 5.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd07346 4 ALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL----ENRSASVggMARQLGEFDSIREILTSATITTLVDLpfALLFVLIIYLVAGD--LALIPLVASLIIIGYTLIV 329
Cdd:cd07346 84 RLSLsffdRNRTGDL--MSRLTSDVDAVQNLVSSGLLQLLSDV--LTLIGALVILFYLNwkLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 330 QPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVS 409
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1310934957 410 VVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASAL 459
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
488-705 |
6.36e-22 |
|
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: 94.65 E-value: 6.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsAQIHPSDlRRNFGY 567
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFhgsvRDnilfgtRQVTEhQLIRAVQLSGVNL---------------FTDLESEGLDQqvgegghsLSRGQRQ 632
Cdd:cd03269 75 LPEERGLY----PK------MKVID-QLVYLAQLKGLKKeearrridewlerleLSEYANKRVEE--------LSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 633 TVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLL-NLVDRIIVMDRGHIIADG 705
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
510-714 |
6.91e-22 |
|
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: 99.88 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRY----DGIDSAQIHPsDLR----RNFGYLPQDVTLF-HGSVR 580
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGP-DGRgrakRYIGILHQEYDLYpHRTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 581 DNIL--FGTRQVTEHQLIRAVQLSGVNLFTDLESEG-LDQQVgeggHSLSRGQRQTVALARAILNDPPVLLMDEPTASLD 657
Cdd:TIGR03269 384 DNLTeaIGLELPDELARMKAVITLKMVGFDEEKAEEiLDKYP----DELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 658 ARAEKQFMRSMHNVSRD--RTLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDKVLEKL 714
Cdd:TIGR03269 460 PITKVDVTHSILKAREEmeQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIGDPEEIVEEL 519
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
488-709 |
7.62e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 99.74 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSekPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdLRRNFG- 566
Cdd:PRK15439 12 LCARSISKQYSGV--EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YL-PQDVTLFHG-SVRDNILFG--TRQVTEHQLIRAVQLSGVNLftdleseGLDQQVGegghSLSRGQRQTVALARAILN 642
Cdd:PRK15439 89 YLvPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQL-------DLDSSAG----SLEVADRQIVEILRGLMR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 643 DPPVLLMDEPTASLD-ARAEKQFMRSMHNVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDK 709
Cdd:PRK15439 158 DSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPeIRQLADRISVMRDGTIALSGKTAD 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
510-710 |
8.29e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.72 E-value: 8.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG----IDSaqihPSD-LRRNFGYLPQDVTLFHG-SVRDNI 583
Cdd:COG3845 26 LTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpvrIRS----PRDaIALGIGMVHQHFMLVPNlTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 LFGTRQV--------TEHQLIRAV-QLSGVNLftDlesegLDQQVgeggHSLSRGQRQTVALARAILNDPPVLLMDEPTA 654
Cdd:COG3845 102 VLGLEPTkggrldrkAARARIRELsERYGLDV--D-----PDAKV----EDLSVGEQQRVEILKALYRGARILILDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 655 SLDARAEKQFMRSMHN-VSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDKV 710
Cdd:COG3845 171 VLTPQEADELFEILRRlAAEGKSIIFITHKLReVMAIADRVTVLRRGKVVGTVDTAET 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
485-712 |
1.03e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.71 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsaqIhpSDL--- 561
Cdd:COG1137 1 MMTLEAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED---I--THLpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 ---RRNFGYLPQDVTLFHG-SVRDNIL--FGTRQVTEHQ-LIRAVQLsgvnlftdLESEGL----DQQvgegGHSLSRGQ 630
Cdd:COG1137 74 kraRLGIGYLPQEASIFRKlTVEDNILavLELRKLSKKErEERLEEL--------LEEFGIthlrKSK----AYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLD--ARAE-KQFMRSMhnvsRDRTL--LIITHKMH-LLNLVDRIIVMDRGHIIAD 704
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpiAVADiQKIIRHL----KERGIgvLITDHNVReTLGICDRAYIISEGKVLAE 217
|
....*...
gi 1310934957 705 GPKDKVLE 712
Cdd:COG1137 218 GTPEEILN 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
520-705 |
1.16e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.46 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 520 IIGRNGSGKSTLAKLLVGLFKPSNGSLR----YDGIDSAQIHPSD------------LRRNFGYLPQ--DVTLFHGSVRD 581
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELITnpyskkiknfkeLRRRVSMVFQfpEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 582 NILFGTRQVTEHQlIRAVQLSGVNLftdlESEGLDQQVGE-GGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARA 660
Cdd:PRK13631 137 DIMFGPVALGVKK-SEAKKLAKFYL----NKMGLDDSYLErSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKG 211
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1310934957 661 EKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDRGHIIADG 705
Cdd:PRK13631 212 EHEMMQLILDAKANnKTVFVITHTMeHVLEVADEVIVMDKGKILKTG 258
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
502-723 |
1.42e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 100.62 E-value: 1.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 502 KPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDgidsaqihpsdlrRNFGYLPQDVTLFHGSVRD 581
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 582 NILFGTRQVTE--HQLIRAVQLSGvnlftDLE--SEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLD 657
Cdd:PTZ00243 740 NILFFDEEDAArlADAVRVSQLEA-----DLAqlGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 658 ARAEKQFMRS-MHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHIIADGP-KDKVLEKLNQGLMAGGK 723
Cdd:PTZ00243 815 AHVGERVVEEcFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSsADFMRTSLYATLAAELK 882
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
501-682 |
1.67e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.01 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsaqIHPSDLRRNFGYL-PQDVTLFHGSV 579
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLgHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 580 RDNILF-----GTRQVTEHQLIRAVQLSGVnlfTDLEsegldqqvgegGHSLSRGQRQTVALARAILNDPPVLLMDEPTA 654
Cdd:PRK13539 91 AENLEFwaaflGGEELDIAAALEAVGLAPL---AHLP-----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180
....*....|....*....|....*....
gi 1310934957 655 SLDARAEKQFMRSM-HNVSRDRTLLIITH 682
Cdd:PRK13539 157 ALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
504-701 |
1.81e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 93.73 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 504 VLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPS---DLR-RNFGYLPQdvtlFHGSV 579
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQ----FHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 580 RD-----NI----LFGTRQVTEHQLiRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMD 650
Cdd:PRK11629 100 PDftaleNVamplLIGKKKPAEINS-RALEM--------LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 651 EPTASLDAR-AEKQF-MRSMHNVSRDRTLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:PRK11629 171 EPTGNLDARnADSIFqLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
497-696 |
4.03e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.47 E-value: 4.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 497 YPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTLFH 576
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 577 GSVRDNILFGtrqvtehQLIRAVQLSGVNLFTDLESEGLDQQVGEGG-HSLSRGQRQTVALARAILNDPPVLLMDEPTAS 655
Cdd:PRK10247 95 DTVYDNLIFP-------WQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1310934957 656 LDARAEKQFMRSMHNVSRDRTL--LIITHKMHLLNLVDRIIVM 696
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIavLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
488-715 |
4.65e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 4.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSY-PGSekpvlhPFA--------LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGI----DSA 554
Cdd:PRK13643 2 IKFEKVNYTYqPNS------PFAsralfdidLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 555 QIHPSDLRRNFGYLPQ--DVTLFHGSVRDNILFGTRQV----TEHQLIRAVQLsgvnlftdlESEGLDQQVGEGG-HSLS 627
Cdd:PRK13643 76 QKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFgipkEKAEKIAAEKL---------EMVGLADEFWEKSpFELS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 628 RGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDRGHIIADG 705
Cdd:PRK13643 147 GGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMdDVADYADYVYLLEKGHIISCG 226
|
250
....*....|
gi 1310934957 706 PKDKVLEKLN 715
Cdd:PRK13643 227 TPSDVFQEVD 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
501-712 |
4.87e-21 |
|
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: 91.82 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGL--FKPSNGSLRYDGIDSAQIHPSDlRRNFGylpqdvtlfhgs 578
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLG------------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 579 vrdniLFGTRQvtehqliRAVQLSGVNLFTDLESegldqqVGEGghsLSRGQRQTVALARAILNDPPVLLMDEPTASLDA 658
Cdd:cd03217 79 -----IFLAFQ-------YPPEIPGVKNADFLRY------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 659 RAEK---QFMRSMHNvsRDRTLLIITHKMHLLNLV--DRIIVMDRGHIIADGPKDKVLE 712
Cdd:cd03217 138 DALRlvaEVINKLRE--EGKSVLIITHYQRLLDYIkpDRVHVLYDGRIVKSGDKELALE 194
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
488-710 |
5.12e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 94.80 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP------GSEKPVLHpfA-----LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQI 556
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVK--AvdgvsFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 557 HPSDLRRnfgyLPQDVTL-F---HGS------VRDNILFGTR---QVTEHQLIRAVQ-LsgvnlftdLESEGLDQQVGEG 622
Cdd:COG4608 86 SGRELRP----LRRRMQMvFqdpYASlnprmtVGDIIAEPLRihgLASKAERRERVAeL--------LELVGLRPEHADR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 623 -GHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKmhlLNLV----DRIIV 695
Cdd:COG4608 154 yPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELglTYLFISHD---LSVVrhisDRVAV 230
|
250
....*....|....*
gi 1310934957 696 MDRGHIIADGPKDKV 710
Cdd:COG4608 231 MYLGKIVEIAPRDEL 245
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
471-709 |
5.38e-21 |
|
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: 97.55 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 471 EFENKGHLVSKQRLMgKIEADDLSFSYPGsekpvlhpFALR-----IRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGS 545
Cdd:COG1245 326 EFEVHAPRREKEEET-LVEYPDLTKSYGG--------FSLEveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 546 LrydgidsaqihPSDLRrnFGYLPQDV-TLFHGSVRDnILFGTRQVT------EHQLIRAVQLSgvNLftdlesegLDQQ 618
Cdd:COG1245 397 V-----------DEDLK--ISYKPQYIsPDYDGTVEE-FLRSANTDDfgssyyKTEIIKPLGLE--KL--------LDKN 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 619 VGEgghsLSRGQRQTVALARAILNDPPVLLMDEPTASLD-------ARAEKQFMRsmhnvSRDRTLLIITHKMHLLNLV- 690
Cdd:COG1245 453 VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRFAE-----NRGKTAMVVDHDIYLIDYIs 523
|
250 260
....*....|....*....|....
gi 1310934957 691 DRIIVMD-----RGHiiADGPKDK 709
Cdd:COG1245 524 DRLMVFEgepgvHGH--ASGPMDM 545
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
488-684 |
7.67e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 7.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLL--VGLFKPS---NGSLRYDG--IDSAQIHPSD 560
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGhnIYSPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 LRRNFGYLPQDVTLFHGSVRDNILFGTR---QVTEHQLIRAVQ--LSGVNLFTDLESEGLDQQVGegghsLSRGQRQTVA 635
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGLRlkgIKDKQVLDEAVEksLKGASIWDEVKDRLHDSALG-----LSGGQQQRVC 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKM 684
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
485-701 |
8.01e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.52 E-value: 8.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRN 564
Cdd:PRK11650 1 MAGLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLF-HGSVRDNILFG--TRQVTEHQLIRAVQLSGvnlfTDLESEG-LDQQVGEgghsLSRGQRQTVALARAI 640
Cdd:PRK11650 78 IAMVFQNYALYpHMSVRENMAYGlkIRGMPKAEIEERVAEAA----RILELEPlLDRKPRE----LSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 641 LNDPPVLLMDEPTASLDA------RAE-KQFMRSMHNVSrdrtlLIITH-KMHLLNLVDRIIVMDRGHI 701
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAklrvqmRLEiQRLHRRLKTTS-----LYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
465-709 |
8.60e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 96.80 E-value: 8.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 465 IMTQEDEFENKGHLVSKQRLMgKIEADDLSFSYPGsekpvlhpFALR-----IRPGERIAIIGRNGSGKSTLAKLLVGLF 539
Cdd:PRK13409 319 IRPEPIEFEERPPRDESERET-LVEYPDLTKKLGD--------FSLEveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 540 KPSNGSLRydgidsaqihpSDLRrnFGYLPQDVTL-FHGSVRDNIlfgtRQVTE--------HQLIRAVQLsgvnlfTDL 610
Cdd:PRK13409 390 KPDEGEVD-----------PELK--ISYKPQYIKPdYDGTVEDLL----RSITDdlgssyykSEIIKPLQL------ERL 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 611 esegLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPTASLD-------ARAEKQFMRsmhnvSRDRTLLIITHK 683
Cdd:PRK13409 447 ----LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAE-----EREATALVVDHD 513
|
250 260 270
....*....|....*....|....*....|..
gi 1310934957 684 MHLLNLV-DRIIVMD-----RGHiiADGPKDK 709
Cdd:PRK13409 514 IYMIDYIsDRLMVFEgepgkHGH--ASGPMDM 543
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
485-706 |
1.17e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.44 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGS-------EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIH 557
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 558 PSD---LRRNFGYLPQD----VTLFHgSVRDNILFGTRQVTE-HQLIRAVQLSGVNLFTDLESEGLDQQVGegghSLSRG 629
Cdd:PRK10419 81 RAQrkaFRRDIQMVFQDsisaVNPRK-TVREIIREPLRHLLSlDKAERLARASEMLRAVDLDDSVLDKRPP----QLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 630 QRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSR--DRTLLIITHKMHLLN-LVDRIIVMDRGHIIADGP 706
Cdd:PRK10419 156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVErFCQRVMVMDNGQIVETQP 235
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
487-701 |
1.18e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 96.19 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:PRK10522 322 TLELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFhgsvrDNILFGTRQVTEHQLIRAVqlsgvnlftdLESEGLDQQVGEGGH-----SLSRGQRQTVALARAIL 641
Cdd:PRK10522 401 AVFTDFHLF-----DQLLGPEGKPANPALVEKW----------LERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 642 NDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITHKMHLLNLVDRIIVMDRGHI 701
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
510-720 |
3.04e-20 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.86 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAqiHPSDLRRNFGYLPQDVTLF-HGSVRDNILFGTR 588
Cdd:PRK11432 27 LTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRDICMVFQSYALFpHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 589 -----------QVTEhqLIRAVQLSGvnlftdLESEGLDQqvgegghsLSRGQRQTVALARAILNDPPVLLMDEPTASLD 657
Cdd:PRK11432 105 mlgvpkeerkqRVKE--ALELVDLAG------FEDRYVDQ--------ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 658 AraekQFMRSMHNVSRDR------TLLIITH-KMHLLNLVDRIIVMDRGHIIADGPKDKVLEKLNQGLMA 720
Cdd:PRK11432 169 A----NLRRSMREKIRELqqqfniTSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMA 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
485-708 |
6.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGkIEADDLSFSYPGS---EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGID-SAQIHPSD 560
Cdd:PRK13649 1 MG-INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 L---RRNFGYLPQ--DVTLFHGSVRDNILFGTRQVTEHQlIRAVQLSGVNLFTDLESEGL-DQQVGEgghsLSRGQRQTV 634
Cdd:PRK13649 80 IkqiRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALAREKLALVGISESLfEKNPFE----LSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDRGHIIADG-PKD 708
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGkPKD 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
485-711 |
6.68e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 89.57 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSA--QIHpSDLR 562
Cdd:PRK10895 1 MATLTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLH-ARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RNFGYLPQDVTLFHG-SVRDNIL--FGTRQ--VTEHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALA 637
Cdd:PRK10895 78 RGIGYLPQEASIFRRlSVYDNLMavLQIRDdlSAEQREDRANEL--------MEEFHIEHLRDSMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 638 RAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVsRDRTL--LIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLgvLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
491-712 |
7.17e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 7.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 491 DDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQ 570
Cdd:PRK10575 15 RNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 571 DVTLFHG-SVRDNILFGT----------RQVTEHQLIRAVQLSGVnlfTDLESEGLDqqvgegghSLSRGQRQTVALARA 639
Cdd:PRK10575 93 QLPAAEGmTVRELVAIGRypwhgalgrfGAADREKVEEAISLVGL---KPLAHRLVD--------SLSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIIThKMHLLNLV----DRIIVMDRGHIIADGPKDKVLE 712
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
488-668 |
9.67e-20 |
|
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: 87.80 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdlrrnfgy 567
Cdd:TIGR01189 1 LAARNLACSR--GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 lPQDVTLFHG---------SVRDNI-----LFGTRQVTEHQLIRAVQLSGvnlFTDLESegldqqvgeggHSLSRGQRQT 633
Cdd:TIGR01189 71 -PHENILYLGhlpglkpelSALENLhfwaaIHGGAQRTIEDALAAVGLTG---FEDLPA-----------AQLSAGQQRR 135
|
170 180 190
....*....|....*....|....*....|....*
gi 1310934957 634 VALARAILNDPPVLLMDEPTASLDARAEKQFMRSM 668
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
487-712 |
1.13e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSY-PGS--EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPS---- 559
Cdd:PRK13651 2 QIKVKNIVKIFnKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 560 --------------------DLRRNFGYLPQ--DVTLFHGSVRDNILFGTRQV---TEHQLIRAVQLsgvnlftdLESEG 614
Cdd:PRK13651 82 kvleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMgvsKEEAKKRAAKY--------IELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 615 LDQQ-VGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNV-SRDRTLLIITHKM-HLLNLVD 691
Cdd:PRK13651 154 LDESyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTK 233
|
250 260
....*....|....*....|.
gi 1310934957 692 RIIVMDRGHIIADGPKDKVLE 712
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILS 254
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
493-702 |
1.13e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 88.48 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 493 LSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSNGSLRYD-GIDSAQIHPSDLRRNFGYLPQ- 570
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGGTTSGQiLFNGQPRKPDQFQKCVAYVRQd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 571 DVTLFHGSVRDNILFgtrqvtehqlirAVQLSGVNLFTDLESEGLDQQVGEG-------GHS----LSRGQRQTVALARA 639
Cdd:cd03234 90 DILLPGLTVRETLTY------------TAILRLPRKSSDAIRKKRVEDVLLRdlaltriGGNlvkgISGGERRRVSIAVQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNVS-RDRTLLIITHK--MHLLNLVDRIIVMDRGHII 702
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIHQprSDLFRLFDRILLLSSGEIV 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
502-703 |
1.14e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 502 KPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-LRRNFGYLPQD---VTLFHG 577
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPEDrkgEGLVLD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 578 -SVRDNILFGT-RQVTEHQLIRAVQLSGV--NLFTDLE--SEGLDQQVGegghSLSRGQRQTVALARAILNDPPVLLMDE 651
Cdd:COG1129 345 lSIRENITLASlDRLSRGGLLDRRRERALaeEYIKRLRikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 652 PTASLD--ARAE-KQFMRSMhnVSRDRTLLIITHKMH-LLNLVDRIIVMDRGHIIA 703
Cdd:COG1129 421 PTRGIDvgAKAEiYRLIREL--AAEGKAVIVISSELPeLLGLSDRILVMREGRIVG 474
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
512-697 |
1.40e-19 |
|
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: 88.62 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAqihpsdlrrnfgYLPQDVTL-FHGSVRDNILFGTRQV 590
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------------YKPQYIKAdYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 591 TEH-----QLIRAVQLSGVnlftdlesegLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPTASLD-------A 658
Cdd:cd03237 90 YTHpyfktEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrlmaS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1310934957 659 RAEKQFMrsMHNvsrDRTLLIITHKMHLLNLV-DRIIVMD 697
Cdd:cd03237 156 KVIRRFA--ENN---EKTAFVVEHDIIMIDYLaDRLIVFE 190
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
510-712 |
1.79e-19 |
|
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: 87.98 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsaqihPSDLRRNFGYLPQ----------DV--TLFHG 577
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS-----PGKGWRHIGYVPQrhefawdfpiSVahTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 578 SVRDNILFGTRQVTEHQLIRAVqLSGVNLftdleSEGLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPTASLD 657
Cdd:TIGR03771 76 RTGHIGWLRRPCVADFAAVRDA-LRRVGL-----TELADRPVGE----LSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 658 ARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDrGHIIADGPKDKVLE 712
Cdd:TIGR03771 146 MPTQELLTELFIELAGAgTAILMTTHDLaQAMATCDRVVLLN-GRVIADGTPQQLQD 201
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
488-701 |
2.03e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEKpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD---LRRN 564
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLFHG-SVRDN-----ILFGTrqvTEHQLIRAVQLSgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALAR 638
Cdd:PRK10908 81 IGMIFQDHHLLMDrTVYDNvaiplIIAGA---SGDDIRRRVSAA-------LDKVGLLDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSR-DRTLLIITHKMHLLNLVD-RIIVMDRGHI 701
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
488-682 |
2.14e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.22 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQihPSDLR----R 563
Cdd:PRK11248 2 LQISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAERgvvfQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 564 NFGYLPQDvtlfhgSVRDNILFG---------TRQVTEHQLIRAVQLSGVnlftdlESEGLDQqvgegghsLSRGQRQTV 634
Cdd:PRK11248 78 NEGLLPWR------NVQDNVAFGlqlagvekmQRLEIAHQMLKKVGLEGA------EKRYIWQ--------LSGGQRQRV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITH 682
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtgKQVLLITH 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
492-711 |
2.34e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 88.53 E-value: 2.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 492 DLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDSAQIHPSDLRRNFGYLP 569
Cdd:PRK13638 6 DLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 QD--VTLFHGSVRDNILFGTRQ--VTEHQLIRAVQlsgvNLFTDLESEGLDQQVGEgghSLSRGQRQTVALARAILNDPP 645
Cdd:PRK13638 84 QDpeQQIFYTDIDSDIAFSLRNlgVPEAEITRRVD----EALTLVDAQHFRHQPIQ---CLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHN-VSRDRTLLIITHKMHLL-NLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
487-684 |
2.73e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.30 E-value: 2.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYpGSEKPVlHPFALRIRPGERIAIIGRNGSGKSTLAKL------LVGLFKpSNGSLRYDG--IDSAQIHP 558
Cdd:PRK14243 10 VLRTENLNVYY-GSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCfnrlndLIPGFR-VEGKVTFHGknLYAPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 559 SDLRRNFGYLPQDVTLFHGSVRDNILFGTR---------QVTEHQLIRAVqlsgvnlftdLESEGLDQqVGEGGHSLSRG 629
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGARingykgdmdELVERSLRQAA----------LWDEVKDK-LKQSGLSLSGG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 630 QRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKM 684
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
487-711 |
3.16e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD------ 560
Cdd:PRK10619 5 KLNVIDLHKRY--GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 -------LRRNFGYLPQDVTLF-HGSVRDNILFGTRQV----TEHQLIRAVQLsgvnlftdLESEGLDQQV-GEGGHSLS 627
Cdd:PRK10619 83 dknqlrlLRTRLTMVFQHFNLWsHMTVLENVMEAPIQVlglsKQEARERAVKY--------LAKVGIDERAqGKYPVHLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 628 RGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLL-NLVDRIIVMDRGHIIADG 705
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFArHVSSHVIFLHQGKIEEEG 234
|
....*.
gi 1310934957 706 PKDKVL 711
Cdd:PRK10619 235 APEQLF 240
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
488-705 |
3.84e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.38 E-value: 3.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRN-FG 566
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVTLFHG-SVRDNILFG---TRQV--------TEHQLIRAVQLSGVNLFTDlesegLDQQVGEgghsLSRGQRQTV 634
Cdd:PRK09700 84 IIYQELSVIDElTVLENLYIGrhlTKKVcgvniidwREMRVRAAMMLLRVGLKVD-----LDEKVAN----LSISHKQML 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 635 ALARAILNDPPVLLMDEPTASL-DARAEKQFMrSMHNVSRDRTLLI-ITHKM-HLLNLVDRIIVMDRGHIIADG 705
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLtNKEVDYLFL-IMNQLRKEGTAIVyISHKLaEIRRICDRYTVMKDGSSVCSG 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
488-708 |
4.20e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.38 E-value: 4.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpGSEKpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSL-----RYD---GIDSAQIhpS 559
Cdd:PRK11124 3 IQLNGINCFY-GAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDfskTPSDKAI--R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 560 DLRRNFGYLPQDVTLF-HGSVRDNILFGTRQV---TEHQLI-RAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTV 634
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWpHLTVQQNLIEAPCRVlglSKDQALaRAEKL--------LERLRLKPYADRFPLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR-TLLIITHKMHLLNLV-DRIIVMDRGHIIADGPKD 708
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKTaSRVVYMENGHIVEQGDAS 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
495-699 |
5.64e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 86.23 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 495 FSYpGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGI----DSAQIHPSDLRRNFGYLPQ 570
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnesePSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 571 DVTLFHGSVRDNILFGTrQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMD 650
Cdd:cd03290 87 KPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 651 EPTASLDARAEKQFMRS-MHNVSRD--RTLLIITHKMHLLNLVDRIIVMDRG 699
Cdd:cd03290 166 DPFSALDIHLSDHLMQEgILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-712 |
7.05e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 90.51 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPG---------SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSNGSLRYDGIDSAQIHP 558
Cdd:COG4172 276 LEARDLKVWFPIkrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 559 SD---LRRNFGYLPQDVtlfHGS------VRDNILFGTR----QVTEHQ-LIRAVQLsgvnlftdLESEGLDQQVGEG-G 623
Cdd:COG4172 355 RAlrpLRRRMQVVFQDP---FGSlsprmtVGQIIAEGLRvhgpGLSAAErRARVAEA--------LEEVGLDPAARHRyP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 624 HSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTL--LIITHKMHLLN-LVDRIIVMDRGH 700
Cdd:COG4172 424 HEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLayLFISHDLAVVRaLAHRVMVMKDGK 503
|
250
....*....|..
gi 1310934957 701 IIADGPKDKVLE 712
Cdd:COG4172 504 VVEQGPTEQVFD 515
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
504-711 |
7.70e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 87.19 E-value: 7.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 504 VLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPS--------NGSLRYDGIDSAQIHPSDLRRNFGYLPQDVT-L 574
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 FHGSVRDNILFG--------------TRQVTEHQLIRAvqlsgvnlftdleseGLDQQVGEGGHSLSRGQRQTVALARAI 640
Cdd:PRK13547 96 FAFSAREIVLLGrypharragalthrDGEIAWQALALA---------------GATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 641 ---------LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTL--LIITHKMHL-LNLVDRIIVMDRGHIIADGPKD 708
Cdd:PRK13547 161 aqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgvLAIVHDPNLaARHADRIAMLADGAIVAHGAPA 240
|
...
gi 1310934957 709 KVL 711
Cdd:PRK13547 241 DVL 243
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
509-711 |
8.22e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.32 E-value: 8.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 509 ALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL----RRNFGYLPQDVTLF-HGSVRDNI 583
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 LFGtrqvtehqliraVQLSGVNLfTDLESEGLD--QQVGEGGHS------LSRGQRQTVALARAILNDPPVLLMDEPTAS 655
Cdd:PRK10070 128 AFG------------MELAGINA-EERREKALDalRQVGLENYAhsypdeLSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 656 LDA--RAEKQFMRSMHNVSRDRTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK10070 195 LDPliRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
503-699 |
2.22e-18 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 84.79 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 503 PVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYD----GIDSAQIHPSD---LRRN-FGYLPQdvtl 574
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQASPREilaLRRRtIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 fhgsvrdnilF-------GTRQVTEHQLIRAvqlsGVNlftdlESEGLDQ--------QVGEGGHSL-----SRGQRQTV 634
Cdd:COG4778 101 ----------FlrviprvSALDVVAEPLLER----GVD-----REEARARarellarlNLPERLWDLppatfSGGEQQRV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDArAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLV-DRIIVMDRG 699
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDA-ANRAVVVELIEEAKARgtAIIGIFHDEEVREAVaDRVVDVTPF 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-712 |
2.22e-18 |
|
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: 88.97 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLS--FSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSN-----GSLRYDGIDSAQIHPSD 560
Cdd:COG4172 7 LSVEDLSvaFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL-PDPaahpsGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 LRRnfgylpqdvtlfhgsVRDN---ILF-------------GtRQVTE----HQLI-------RAVQLsgvnlftdLESE 613
Cdd:COG4172 86 LRR---------------IRGNriaMIFqepmtslnplhtiG-KQIAEvlrlHRGLsgaaaraRALEL--------LERV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 614 GLD---QQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKmhlLN 688
Cdd:COG4172 142 GIPdpeRRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITHD---LG 218
|
250 260
....*....|....*....|....*...
gi 1310934957 689 LV----DRIIVMDRGHIIADGPKDKVLE 712
Cdd:COG4172 219 VVrrfaDRVAVMRQGEIVEQGPTAELFA 246
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
507-711 |
2.37e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 85.61 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 507 PFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRydgIDSAQIHPSDlrrnFGYLPQdvtlfhgsvRDNILF- 585
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL---IDDHPLHFGD----YSYRSQ---------RIRMIFq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 586 -GTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVGEG--------------GHSLSRGQRQTVALARAILNDPPVLLMD 650
Cdd:PRK15112 95 dPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETlrqvgllpdhasyyPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 651 EPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHL---LNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLgmmKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
505-705 |
3.73e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.06 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 505 LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFK-----PSNGSLRYDGIDSAQIHPSDLRRN---FGYLPQDVTLFH 576
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksaGSHIELLGRTVQREGRLARDIRKSranTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 577 G-SVRDNILFGT-----------RQVTEHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDP 644
Cdd:PRK09984 100 RlSVLENVLIGAlgstpfwrtcfSWFTREQKQRALQA--------LTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKM-HLLNLVDRIIVMDRGHIIADG 705
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVdYALRYCERIVALRQGHVFYDG 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
486-705 |
8.04e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 8.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 486 GKIEADDLSFSYPGS---EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNG-SLRYDGIDSAQIHP--- 558
Cdd:PRK13645 5 KDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKKike 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 559 -SDLRRNFGYLPQ--DVTLFHGSVRDNILFGTRQVTEH---------QLIRAVQLSgvnlftdleseglDQQVGEGGHSL 626
Cdd:PRK13645 85 vKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENkqeaykkvpELLKLVQLP-------------EDYVKRSPFEL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 627 SRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD--RTLLIITHKM-HLLNLVDRIIVMDRGHIIA 703
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMdQVLRIADEVIVMHEGKVIS 231
|
..
gi 1310934957 704 DG 705
Cdd:PRK13645 232 IG 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
469-715 |
9.87e-18 |
|
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: 88.53 E-value: 9.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 469 EDEFENKGHLVSKQRLMGKIEADDLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRY 548
Cdd:TIGR01257 1919 DDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV 1998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 549 DGiDSAQIHPSDLRRNFGYLPQDVTLfhgsvrDNILFGTRQVTEHQLIRAVQLSGVNLFTD--LESEGLDQQVGEGGHSL 626
Cdd:TIGR01257 1999 AG-KSILTNISDVHQNMGYCPQFDAI------DDLLTGREHLYLYARLRGVPAEEIEKVANwsIQSLGLSLYADRLAGTY 2071
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 627 SRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLN-LVDRIIVMDRG----- 699
Cdd:TIGR01257 2072 SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREgRAVVLTSHSMEECEaLCTRLAIMVKGafqcl 2151
|
250 260 270
....*....|....*....|....*....|..
gi 1310934957 700 ----HI---IADG---------PKDKVLEKLN 715
Cdd:TIGR01257 2152 gtiqHLkskFGDGyivtmkiksPKDDLLPDLN 2183
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
483-685 |
1.69e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 83.16 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 483 RLMGKIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLvGLFKPSNGSLRYDG--------IDSA 554
Cdd:PRK14258 3 KLIPAIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGrveffnqnIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 555 QIHPSDLRRNFGYLPQDVTLFHGSVRDNILFGTRQVTEHQlirAVQLSGVnLFTDLESEGLDQQVGEGGHS----LSRGQ 630
Cdd:PRK14258 80 RVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRP---KLEIDDI-VESALKDADLWDEIKHKIHKsaldLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVS--RDRTLLIITHKMH 685
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLH 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
501-668 |
1.85e-17 |
|
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: 81.39 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSdLRRNFGYLP-QDVTLFHGSV 579
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLGhAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 580 RDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESegldqqvgeggHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDAR 659
Cdd:cd03231 91 LENLRFWHADHSDEQVEEALARVGLNGFEDRPV-----------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
....*....
gi 1310934957 660 AEKQFMRSM 668
Cdd:cd03231 160 GVARFAEAM 168
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
510-701 |
2.25e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 84.70 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDlrRNFGYLPQDVTLF-HGSVRDNILFGtr 588
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--RGVGMVFQSYALYpHLSVAENMSFG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 589 qvtehqliraVQLSGVNlftdlESEgLDQQVGEG------GH-------SLSRGQRQTVALARAILNDPPVLLMDEPTAS 655
Cdd:PRK11000 100 ----------LKLAGAK-----KEE-INQRVNQVaevlqlAHlldrkpkALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 656 LDARAEKQfMRSmhNVSR-----DRTLLIITH-KMHLLNLVDRIIVMDRGHI 701
Cdd:PRK11000 164 LDAALRVQ-MRI--EISRlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRV 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
487-714 |
8.00e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 81.19 E-value: 8.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 487 KIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFG 566
Cdd:PRK10253 7 RLRGEQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 567 YLPQDVT----------LFHGSVRDNILFGT-RQVTEHQLIRAVQLSGVnlfTDLESEGLDqqvgegghSLSRGQRQTVA 635
Cdd:PRK10253 85 LLAQNATtpgditvqelVARGRYPHQPLFTRwRKEDEEAVTKAMQATGI---THLADQSVD--------TLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 636 LARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMH-LLNLVDRIIVMDRGHIIADG-PKDKVL 711
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGaPKEIVT 233
|
...
gi 1310934957 712 EKL 714
Cdd:PRK10253 234 AEL 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
519-705 |
9.41e-17 |
|
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: 85.07 E-value: 9.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 519 AIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDsAQIHPSDLRRNFGYLPQDvtlfhgsvrdNILFGTRQVTEHQLIRA 598
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD-IETNLDAVRQSLGMCPQH----------NILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 599 vQLSG-------VNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNV 671
Cdd:TIGR01257 1029 -QLKGrsweeaqLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107
|
170 180 190
....*....|....*....|....*....|....*
gi 1310934957 672 SRDRTLLIITHKMHLLNLV-DRIIVMDRGHIIADG 705
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLgDRIAIISQGRLYCSG 1142
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
437-657 |
1.12e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 83.79 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 437 RAVAPMAQLANLMTR-------ANQTASALRQLDQIMTQED------------EFENKGHlvskqRLMgkIEADDLSFSY 497
Cdd:PRK15064 257 KKKAQIAELQSFVSRfsanaskAKQATSRAKQIDKIKLEEVkpssrqnpfirfEQDKKLH-----RNA--LEVENLTKGF 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 498 PGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDgiDSAQIhpsdlrrnfGYLPQD------ 571
Cdd:PRK15064 330 DN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--ENANI---------GYYAQDhaydfe 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 --VTLFhgsvrDNILFGTRQVTEHQLIRAVQlsGVNLFTdleseglDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLM 649
Cdd:PRK15064 397 ndLTLF-----DWMSQWRQEGDDEQAVRGTL--GRLLFS-------QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
....*...
gi 1310934957 650 DEPTASLD 657
Cdd:PRK15064 463 DEPTNHMD 470
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
501-706 |
1.75e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLfkpSNGSLRYDG---IDSAQIHPSDLRRNFGYLPQDvTLFHG 577
Cdd:TIGR00955 37 RKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGsvlLNGMPIDAKEMRAISAYVQQD-DLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 578 S--VRDNILFGT-----RQVTEHQLIRAVQlsgvNLFTDLeseGL----DQQVGEGGH--SLSRGQRQTVALARAILNDP 644
Cdd:TIGR00955 113 TltVREHLMFQAhlrmpRRVTKKEKRERVD----EVLQAL---GLrkcaNTRIGVPGRvkGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIIT-HK--MHLLNLVDRIIVMDRGHIIADGP 706
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQpsSELFELFDKIILMAEGRVAYLGS 250
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
493-702 |
2.70e-16 |
|
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: 82.68 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 493 LSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRY-DGIdsaqihpsdlrrNFGYLPQ- 570
Cdd:TIGR03719 10 VSKVVPP-KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI------------KVGYLPQe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 571 ---DVTLfhgSVRDNILFGTRQVtEHQLIRAVQLSgvNLFTDlESEGLDQQVGE-----------GGHS----------- 625
Cdd:TIGR03719 77 pqlDPTK---TVRENVEEGVAEI-KDALDRFNEIS--AKYAE-PDADFDKLAAEqaelqeiidaaDAWDldsqleiamda 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 626 ------------LSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSrdRTLLIITHKMHLL-NLVDR 692
Cdd:TIGR03719 150 lrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP--GTVVAVTHDRYFLdNVAGW 227
|
250
....*....|
gi 1310934957 693 IIVMDRGHII 702
Cdd:TIGR03719 228 ILELDRGRGI 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
489-723 |
3.30e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFSyPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRN-FGY 567
Cdd:COG3845 259 EVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDvTLFHG-----SVRDNILFGT--------------RQVTEH--QLIRAvqlsgvnlFtDLESEGLDQQVGegghSL 626
Cdd:COG3845 338 IPED-RLGRGlvpdmSVAENLILGRyrrppfsrggfldrKAIRAFaeELIEE--------F-DVRTPGPDTPAR----SL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 627 SRGQRQTVALARAILNDPPVLLMDEPTASLDARAekqfMRSMHNV---SRDR--TLLIITHKM-HLLNLVDRIIVMDRGH 700
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGA----IEFIHQRlleLRDAgaAVLLISEDLdEILALSDRIAVMYEGR 479
|
250 260
....*....|....*....|....
gi 1310934957 701 IIADGPKDKV-LEKLNQgLMAGGK 723
Cdd:COG3845 480 IVGEVPAAEAtREEIGL-LMAGVK 502
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
488-710 |
4.06e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 80.01 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYP---GSEKPVLHPFAL-----RIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPS 559
Cdd:PRK11308 6 LQAIDLKKHYPvkrGLFKPERLVKALdgvsfTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 560 DLRRnfgyLPQDVTL-F---HGSV--RDNIlfgtRQVTEHQLIravqlsgVNlfTDLESEGLDQQVGE-----G------ 622
Cdd:PRK11308 86 AQKL----LRQKIQIvFqnpYGSLnpRKKV----GQILEEPLL-------IN--TSLSAAERREKALAmmakvGlrpehy 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 623 ---GHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTL--LIITHKMHLLNLV-DRIIVM 696
Cdd:PRK11308 149 dryPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLsyVFISHDLSVVEHIaDEVMVM 228
|
250
....*....|....
gi 1310934957 697 DRGHIIADGPKDKV 710
Cdd:PRK11308 229 YLGRCVEKGTKEQI 242
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
485-711 |
6.18e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.03 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKL---LVGLFKPS--NGSLRYDGIDSAQIHPS 559
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVE--VLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEArvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 560 DLRRNFGY---LPQDVTLFhgSVRDNILFG---TRQV-TEHQLIRAVQ--LSGVNLFTDLESEgLDQQVGegghSLSRGQ 630
Cdd:PRK14247 79 ELRRRVQMvfqIPNPIPNL--SIFENVALGlklNRLVkSKKELQERVRwaLEKAQLWDEVKDR-LDAPAG----KLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITH-KMHLLNLVDRIIVMDRGHIIADGPKDK 709
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
..
gi 1310934957 710 VL 711
Cdd:PRK14247 232 VF 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
501-712 |
1.02e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.41 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGL--FKPSNGSLRYDGID----------------SAQiHPSDLR 562
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDilelspderaragiflAFQ-YPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 ----RNF--------GYLPQDVTLFHGSVRDNilfgtrqvtehqliravqLSGVNLFTDLesegLDQQVGEGghsLSRGQ 630
Cdd:COG0396 91 gvsvSNFlrtalnarRGEELSAREFLKLLKEK------------------MKELGLDEDF----LDRYVNEG---FSGGE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEK---QFMRSMHnvSRDRTLLIITHKMHLLNLV--DRIIVMDRGHIIADG 705
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRivaEGVNKLR--SPDRGILIITHYQRILDYIkpDFVHVLVDGRIVKSG 223
|
....*..
gi 1310934957 706 PKDKVLE 712
Cdd:COG0396 224 GKELALE 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
510-703 |
1.10e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.32 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsAQIHPSDL--RRNFGYLPQDVTLFhG--SVRDNI-- 583
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG---QPVDAGDIatRRRVGYMSQAFSLY-GelTVRQNLel 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 ---LFG--TRQVTE--HQLIRAVQLSGVnlftdlesegLDQQVGegghSLSRGQRQTVALARAILNDPPVLLMDEPTASL 656
Cdd:NF033858 363 harLFHlpAAEIAArvAEMLERFDLADV----------ADALPD----SLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1310934957 657 DARAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDRGHIIA 703
Cdd:NF033858 429 DPVARDMFWRLLIELSREDgvTIFISTHFMNEAERCDRISLMHAGRVLA 477
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
505-711 |
1.21e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 77.19 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 505 LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVTL------FHG- 577
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPpfampvFQYl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 578 --SVRDNILFGTRQVTEHQLIRAVQLsgvnlfTDLESEGLDQqvgegghsLSRGQRQTVALARAILN-------DPPVLL 648
Cdd:COG4138 91 alHQPAGASSEAVEQLLAQLAEALGL------EDKLSRPLTQ--------LSGGEWQRVRLAAVLLQvwptinpEGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 649 MDEPTASLDARAEK---QFMRSMHnvSRDRTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:COG4138 157 LDEPMNSLDVAQQAaldRLLRELC--QQGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
488-697 |
1.52e-15 |
|
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: 74.88 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLrydgidsaqIHPSDlrRNFGY 567
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEG--EDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQDVTLFHGSVRDNILFGTRQVtehqliravqlsgvnlftdlesegldqqvgegghsLSRGQRQTVALARAILNDPPVL 647
Cdd:cd03223 69 LPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHnvSRDRTLLIITHKMHLLNLVDRIIVMD 697
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLK--ELGITVISVGHRPSLWKFHDRVLDLD 161
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
420-696 |
1.84e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 80.84 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 420 DNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHlVSKQRLMGKIEADDLSFSYPG 499
Cdd:PTZ00265 316 NNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDD-GKKLKDIKKIQFKNVRFHYDT 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 500 SEK-PVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDgiDSAQIHPSDL---RRNFGYLPQDVTLF 575
Cdd:PTZ00265 395 RKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLkwwRSKIGVVSQDPLLF 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 576 HGSVRDNILFG------------------------------------------TRQVTEHQLIRA------------VQL 601
Cdd:PTZ00265 473 SNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmSNTTDSNELIEMrknyqtikdsevVDV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 602 SGVNLFTDLES---EGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNV--SRDRT 676
Cdd:PTZ00265 553 SKKVLIHDFVSalpDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRI 632
|
330 340
....*....|....*....|
gi 1310934957 677 LLIITHKMHLLNLVDRIIVM 696
Cdd:PTZ00265 633 TIIIAHRLSTIRYANTIFVL 652
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
493-712 |
2.36e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 79.99 E-value: 2.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 493 LSFSYpgseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG---IDSAQIHPsdlrrnfgylP 569
Cdd:PRK11147 11 LSFSD----APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdliVARLQQDP----------P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 QDVTlfhGSVRDNILFGTRQVTE-----HQLIRAV----------QLSGVNlfTDLESEGLDQ----------QVGEGGH 624
Cdd:PRK11147 77 RNVE---GTVYDFVAEGIEEQAEylkryHDISHLVetdpseknlnELAKLQ--EQLDHHNLWQlenrinevlaQLGLDPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 625 ----SLSRGQRQTVALARAILNDPPVLLMDEPTASLDARA----E---KQFMRSMHNVSRDRTLLiitHKMhllnlVDRI 693
Cdd:PRK11147 152 aalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiewlEgflKTFQGSIIFISHDRSFI---RNM-----ATRI 223
|
250 260
....*....|....*....|
gi 1310934957 694 IVMDRGHIIA-DGPKDKVLE 712
Cdd:PRK11147 224 VDLDRGKLVSyPGNYDQYLL 243
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
500-702 |
3.22e-15 |
|
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: 74.99 E-value: 3.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 500 SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPS---NGSLRYDGIDSAQIHpSDLRRNFGYLPQ-DVTLF 575
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKYPGEIIYVSEeDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 576 HGSVRDNILFGTRqVTEHQLIRAVqlSGvnlftdlesegldqqvgegghslsrGQRQTVALARAILNDPPVLLMDEPTAS 655
Cdd:cd03233 97 TLTVRETLDFALR-CKGNEFVRGI--SG-------------------------GERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 656 LDARAEKQF---MRSMHNVSRDRTLLIITH-KMHLLNLVDRIIVMDRGHII 702
Cdd:cd03233 149 LDSSTALEIlkcIRTMADVLKTTTFVSLYQaSDEIYDLFDKVLVLYEGRQI 199
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
489-703 |
3.45e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 489 EADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG-----------IDS--AQ 555
Cdd:PRK11288 6 SFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfasttaaLAAgvAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 556 IHpsdlrrnfgylpQDVTLF-HGSVRDNILFG---TRQ--VTEHQLIRAVQLSgvnlftdLESEGLDQQVGEGGHSLSRG 629
Cdd:PRK11288 84 IY------------QELHLVpEMTVAENLYLGqlpHKGgiVNRRLLNYEAREQ-------LEHLGVDIDPDTPLKYLSIG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 630 QRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDRGHIIA 703
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMeEIFALCDAITVFKDGRYVA 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
488-694 |
5.25e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 5.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPsDLRRNFGY 567
Cdd:PRK13538 2 LEARNLACER--DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 568 LPQdvtlfHGSVRD------NILF---GTRQVTEHQLIRAvqLSGVNL--FTDLESegldqqvgeggHSLSRGQRQTVAL 636
Cdd:PRK13538 79 LGH-----QPGIKTeltaleNLRFyqrLHGPGDDEALWEA--LAQVGLagFEDVPV-----------RQLSAGQQRRVAL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 637 ARAILNDPPVLLMDEPTASLDARAEKQFMRSM-HNVSRDRTLLIITHkmHLLNLVDRII 694
Cdd:PRK13538 141 ARLWLTRAPLWILDEPFTAIDKQGVARLEALLaQHAEQGGMVILTTH--QDLPVASDKV 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
492-708 |
7.42e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 7.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 492 DLSFSYPGsekpvlhpfalrirpGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIhpsdLRRNF-GYLPQ 570
Cdd:PRK15056 25 DASFTVPG---------------GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNLvAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 571 DVTL---FHGSVRDNILFGT-------RQVTEH-QLIRAVQLSGVNLftdleSEGLDQQVGEgghsLSRGQRQTVALARA 639
Cdd:PRK15056 86 SEEVdwsFPVLVEDVVMMGRyghmgwlRRAKKRdRQIVTAALARVDM-----VEFRHRQIGE----LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 640 ILNDPPVLLMDEPTASLDARAEKQFMRSMHNVsRD--RTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKD 708
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
488-717 |
1.37e-14 |
|
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: 77.15 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGL--FKPSNGSLRY----------------- 548
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 549 ----------------DGIDSAQIHPSDLRRNFGYLPQDVTLFHG--SVRDNILFGTRQV---TEHQLIRAVQLsgvnlf 607
Cdd:TIGR03269 79 gepcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEIgyeGKEAVGRAVDL------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 608 tdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMH 685
Cdd:TIGR03269 153 --IEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPE 230
|
250 260 270
....*....|....*....|....*....|...
gi 1310934957 686 LL-NLVDRIIVMDRGHIIADGPKDKVLEKLNQG 717
Cdd:TIGR03269 231 VIeDLSDKAIWLENGEIKEEGTPDEVVAVFMEG 263
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
504-711 |
1.51e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 504 VLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-LRRNFGYLPQDVTLF-HGSVRD 581
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGRRVFsRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 582 NI----LFGTRQVTEHQLIRAVQlsgvnLFTDLEsEGLDQQVGegghSLSRGQRQTVALARAILNDPPVLLMDEPTASLD 657
Cdd:PRK11614 100 NLamggFFAERDQFQERIKWVYE-----LFPRLH-ERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 658 ARAEKQFMRSMHNVSRD--RTLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK11614 170 PIIIQQIFDTIEQLREQgmTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
500-713 |
1.52e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 74.31 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 500 SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFK------PSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVT 573
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 574 LF-HGSVRDNILF-----GTRQVTEHQLIRAVQLSGVNLFTDLESegldqQVGEGGHSLSRGQRQTVALARAILNDPPVL 647
Cdd:PRK14246 101 PFpHLSIYDNIAYplkshGIKEKREIKKIVEECLRKVGLWKEVYD-----RLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 648 LMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHK-MHLLNLVDRIIVMDRGHIIADG--------PKDKVLEK 713
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNpQQVARVADYVAFLYNGELVEWGssneiftsPKNELTEK 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
482-711 |
1.86e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.36 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 482 QRLMGKIEADDLSFSYPG----------SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGsLRYDG- 550
Cdd:PRK14271 4 ERLGGQSGAADVDAAAPAmaavnltlgfAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 551 --IDSAQIHPS----DLRRNFGYLPQDVTLFHGSVRDNILFGTRQvteHQLIRAVQLSGVNLFTDLES---EGLDQQVGE 621
Cdd:PRK14271 83 vlLGGRSIFNYrdvlEFRRRVGMLFQRPNPFPMSIMDNVLAGVRA---HKLVPRKEFRGVAQARLTEVglwDAVKDRLSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 622 GGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKM-HLLNLVDRIIVMDRGH 700
Cdd:PRK14271 160 SPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGR 239
|
250
....*....|.
gi 1310934957 701 IIADGPKDKVL 711
Cdd:PRK14271 240 LVEEGPTEQLF 250
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
510-692 |
2.40e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHP---SDLR-RNFGYLPQDVTLFHG-SVRDNI- 583
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSFMLIPTlNALENVe 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 ----LFGTRQVTEHQliRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDAR 659
Cdd:PRK10584 111 lpalLRGESSRQSRN--GAKAL--------LEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190
....*....|....*....|....*....|....*
gi 1310934957 660 AEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVDR 692
Cdd:PRK10584 181 TGDKIADLLFSLNREHgtTLILVTHDLQLAARCDR 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
512-711 |
3.49e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.04 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG-----IDSAQIHPSDLRR----NFGYLPQDVtlfhgsvRD- 581
Cdd:PRK11701 29 LYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRllrtEWGFVHQHP-------RDg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 582 ---------NIlfGTRqvtehqlIRAVqlsGVNLFTDLESEGLD--QQV-------GEGGHSLSRGQRQTVALARAILND 643
Cdd:PRK11701 102 lrmqvsaggNI--GER-------LMAV---GARHYGDIRATAGDwlERVeidaariDDLPTTFSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 644 PPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTL--LIITHKMHLLNLV-DRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLavVIVTHDLAVARLLaHRLLVMKQGRVVESGLTDQVL 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
500-711 |
5.41e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 500 SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSNGSLRYDGIDSAQIHPSDLRRNFGYLPQDVT------ 573
Cdd:PRK03695 7 AVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTppfamp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 574 LFHG---SVRDNILFGTRQVTEHQLIRAVQLsgvnlfTDLESEGLDQqvgegghsLSRGQRQTVALARAILNDPP----- 645
Cdd:PRK03695 86 VFQYltlHQPDKTRTEAVASALNEVAEALGL------DDKLGRSVNQ--------LSGGEWQRVRLAAVVLQVWPdinpa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 646 --VLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK03695 152 gqLLLLDEPMNSLDVAQQAALDRLLSELCQQgIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
176-436 |
1.74e-13 |
|
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: 71.52 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLW--VLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYK 253
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPETQAlnVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 254 AIGIPLENRSA-SVGG-MARQLGEFDSIREILTSaTITTLVDLPFALLFVLIIYLVAG-DLALIPLVASLIIIGYTLIVQ 330
Cdd:pfam00664 84 ILRQPMSFFDTnSVGElLSRLTNDTSKIRDGLGE-KLGLLFQSLATIVGGIIVMFYYGwKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 331 PRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIghtANWQLRSKKLSNSVA---NVANFVVQLTV 407
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKAL---EEALKAGIKKAVANGlsfGITQFIGYLSY 239
|
250 260
....*....|....*....|....*....
gi 1310934957 408 VSVVILGVYRVADNDISMGGIIAAVMLAS 436
Cdd:pfam00664 240 ALALWFGAYLVISGELSVGDLVAFLSLFA 268
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
502-706 |
1.74e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 70.88 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 502 KPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKP----SNGSLRYDGIdsaQIHPSDLR-RNFGYLPQD----- 571
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALRgRKIATIMQNprsaf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 --VTLFHGSVRDNILFGTRQVTEHQLIRAvqlsgvnlftdLESEGLDQQ---VGEGGHSLSRGQRQTVALARAILNDPPV 646
Cdd:PRK10418 93 npLHTMHTHARETCLALGKPADDATLTAA-----------LEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 647 LLMDEPTASLDARAEKQFMRSMHNVSRDRTL--LIITHKMHLL-NLVDRIIVMDRGHIIADGP 706
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVaRLADDVAVMSHGRIVEQGD 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
501-710 |
2.01e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRydgidsaqiHPSDLRrnFGYLPQ----DVT--- 573
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLR--IGYVPQklylDTTlpl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 574 -------LFHGSVRDNILFGTRQVTEHQLIRAVQlsgvnlftdlesegldqqvgeggHSLSRGQRQTVALARAILNDPPV 646
Cdd:PRK09544 85 tvnrflrLRPGTKKEDILPALKRVQAGHLIDAPM-----------------------QKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 647 LLMDEPTASLDARAEKQFMRSMHNVSR--DRTLLIITHKMHL-LNLVDRIIVMDRgHIIADGPKDKV 710
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLvMAKTDEVLCLNH-HICCSGTPEVV 207
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
501-657 |
2.28e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 73.13 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVG-----------LFKPSNGSlrydgidSAQIHpsDLRRNFGYLP 569
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS-------GETIW--DIKKHIGYVS 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 QDVTL---FHGSVRDNILFG-------TRQVTEHQLIRAVQLsgvnlftdLESEGLDQQVGEGG-HSLSRGQRQTVALAR 638
Cdd:PRK10938 343 SSLHLdyrVSTSVRNVILSGffdsigiYQAVSDRQQKLAQQW--------LDILGIDKRTADAPfHSLSWGQQRLALIVR 414
|
170
....*....|....*....
gi 1310934957 639 AILNDPPVLLMDEPTASLD 657
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLD 433
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
501-713 |
2.54e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVG--LFKPSNGSLRYDGIDSAQIHPsDLRRNFG-YL----PQDVT 573
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEP-EERAHLGiFLafqyPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 574 lfhGSVRDNIL---FGTRQVTEHQliraVQLSGVNLFT---------DLESEGLDQQVGEGghsLSRGQRQTVALARAIL 641
Cdd:CHL00131 98 ---GVSNADFLrlaYNSKRKFQGL----PELDPLEFLEiineklklvGMDPSFLSRNVNEG---FSGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 642 NDPPVLLMDEPTASLDARAEKQFMRSMHNVSR-DRTLLIITHKMHLLNLV--DRIIVMDRGHIIADGPKD--KVLEK 713
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHYQRLLDYIkpDYVHVMQNGKIIKTGDAElaKELEK 244
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
512-712 |
2.66e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 2.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLL----VGLFKPSNGSLRYDGIDSAQIHPSdLRRNFGYLPQ-DVTLFHGSVRDNILF- 585
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKH-YRGDVVYNAEtDVHFPHLTVGETLDFa 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 586 ------GTRQVTEHQLIRAVQLSGVNLFTDLESEGLDQQVG-EGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDA 658
Cdd:TIGR00956 163 arcktpQNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 659 RAEKQFMRSMHNVSR--DRTLLIITHK--MHLLNLVDRIIVMDRGHIIADGPKDKVLE 712
Cdd:TIGR00956 243 ATALEFIRALKTSANilDTTPLVAIYQcsQDAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
490-657 |
5.63e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.72 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 490 ADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRNFGYLP 569
Cdd:PRK13543 14 AHALAFSR--NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 ---QDVtlfhgSVRDNILFgtrqVTEHQLIRAVQLSGVNLFTdlesegldqqVGEGGHS------LSRGQRQTVALARAI 640
Cdd:PRK13543 92 glkADL-----STLENLHF----LCGLHGRRAKQMPGSALAI----------VGLAGYEdtlvrqLSAGQKKRLALARLW 152
|
170
....*....|....*..
gi 1310934957 641 LNDPPVLLMDEPTASLD 657
Cdd:PRK13543 153 LSPAPLWLLDEPYANLD 169
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
514-712 |
6.67e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.81 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 514 PGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG--IDS---AQIHPsdLRRNFGYLPQDVtlfHGSVrdnilfGTR 588
Cdd:PRK10261 349 PGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTlspGKLQA--LRRDIQFIFQDP---YASL------DPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 589 QVTEHQLIRAVQLSGV--------NLFTDLESEGL-DQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDAR 659
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLlpgkaaaaRVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 660 AEKQFMRSMHNVSRDR--TLLIITHKMHLLNLVD-RIIVMDRGHIIADGPKDKVLE 712
Cdd:PRK10261 498 IRGQIINLLLDLQRDFgiAYLFISHDMAVVERIShRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
484-712 |
1.24e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.33 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 484 LMGKIEADDLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKpSNGSLRYDG--------IDSAQ 555
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLE-LNEEARVEGevrlfgrnIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 556 IHPSDLRRNFGYLPQDVTLF-HGSVRDNILFGtrqVTEHQLIRAVQLSGVNLFTDLESEGLDQQV----GEGGHSLSRGQ 630
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFpHLTIYDNVAIG---VKLNGLVKSKKELDERVEWALKKAALWDEVkdrlNDYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 631 RQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHK-MHLLNLVDRIIVMDRGHIIADGPKDK 709
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
...
gi 1310934957 710 VLE 712
Cdd:PRK14267 235 VFE 237
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
508-704 |
1.38e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.80 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 508 FALRirPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-LRRNFGYLPQDVT---LFHG-SVRDN 582
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKrdgLVLGmSVKEN 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 583 I-LFGTRQVTEH--QLIRAVQLSGVNLFTDL---ESEGLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPTASL 656
Cdd:PRK10762 351 MsLTALRYFSRAggSLKHADEQQAVSDFIRLfniKTPSMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTRGV 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1310934957 657 DARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDRGHIIAD 704
Cdd:PRK10762 427 DVGAKKEIYQLINQFKAEgLSIILVSSEMpEVLGMSDRILVMHEGRISGE 476
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
493-702 |
1.71e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 70.53 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 493 LSFSYPGsEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRY-DGIdsaqihpsdlrrNFGYLPQD 571
Cdd:PRK11819 12 VSKVVPP-KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI------------KVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 VTLFHG-SVRDNILFGTRQVTEHQ-------------------LIR---AVQ--LSGVNLFtDLES------EGL----- 615
Cdd:PRK11819 79 PQLDPEkTVRENVEEGVAEVKAALdrfneiyaayaepdadfdaLAAeqgELQeiIDAADAW-DLDSqleiamDALrcppw 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 616 DQQVGegghSLSRGQRQTVALARAILNDPPVLLMDEPTASLDarAE-----KQFMRSMHNvsrdrTLLIITHKMHLL-NL 689
Cdd:PRK11819 158 DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD--AEsvawlEQFLHDYPG-----TVVAVTHDRYFLdNV 226
|
250
....*....|...
gi 1310934957 690 VDRIIVMDRGHII 702
Cdd:PRK11819 227 AGWILELDRGRGI 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
488-706 |
1.99e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPG---------SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSNGSLRYDG-----IDS 553
Cdd:PRK15134 276 LDVEQLQVAFPIrkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGqplhnLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 554 AQIHPsdLRRNFGYLPQDVtlfHGSV--RDNILfgtrQVTE-----HQLIRAVQLSGVNLFTDLESEGLDQqvgEGGH-- 624
Cdd:PRK15134 355 RQLLP--VRHRIQVVFQDP---NSSLnpRLNVL----QIIEeglrvHQPTLSAAQREQQVIAVMEEVGLDP---ETRHry 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 625 --SLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTL--LIITHKMHLL-NLVDRIIVMDRG 699
Cdd:PRK15134 423 paEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVrALCHQVIVLRQG 502
|
....*..
gi 1310934957 700 HIIADGP 706
Cdd:PRK15134 503 EVVEQGD 509
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
501-699 |
2.24e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.91 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVG--LFKPSNGSLRYDGIDsaqihpsdlrrnfgyLPQDVTLFhgs 578
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQ---------------FGREASLI--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 579 vrDNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEgldqqvgegghsLSRGQRQTVALARAILNDPPVLLMDEPTASLDA 658
Cdd:COG2401 104 --DAIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1310934957 659 RAEKQFMRSMHNVSRDR--TLLIITHKMHLLNLV--DRIIVMDRG 699
Cdd:COG2401 170 QTAKRVARNLQKLARRAgiTLVVATHHYDVIDDLqpDLLIFVGYG 214
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
176-448 |
3.95e-12 |
|
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: 67.49 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18545 5 ALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL---ENRSAsvgG--MARQLGEFDSIREILTSATITTLVDLpFALLFVLII-YLVAGDLALIPLVASLIIIGYTLIV 329
Cdd:cd18545 85 KLSFsffDSRPV---GkiLSRVINDVNSLSDLLSNGLINLIPDL-LTLVGIVIImFSLNVRLALVTLAVLPLLVLVVFLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 330 QPRLKTA-IEESNKFASLkHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVV 408
Cdd:cd18545 161 RRRARKAwQRVRKKISNL-NAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1310934957 409 SVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANL 448
Cdd:cd18545 240 LVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNF 279
|
|
| Peptidase_C39_like |
cd02259 |
Peptidase family C39 mostly contains bacteriocin-processing endopeptidases from bacteria. The ... |
18-140 |
4.17e-12 |
|
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: 63.56 E-value: 4.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 18 QRVTVDPLLDSLVLLTEYFGSPCSSESLAAGLPLSSAVLSPELVPQAAARAGLTAKLSRKGLNQVTAIQLPCILLLKDKK 97
Cdd:cd02259 1 GGGPLDCGLACLQMLLRYFGIPVRRDVLLNAQQRRQQGLSLADLVSLANKLGLTAQGVKLPLAALSRLQLPALLLWKQGH 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1310934957 98 ACILRELDlEQQYaVIQLPETGGEQRLSIEELETLYVGYLFLV 140
Cdd:cd02259 81 FVILYGAD-KGQV-LIADPLEEGPVTLSESELEERWTGHWVLL 121
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
492-721 |
7.26e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 492 DLSFSYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsaqiHPSDLRRNFGYLPQD 571
Cdd:PRK10982 3 NISKSFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG------KEIDFKSSKEALENG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 VTLFHG--------SVRDNILFGTRQ-----VTEHQLIRAVQlsgvNLFTDLeseGLDQQVGEGGHSLSRGQRQTVALAR 638
Cdd:PRK10982 75 ISMVHQelnlvlqrSVMDNMWLGRYPtkgmfVDQDKMYRDTK----AIFDEL---DIDIDPRAKVATLSVSQMQMIEIAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 639 AILNDPPVLLMDEPTASLDARaEKQFMRSMHNVSRDRTLLI--ITHKM-HLLNLVDRIIVMDRGHIIADGPKDKVLEKLN 715
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSLTEK-EVNHLFTIIRKLKERGCGIvyISHKMeEIFQLCDEITILRDGQWIATQPLAGLTMDKI 226
|
....*.
gi 1310934957 716 QGLMAG 721
Cdd:PRK10982 227 IAMMVG 232
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
513-706 |
9.71e-12 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 68.72 E-value: 9.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 513 RPGERIAIIGRNGSGKSTLAKLLVGLFKPS--NGSLRYDGIDSAQihpSDLRRNFGYLPQ-DVTLFHGSVRDNILFGT-- 587
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQ---ETFARISGYCEQnDIHSPQVTVRESLIYSAfl 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 588 ---RQVTEHQLIRAVQlsgvNLFTDLESEGL-DQQVG-EGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEK 662
Cdd:PLN03140 981 rlpKEVSKEEKMMFVD----EVMELVELDNLkDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA 1056
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1310934957 663 QFMRSMHN-VSRDRTLLIITHK--MHLLNLVDRIIVMDR-GHIIADGP 706
Cdd:PLN03140 1057 IVMRTVRNtVDTGRTVVCTIHQpsIDIFEAFDELLLMKRgGQVIYSGP 1104
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
482-682 |
1.39e-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: 67.65 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 482 QRLMGK-IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDgiDSAQIHPSD 560
Cdd:TIGR03719 316 PRLGDKvIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 561 LRRNfgYLPQDVTLFH----GSvrDNILFGTRQVTEHQLIRAVQLSGVnlftdleseglDQQ--VGEgghsLSRGQRQTV 634
Cdd:TIGR03719 392 QSRD--ALDPNKTVWEeisgGL--DIIKLGKREIPSRAYVGRFNFKGS-----------DQQkkVGQ----LSGGERNRV 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 635 ALARAILNDPPVLLMDEPTASLDARAekqfMRSMHN-----------VSRDRTLL--IITH 682
Cdd:TIGR03719 453 HLAKTLKSGGNVLLLDEPTNDLDVET----LRALEEallnfagcavvISHDRWFLdrIATH 509
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
510-708 |
2.52e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSnGSlrYDG---IDSAQIHPSDLR----RNFGYLPQDVTLF-HGSVRD 581
Cdd:PRK13549 26 LKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PH-GT--YEGeiiFEGEELQASNIRdterAGIAIIHQELALVkELSVLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 582 NILFGtRQVTEHQLI-------RAVQ-LSGVNLFTDlesegLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPT 653
Cdd:PRK13549 102 NIFLG-NEITPGGIMdydamylRAQKlLAQLKLDIN-----PATPVGN----LGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 654 ASLDARAEKQFMRSMHNV-SRDRTLLIITHKmhlLNLV----DRIIVMDRGHIIADGPKD 708
Cdd:PRK13549 172 ASLTESETAVLLDIIRDLkAHGIACIYISHK---LNEVkaisDTICVIRDGRHIGTRPAA 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
491-699 |
3.18e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 491 DDLS--FSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPS------NGSLRYDGIDSAQIHPSDLR 562
Cdd:PRK15134 9 ENLSvaFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 563 RnfgylpqdvtlfhgsVRDN---ILFGTRQVT-------EHQLIRAVQL--------SGVNLFTDLESEGLDQ---QVGE 621
Cdd:PRK15134 88 G---------------VRGNkiaMIFQEPMVSlnplhtlEKQLYEVLSLhrgmrreaARGEILNCLDRVGIRQaakRLTD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 622 GGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSR--DRTLLIITHKMHLL-NLVDRIIVMDR 698
Cdd:PRK15134 153 YPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQN 232
|
.
gi 1310934957 699 G 699
Cdd:PRK15134 233 G 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
496-706 |
3.76e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 496 SYPGSEkpVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRR-NFGYLPQDVTL 574
Cdd:PRK10762 13 AFPGVK--ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEaGIGIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 F-HGSVRDNILFGTRQVTEHQLI--RAVQLSGVNLFTDLE-SEGLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMD 650
Cdd:PRK10762 91 IpQLTIAENIFLGREFVNRFGRIdwKKMYAEADKLLARLNlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 651 EPTASL-DARAEkqfmrSMHNVSRD-----RTLLIITHKM-HLLNLVDRIIVMDRGHIIADGP 706
Cdd:PRK10762 167 EPTDALtDTETE-----SLFRVIRElksqgRGIVYISHRLkEIFEICDDVTVFRDGQFIAERE 224
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
514-700 |
5.55e-11 |
|
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: 61.24 E-value: 5.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 514 PGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYdgidsaqihpsdlrrnfgylpqdvtlfhgsvrdnilfgtrqvteh 593
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 594 qliravqLSGVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMH---- 669
Cdd:smart00382 36 -------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1310934957 670 ---NVSRDRTLLIITH------KMHLLNLVDRIIVMDRGH 700
Cdd:smart00382 109 lllKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLIL 148
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
505-706 |
7.06e-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: 65.23 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 505 LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPS--NGSLRYDGIDSAQIHPSDL-RRNFGYLPQDVTLFHG-SVR 580
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 581 DNILFGtRQVTE--------------HQLIRAVQLSGVNlftdlesegLDQQVGEGGhslsRGQRQTVALARAILNDPPV 646
Cdd:TIGR02633 97 ENIFLG-NEITLpggrmaynamylraKNLLRELQLDADN---------VTRPVGDYG----GGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 647 LLMDEPTASLdARAEKQFMRSM------HNVSrdrtLLIITHKMHLLNLV-DRIIVMDRGHIIADGP 706
Cdd:TIGR02633 163 LILDEPSSSL-TEKETEILLDIirdlkaHGVA----CVYISHKLNEVKAVcDTICVIRDGQHVATKD 224
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
498-699 |
1.86e-10 |
|
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: 60.72 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 498 PGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLL-----VGLFKpsnGSLRYDGidsaQIHPSDLRRNFGYLPQ-D 571
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILING----RPLDKNFQRSTGYVEQqD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 VTLFHGSVRDNILFgtrqvteHQLIRAvqlsgvnlftdlesegldqqvgegghsLSRGQRQTVALARAILNDPPVLLMDE 651
Cdd:cd03232 89 VHSPNLTVREALRF-------SALLRG---------------------------LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1310934957 652 PTASLDARAEKQFMRSMHNVSRD-RTLLIITHK--MHLLNLVDRIIVMDRG 699
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKLADSgQAILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
488-652 |
2.45e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDL---RRN 564
Cdd:PRK11831 8 VDMRGVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 565 FGYLPQDVTLFHG-SVRDNILFGTRQVTehQLIRAVQLSGVNLftDLESEGLDQQVGEGGHSLSRGQRQTVALARAILND 643
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPLREHT--QLPAPLLHSTVMM--KLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
|
....*....
gi 1310934957 644 PPVLLMDEP 652
Cdd:PRK11831 162 PDLIMFDEP 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
510-701 |
2.58e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.53 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-LRRNFGYLPQD----------------V 572
Cdd:PRK15439 284 LEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEDrqssglyldaplawnvC 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 573 TLFHGsvrdNILFGTRQVTEhqliRAVqLSGVNLFTDLESEGLDQQVGegghSLSRGQRQTVALARAILNDPPVLLMDEP 652
Cdd:PRK15439 364 ALTHN----RRGFWIKPARE----NAV-LERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 653 TASLD--ARAE-KQFMRSM--HNVSrdrtLLIITHKMH-LLNLVDRIIVMDRGHI 701
Cdd:PRK15439 431 TRGVDvsARNDiYQLIRSIaaQNVA----VLFISSDLEeIEQMADRVLVMHQGEI 481
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
501-687 |
2.83e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.65 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRY-DGIdsaqihpsdlrrNFGYLPQDVTLFHGSV 579
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGI------------KLGYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 580 RDNILFGTR---QVTEHQLirAVQLSGVNLFTDlesegldqQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASL 656
Cdd:PRK10636 392 ESPLQHLARlapQELEQKL--RDYLGGFGFQGD--------KVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180 190
....*....|....*....|....*....|.
gi 1310934957 657 DARAEKQFMRSMhnVSRDRTLLIITHKMHLL 687
Cdd:PRK10636 462 DLDMRQALTEAL--IDFEGALVVVSHDRHLL 490
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
492-705 |
3.58e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 492 DLSFSYPGSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG----------IDSAQIHPSDL 561
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 562 RRNFGylpQDVTL-FHGSVRD-NILFGT-RQVTE----HQ-LIRAVQLSGVNLFTDL----ESEGLdqqVGEGGHSLSRG 629
Cdd:PRK10261 99 RHVRG---ADMAMiFQEPMTSlNPVFTVgEQIAEsirlHQgASREEAMVEAKRMLDQvripEAQTI---LSRYPHQLSGG 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 630 QRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTL--LIITHKMHLL-NLVDRIIVMDRGHIIADG 705
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVaEIADRVLVMYQGEAVETG 251
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
485-711 |
5.64e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.36 E-value: 5.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYPGSEKPV--LHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKP----SNGSLRYDGIDSAQIHP 558
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 559 SDLRRNFGYlpqDVTLFHGSVRDNILFGTRqvTEHQLIRAV----------QLSGVNLFTDLEsegLDQQVGEGGH---- 624
Cdd:PRK15093 81 RERRKLVGH---NVSMIFQEPQSCLDPSER--VGRQLMQNIpgwtykgrwwQRFGWRKRRAIE---LLHRVGIKDHkdam 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 625 -----SLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMR--SMHNVSRDRTLLIITHKMHLLN-LVDRIIVM 696
Cdd:PRK15093 153 rsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRllTRLNQNNNTTILLISHDLQMLSqWADKINVL 232
|
250
....*....|....*
gi 1310934957 697 DRGHIIADGPKDKVL 711
Cdd:PRK15093 233 YCGQTVETAPSKELV 247
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
510-710 |
7.26e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 61.26 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSDLRRnfgylpqdvtlfhgsVRDNIlfgtrq 589
Cdd:PRK15079 42 LRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRA---------------VRSDI------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 590 vtehQLIRAVQLSGVN---LFTDLESEGL--------DQQVGEG------------------GHSLSRGQRQTVALARAI 640
Cdd:PRK15079 101 ----QMIFQDPLASLNprmTIGEIIAEPLrtyhpklsRQEVKDRvkammlkvgllpnlinryPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDR--TLLIITHKMHLL-NLVDRIIVMDRGHIIADGPKDKV 710
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVkHISDRVLVMYLGHAVELGTYDEV 249
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
610-714 |
1.18e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.52 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 610 LESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKM-HLL 687
Cdd:NF000106 129 LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMeEAE 208
|
90 100
....*....|....*....|....*..
gi 1310934957 688 NLVDRIIVMDRGHIIADGPKDKVLEKL 714
Cdd:NF000106 209 QLAHELTVIDRGRVIADGKVDELKTKV 235
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
474-699 |
1.25e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.43 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 474 NKGHLVsKQRLMGKIEADDLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGS---LRYDG 550
Cdd:PLN03211 56 NKGSNI-KRILGHKPKISDETRQI--QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTgtiLANNR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 551 IDSAQIhpsdLRRNfGYLPQDVTLF-HGSVRDNILFGT-----RQVTEHQLIRAVQ--LSGVNLfTDLESEGLDQQVGEG 622
Cdd:PLN03211 133 KPTKQI----LKRT-GFVTQDDILYpHLTVRETLVFCSllrlpKSLTKQEKILVAEsvISELGL-TKCENTIIGNSFIRG 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 623 ghsLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVS-RDRTLLIITHK--MHLLNLVDRIIVMDRG 699
Cdd:PLN03211 207 ---ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQpsSRVYQMFDSVLVLSEG 283
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
491-657 |
1.34e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 491 DDLSFSYPgsekpvlhpfalrirPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYdGiDSAQIHPSDLRRnfGYLPQ 570
Cdd:PRK11819 341 DDLSFSLP---------------PGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKLAYVDQSR--DALDP 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 571 DVTLFH----GSvrDNILFGTRQVTEhqliRAVqLSGVNlFTdleseGLDQQ--VGEgghsLSRGQRQTVALARAILNDP 644
Cdd:PRK11819 402 NKTVWEeisgGL--DIIKVGNREIPS----RAY-VGRFN-FK-----GGDQQkkVGV----LSGGERNRLHLAKTLKQGG 464
|
170
....*....|...
gi 1310934957 645 PVLLMDEPTASLD 657
Cdd:PRK11819 465 NVLLLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
513-696 |
1.48e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 513 RPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGslRYDGIDSAQ-----IHPSDLRRNFGYL----------PQDVTL--- 574
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWDeildeFRGSELQNYFTKLlegdvkvivkPQYVDLipk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 -FHGSVRDNILFGTRQVTEHQLIRAVQLSGVnlftdlesegLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPT 653
Cdd:cd03236 102 aVKGKVGELLKKKDERGKLDELVDQLELRHV----------LDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1310934957 654 ASLDARAEKQFMRSMHNVSRD-RTLLIITHKMHLLN-LVDRIIVM 696
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDdNYVLVVEHDLAVLDyLSDYIHCL 212
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
176-462 |
2.07e-09 |
|
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: 59.37 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNlafESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18551 4 ALLLSLLGTAASLAQPLLVKNLIDALSAG---GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL----ENRSASVggMARQLGEFDSIREILTSatitTLVDLPFALLFVL--IIYLVAGD--LALIPLVASLIIIGYTL 327
Cdd:cd18551 81 RLPVsffdRRRSGDL--VSRVTNDTTLLRELITS----GLPQLVTGVLTVVgaVVLMFLLDwvLTLVTLAVVPLAFLIIL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 328 IVQPRLKTAIEES-NKFASLKhGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLT 406
Cdd:cd18551 155 PLGRRIRKASKRAqDALGELS-AALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 407 VVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQL 462
Cdd:cd18551 234 LLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
506-708 |
2.17e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 506 HPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG----IDSAQ--IH------PSDlRRNFGYLPqdvt 573
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidIRSPRdaIRagimlcPED-RKAEGIIP---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 574 lfHGSVRDNILFGTRqvtehqliRAVQLSGVNLFTDLESEGLDQQVGE------GGHS----LSRGQRQTVALARAILND 643
Cdd:PRK11288 345 --VHSVADNINISAR--------RHHLRAGCLINNRWEAENADRFIRSlniktpSREQlimnLSGGNQQKAILGRWLSED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 644 PPVLLMDEPTASLDARAEKQFMRSMHNVS-RDRTLLIITHK-MHLLNLVDRIIVMDRGHIIADGPKD 708
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAaQGVAVLFVSSDlPEVLGVADRIVVMREGRIAGELARE 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
512-712 |
2.55e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.02 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGLFKPS---NGSLRYDGIDSAQIHPsdlRRNFGYLPQ-DVTLFHGSVRDNILF-- 585
Cdd:PLN03140 188 IKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVP---RKTSAYISQnDVHVGVMTVKETLDFsa 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 586 -----GTRQVTEHQLIR------------------AVQLSGV--NLFTD--LESEGLD----QQVG-EGGHSLSRGQRQT 633
Cdd:PLN03140 265 rcqgvGTRYDLLSELARrekdagifpeaevdlfmkATAMEGVksSLITDytLKILGLDickdTIVGdEMIRGISGGQKKR 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 634 VALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSR--DRTLLiithkMHLL-------NLVDRIIVMDRGHIIAD 704
Cdd:PLN03140 345 VTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHltEATVL-----MSLLqpapetfDLFDDIILLSEGQIVYQ 419
|
....*...
gi 1310934957 705 GPKDKVLE 712
Cdd:PLN03140 420 GPRDHILE 427
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
486-547 |
2.57e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 2.57e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 486 GKI--EADDLSFSYPGseKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLR 547
Cdd:PRK11147 316 GKIvfEMENVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
492-691 |
2.88e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 492 DLSFSYpgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGidsaQIHPSDLRrnfGYLPQD 571
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER----QSIKKDLC---TYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 VTLFHGS-------VRDNILF------GTRQVTEhqLIRAVQLSGVnlftdlesegLDQQVGegghSLSRGQRQTVALAR 638
Cdd:PRK13540 77 CFVGHRSginpyltLRENCLYdihfspGAVGITE--LCRLFSLEHL----------IDYPCG----LLSSGQKRQVALLR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 639 AILNDPPVLLMDEPTASLDARAEKQFMRSMH-NVSRDRTLLIITHKMHLLNLVD 691
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQeHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
512-696 |
4.03e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 4.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGLFKPS---NGSLRYDGIDSAQIHPSDLRR----NFGYLPQD-VTLFHGSVRdni 583
Cdd:PRK09473 39 LRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDpMTSLNPYMR--- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 584 lfgtrqVTEhQLIRAVQL-SGVNLFTDLES--EGLD--------QQVGEGGHSLSRGQRQTVALARAILNDPPVLLMDEP 652
Cdd:PRK09473 116 ------VGE-QLMEVLMLhKGMSKAEAFEEsvRMLDavkmpearKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEP 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1310934957 653 TASLDARAEKQFMRSMHNVSRD--RTLLIITHKMHLL-NLVDRIIVM 696
Cdd:PRK09473 189 TTALDVTVQAQIMTLLNELKREfnTAIIMITHDLGVVaGICDKVLVM 235
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
512-696 |
4.13e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGslRYDGIDSA------------QIHPSDLRRN---FGYLPQDVTL-- 574
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLG--DYEEEPSWdevlkrfrgtelQNYFKKLYNGeikVVHKPQYVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 --FHGSVRDnILfgtRQVTEH----QLIRAVQLSGVnlftdlesegLDQQVGEgghsLSRGQRQTVALARAILNDPPVLL 648
Cdd:PRK13409 174 kvFKGKVRE-LL---KKVDERgkldEVVERLGLENI----------LDRDISE----LSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1310934957 649 MDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLN-LVDRIIVM 696
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDyLADNVHIA 284
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
512-701 |
5.50e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 5.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHPSD-LRRNFGYLPQdvtlfhgSVRDNILFGTRQV 590
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDaVKKGMAYITE-------SRRDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 591 TEHQLI-RAVQLSG----VNLFTD---------------LESEGLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMD 650
Cdd:PRK09700 359 AQNMAIsRSLKDGGykgaMGLFHEvdeqrtaenqrellaLKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 651 EPTASLDARAEKQFMRSMHNVSRD-RTLLIITHKM-HLLNLVDRIIVMDRGHI 701
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELpEIITVCDRIAVFCEGRL 487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
515-690 |
5.89e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 515 GERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDgidsaqihpSDLRrnFGYLPQDVTLFHG-SVRDNILFGTRQV--- 590
Cdd:PRK15064 27 GNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD---------PNER--LGKLRQDQFAFEEfTVLDTVIMGHTELwev 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 591 -------------TEHQLIRAVQLS--------------------GVNLFTDLESeGLDQQVgegghslSRGQRQTVALA 637
Cdd:PRK15064 96 kqerdriyalpemSEEDGMKVADLEvkfaemdgytaearagelllGVGIPEEQHY-GLMSEV-------APGWKLRVLLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 638 RAILNDPPVLLMDEPTASLDARAekqfMRSMHNV--SRDRTLLIITHKMHLLNLV 690
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINT----IRWLEDVlnERNSTMIIISHDRHFLNSV 218
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
510-713 |
5.99e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.37 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQI-HPSDLRRNFGYLPQDV------TLfhgSVRDN 582
Cdd:NF033858 22 LDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADArHRRAVCPRIAYMPQGLgknlypTL---SVFEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 583 I-----LFGTRQVTEHQLIRAVqlsgvnlftdLESEGL----DQQVGEgghsLSRGQRQTVALARAILNDPPVLLMDEPT 653
Cdd:NF033858 99 LdffgrLFGQDAAERRRRIDEL----------LRATGLapfaDRPAGK----LSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1310934957 654 ASLDARAEKQFMRSMHNVSRDR---TLLIITHKMHLLNLVDRIIVMDRGHIIADGPKDKVLEK 713
Cdd:NF033858 165 TGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERFDWLVAMDAGRVLATGTPAELLAR 227
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
176-460 |
6.09e-09 |
|
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: 57.82 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18552 4 AILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL----ENRSASVggMARQLGEFDSIREILTSAtITTLVDLPFALLFvLIIYLVAGD--LALIPLVASLIIIGYTLIV 329
Cdd:cd18552 84 RLPLsffdRNSSGDL--ISRITNDVNQVQNALTSA-LTVLVRDPLTVIG-LLGVLFYLDwkLTLIALVVLPLAALPIRRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 330 QPRL-KTAIEESNKFASLKHgHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVV 408
Cdd:cd18552 160 GKRLrKISRRSQESMGDLTS-VLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 409 SVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALR 460
Cdd:cd18552 239 LVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
488-701 |
8.86e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 58.72 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 488 IEADDLSFSYPGSekPVL-HPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSL--------------RYDGID 552
Cdd:PLN03073 509 ISFSDASFGYPGG--PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 553 SAQIHPSDLRRNFGYLPQdvtlfhgsvrdnilfgtrqvtehQLIRAvQLSGVNLFTDLESEGLdqqvgeggHSLSRGQRQ 632
Cdd:PLN03073 587 LSSNPLLYMMRCFPGVPE-----------------------QKLRA-HLGSFGVTGNLALQPM--------YTLSGGQKS 634
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 633 TVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMhnVSRDRTLLIITHKMHLLN-LVDRIIVMDRGHI 701
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
485-706 |
9.43e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 9.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 485 MGKIEADDLSFSYpGSEKPvlhPF------ALRIRPGERIAIIGRNGSGKSTLAKLLVGLF----KPSNGSLRYDGIDSA 554
Cdd:PRK11022 1 MALLNVDKLSVHF-GDESA---PFravdriSYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 555 QIHPSDLRRNFGylpQDVTLFHG----------SVRDNIL------FGTRQVTEHQliRAVQLSGVNLFTDLESEgLDQQ 618
Cdd:PRK11022 77 RISEKERRNLVG---AEVAMIFQdpmtslnpcyTVGFQIMeaikvhQGGNKKTRRQ--RAIDLLNQVGIPDPASR-LDVY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 619 vgegGHSLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVSR--DRTLLIITHKMHLL-NLVDRIIV 695
Cdd:PRK11022 151 ----PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIV 226
|
250
....*....|.
gi 1310934957 696 MDRGHIIADGP 706
Cdd:PRK11022 227 MYAGQVVETGK 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
512-699 |
3.12e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGlfkPSNGSLRYDGIDSAQIHPSD--LRRNFGYLPQ-DVTLFHGSVRDNILFGT- 587
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE---RVTTGVITGGDRLVNGRPLDssFQRSIGYVQQqDLHLPTSTVRESLRFSAy 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 588 -RQVTEhqliraVQLSGVNLFTD-----LESEGL-DQQVGEGGHSLSRGQRQTVALARAILNDPPVLL-MDEPTASLDAR 659
Cdd:TIGR00956 863 lRQPKS------VSKSEKMEYVEeviklLEMESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1310934957 660 AEKQFMRSMHNVSRD-RTLLIITHK--MHLLNLVDRIIVMDRG 699
Cdd:TIGR00956 937 TAWSICKLMRKLADHgQAILCTIHQpsAILFEEFDRLLLLQKG 979
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
510-705 |
3.29e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPS---NGSLRYDG-------I-DSAQ-----IHpsdlrrnfgylpQDVT 573
Cdd:NF040905 22 LSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfkdIrDSEAlgiviIH------------QELA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 574 LF-HGSVRDNILFGTRQVT------EHQLIRAVQLsgvnlftdLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDPPV 646
Cdd:NF040905 89 LIpYLSIAENIFLGNERAKrgvidwNETNRRAREL--------LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1310934957 647 LLMDEPTASL---DARAEKQFMRSMhnvsRDR--TLLIITHKmhlLNLVDRiiVMDRGHIIADG 705
Cdd:NF040905 161 LILDEPTAALneeDSAALLDLLLEL----KAQgiTSIIISHK---LNEIRR--VADSITVLRDG 215
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
500-711 |
4.66e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 500 SEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRydgidSAQIHPSDL--------------RRNF 565
Cdd:PRK10938 14 SDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQ-----SQFSHITRLsfeqlqklvsdewqRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 566 GYLPQDVTLFHGSVRDNILFGTRQVTehqliRAVQLSGVNLFTDLESEGLDQqvgegghsLSRGQRQTVALARAILNDPP 645
Cdd:PRK10938 89 DMLSPGEDDTGRTTAEIIQDEVKDPA-----RCEQLAQQFGITALLDRRFKY--------LSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1310934957 646 VLLMDEPTASLDARAEKQFMRSMHNVSRDR-TLLIITHKMH-LLNLVDRIIVMDRGHIIADGPKDKVL 711
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGiTLVLVLNRFDeIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
491-712 |
6.52e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 491 DDLSFSypgsekpvlhpfalrIRPGERIAIIGRNGSGKSTLAKLLVGLFK-PSNGSLRYDGIDSAQIHPSD-LRRNFGYL 568
Cdd:PRK13549 279 DDVSFS---------------LRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQGIAMV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 569 PQD------VTLFhgSVRDNI-LFGTRQVTEHQLIR-AVQLSGVNLFTD---LESEGLDQQVGegghSLSRGQRQTVALA 637
Cdd:PRK13549 344 PEDrkrdgiVPVM--GVGKNItLAALDRFTGGSRIDdAAELKTILESIQrlkVKTASPELAIA----RLSGGNQQKAVLA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 638 RAILNDPPVLLMDEPTASLDARAEKQFMRSMHN-VSRDRTLLIITHKM-HLLNLVDRIIVMDRGHIIADGPKD-----KV 710
Cdd:PRK13549 418 KCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELpEVLGLSDRVLVMHEGKLKGDLINHnltqeQV 497
|
..
gi 1310934957 711 LE 712
Cdd:PRK13549 498 ME 499
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-460 |
7.00e-08 |
|
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: 54.82 E-value: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVV----PNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLF 251
Cdd:cd18563 4 GFLLMLLGTALGLVPPYLTKILIDDVLiqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 252 YKAIGIPLE--NRSaSVGG-MARQLGEFDSIREILTSATITTLVD-LPFALLFVLIIYLVAGdLALIPLVASLIIIGYTL 327
Cdd:cd18563 84 EHLQRLSLSffDKR-QTGSlMSRVTSDTDRLQDFLSDGLPDFLTNiLMIIGIGVVLFSLNWK-LALLVLIPVPLVVWGSY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 328 IVQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTV 407
Cdd:cd18563 162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGT 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 408 VSVVILGVYRVADNDISMGGIIAAVMLASRAVAP---MAQLANLMTRAnqTASALR 460
Cdd:cd18563 242 LIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPlqwLSRLNNWITRA--LTSAER 295
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
177-462 |
9.63e-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: 54.03 E-value: 9.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 177 LIASILV---NLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYK 253
Cdd:cd18546 2 ALALLLVvvdTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 254 AIGIPL----ENRSASVggMARQLGEFDSIREILTSATITTLVDLpFALLFVLIIyLVAGD--LALIPLVASLIIIGYTL 327
Cdd:cd18546 82 LQRLSLdfheRETSGRI--MTRMTSDIDALSELLQTGLVQLVVSL-LTLVGIAVV-LLVLDprLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 328 IVQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTV 407
Cdd:cd18546 158 WFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLAT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 408 VSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQL 462
Cdd:cd18546 238 AAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| Peptidase_C39_likeA |
cd02417 |
A sub-family of peptidase C39 which contains Cyclolysin and Hemolysin processing peptidases. ... |
22-140 |
1.18e-07 |
|
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: 50.71 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 22 VDPLLDSLVLLTEYFGSPCSSESLAAGLPLSSAVLSPELVPQAAARAGLTAKLSRKGLNQVTAIQLPCILLLKDKKACIL 101
Cdd:cd02417 5 PDSGLLALVLLARYHGIAADPEQLRHEFGLAGEPFNSTELLLAAKSLGLKAKAVRQPVERLARLPLPALAWDDDGGHFIL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1310934957 102 RELDlEQQYaVIQLPETGGEQRLSIEELETLYVGYLFLV 140
Cdd:cd02417 85 AKLD-GQKY-LIQDPISQRPEVLSREEFEARWSGELILV 121
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
513-696 |
2.27e-07 |
|
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: 54.02 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 513 RPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSL-----------RYDGIDsAQIHPSDLRRN---FGYLPQDVTL---- 574
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTE-LQDYFKKLANGeikVAHKPQYVDLipkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 575 FHGSVRDnILfgtRQVTEH----QLIRAVQLSGVnlftdlesegLDQQVGEgghsLSRGQRQTVALARAILNDPPVLLMD 650
Cdd:COG1245 176 FKGTVRE-LL---EKVDERgkldELAEKLGLENI----------LDRDISE----LSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 651 EPTASLDARaekQFMrsmhNVSR--------DRTLLIITHKMHLLNLV-DRIIVM 696
Cdd:COG1245 238 EPSSYLDIY---QRL----NVARlirelaeeGKYVLVVEHDLAILDYLaDYVHIL 285
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
423-698 |
2.48e-07 |
|
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: 53.98 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 423 ISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALRQLDQIMTQEDEFENKGHLVSKQRLM---GKIEADDLSFSYpg 499
Cdd:TIGR00954 377 LKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVpgrGIVEYQDNGIKF-- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 500 SEKPVLHP--------FALRIRPGERIAIIGRNGSGKSTLAKLLVGLFkPSNGSLRYdgidsaqihpSDLRRNFGYLPQD 571
Cdd:TIGR00954 455 ENIPLVTPngdvliesLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT----------KPAKGKLFYVPQR 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 572 VTLFHGSVRDNIL-------FGTRQVTEHQLIRAVQLsgVNLFTDLESEGLDQQVGEGGHSLSRGQRQTVALARAILNDP 644
Cdd:TIGR00954 524 PYMTLGTLRDQIIypdssedMKRRGLSDKDLEQILDN--VQLTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKP 601
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 645 PVLLMDEPTASLDARAEKQfmrsMHNVSRDR--TLLIITHKMHLLNLVDRIIVMDR 698
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGY----MYRLCREFgiTLFSVSHRKSLWKYHEYLLYMDG 653
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
176-448 |
2.59e-07 |
|
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: 52.86 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18569 7 VVLAGLLLVIPGLVIPVFSRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPLE---NRSAsvGGMARQLGEFDSIREILTSATITTLVDLPFALLF--VLIIYLVAgdLALIPLVASLIIIGYTLIVQ 330
Cdd:cd18569 87 RLPVEffsQRYA--GDIASRVQSNDRVANLLSGQLATTVLNLVMAVFYalLMLQYDVP--LTLIGIAIALLNLLVLRLVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 331 PRLKTA----IEESNKFAslkhGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLT 406
Cdd:cd18569 163 RKRVDLnrrlLQDSGKLT----GTTMSGLQMIETLKASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1310934957 407 VVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANL 448
Cdd:cd18569 239 NAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGL 280
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
176-458 |
4.16e-07 |
|
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: 52.10 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPL----ENRSASVggMARQLGEFDSIREILTSaTITTLVDLPFALLF-VLIIYLVAGDLALI------PLVASLIIIG 324
Cdd:cd18576 81 RLPLsffhERRVGEL--TSRLSNDVTQIQDTLTT-TLAEFLRQILTLIGgVVLLFFISWKLTLLmlatvpVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 325 YTLivQPRLKTAIE---ESNkfaslkhGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANF 401
Cdd:cd18576 158 RRI--RKLSKKVQDelaEAN-------TIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 402 VVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASA 458
Cdd:cd18576 229 LLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGA 285
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
625-701 |
4.21e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.21e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 625 SLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAEKQFMRSMHNVS-RDRTLLIITHKM-HLLNLVDRIIVMDRGHI 701
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMpELLGITDRILVMSNGLV 469
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
520-704 |
7.83e-07 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 51.12 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 520 IIGRNGSGKSTLAKLLVGLFKpSN----GSLRydgIDSAQIHPSDLR--RNFGYLPQDVTLF-HGSVRDNILFGTRQVTE 592
Cdd:COG4938 25 LIGPNGSGKSTLIQALLLLLQ-SNfiylPAER---SGPARLYPSLVRelSDLGSRGEYTADFlAELENLEILDDKSKELL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 593 HQL---IRAVQLSGVNLFTDLESEGLDQQVGEGGHSL-----SRGQRQTVALARAILNDPP---VLLMDEPTASLDARAE 661
Cdd:COG4938 101 EQVeewLEKIFPGKVEVDASSDLVRLVFRPSGNGKRIplsnvGSGVSELLPILLALLSAAKpgsLLIIEEPEAHLHPKAQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1310934957 662 KQFMRSMHN-VSRDRTLLIITHKMHLLNLVdRIIVMDRGHIIAD 704
Cdd:COG4938 181 SALAELLAElANSGVQVIIETHSDYILNGL-RNLIKEGKLLDPD 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
491-704 |
1.74e-06 |
|
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: 51.36 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 491 DDLSFSypgsekpvlhpfalrIRPGERIAIIGRNGSGKSTLAKLLVGLFKPS-NGSLRYDGIDSAQIHPSD-LRRNFGYL 568
Cdd:TIGR02633 277 DDVSFS---------------LRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQaIRAGIAMV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 569 PQDVTLfHGSVrdNILFGTRQVTEHQLIRAVQLSGVNLFTDLES--EGLDQQVGEGGH------SLSRGQRQTVALARAI 640
Cdd:TIGR02633 342 PEDRKR-HGIV--PILGVGKNITLSVLKSFCFKMRIDAAAELQIigSAIQRLKVKTASpflpigRLSGGNQQKAVLAKML 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 641 LNDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLII--THKMHLLNLVDRIIVMDRGHIIAD 704
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVvsSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-449 |
2.05e-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: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKV-VPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKA 254
Cdd:cd18778 4 TLLCALLSTLLGLVPPWLIRELVDLVtIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 255 IGIPL---ENRSAsvgG--MARQLGEFDSIREILTSATITTLVDLpFALLFVLIIYLVA----GDLALIPL-VASLIIIG 324
Cdd:cd18778 84 QRLSLryfDDRQT---GdlMSRVINDVANVERLIADGIPQGITNV-LTLVGVAIILFSInpklALLTLIPIpFLALGAWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 325 YTLIVQPRLKTAIEESNKFASLkhghLIESLASLESIKSYGAEglvQKAWQQMIGHTANW---QLRSKKLSNSVANVANF 401
Cdd:cd18778 160 YSKKVRPRYRKVREALGELNAL----LQDNLSGIREIQAFGRE---EEEAKRFEALSRRYrkaQLRAMKLWAIFHPLMEF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1310934957 402 VVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLM 449
Cdd:cd18778 233 LTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLN 280
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
501-705 |
2.14e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 501 EKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGL--FKPSNGSLRYDGIDSAQIHPSDlRRNFGYLpqdvTLFHGS 578
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPED-RAGEGIF----MAFQYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 579 VR----DNILFGTRQVTEHQLIRAVQLSGVNLFTDLESEG----------LDQQVGEGghsLSRGQRQTVALARAILNDP 644
Cdd:PRK09580 88 VEipgvSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKiallkmpedlLTRSVNVG---FSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 645 PVLLMDEPTASLDARAEKQFMRSMhNVSRD--RTLLIITHKMHLLNLV--DRIIVMDRGHIIADG 705
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGV-NSLRDgkRSFIIVTHYQRILDYIkpDYVHVLYQGRIVKSG 228
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
176-460 |
3.01e-06 |
|
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: 49.74 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18542 4 AILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPLE----NRSasvgG--MARQLGEFDSIREILtSATITTLVDLpfALLFVLIIYLVAG---DLALIPLVASLIIIGYT 326
Cdd:cd18542 84 RLSFSfhdkART----GdlMSRCTSDVDTIRRFL-AFGLVELVRA--VLLFIGALIIMFSinwKLTLISLAIIPFIALFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 327 LIVQPRLKTAIEE-SNKFASLkHGHLIESLASLESIKSYGAEGL-VQKawqqMIGHTANWQLRSKKLSNSVAN---VANF 401
Cdd:cd18542 157 YVFFKKVRPAFEEiREQEGEL-NTVLQENLTGVRVVKAFAREDYeIEK----FDKENEEYRDLNIKLAKLLAKywpLMDF 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 402 VVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLA---NLMTRANqtASALR 460
Cdd:cd18542 232 LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGrliNDMSRAS--ASAER 291
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
510-699 |
3.15e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 50.00 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 510 LRIRPGERI-AIIGRNGSGKSTLAKLLVGLFKPSNgslrydgidSAQIHPSDLRRNFGYLPQDVT--------------- 573
Cdd:COG3593 17 LSIELSDDLtVLVGENNSGKSSILEALRLLLGPSS---------SRKFDEEDFYLGDDPDLPEIEieltfgsllsrllrl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 574 LFHGSVRDNILFGTRQVTEH--QLIRAVQ----------LSGVNLFTDLESEGLDQ-------QVGEGG----HSLSRGQ 630
Cdd:COG3593 88 LLKEEDKEELEEALEELNEElkEALKALNellseylkelLDGLDLELELSLDELEDllkslslRIEDGKelplDRLGSGF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 631 RQTV--ALARAIL-----NDPPVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLII-THKMHLLNLV--DRIIVMDRG 699
Cdd:COG3593 168 QRLIllALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIItTHSPHLLSEVplENIRRLRRD 246
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
512-694 |
3.78e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 512 IRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDG-------------IDSAQI-HPSDLRRNFGYLPQDvtLFHG 577
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpaLPQPALeYVIDGDREYRQLEAQ--LHDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 578 SVRDNilfGTRQVTEHQLIRAVQ-----------LSGVNlftdLESEGLDQQVgeggHSLSRGQRQTVALARAILNDPPV 646
Cdd:PRK10636 102 NERND---GHAIATIHGKLDAIDawtirsraaslLHGLG----FSNEQLERPV----SDFSGGWRMRLNLAQALICRSDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1310934957 647 LLMDEPTASLDARAEKQFMRSMHNVSrdRTLLIITHKMHLLN-LVDRII 694
Cdd:PRK10636 171 LLLDEPTNHLDLDAVIWLEKWLKSYQ--GTLILISHDRDFLDpIVDKII 217
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
176-460 |
5.58e-06 |
|
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: 48.71 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAI 255
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 256 GIPLE----NRSASVggMARQLGEFDSIREILT---SATITTLVDLPFALLFVLII----YLVAgdLALIPLVASLIIIg 324
Cdd:cd18557 81 RQEIAffdkHKTGEL--TSRLSSDTSVLQSAVTdnlSQLLRNILQVIGGLIILFILswklTLVL--LLVIPLLLIASKI- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 325 YTLIVQPRLKT---AIEESNKFASlkhghliESLASLESIKSYGAEGLVQKAWQQMIGHT---ANWQLRSKKLSNSVANV 398
Cdd:cd18557 156 YGRYIRKLSKEvqdALAKAGQVAE-------ESLSNIRTVRSFSAEEKEIRRYSEALDRSyrlARKKALANALFQGITSL 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 399 ANFVVQLTVVSvviLGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASALR 460
Cdd:cd18557 229 LIYLSLLLVLW---YGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASE 287
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
176-459 |
6.01e-06 |
|
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: 48.57 E-value: 6.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAF---ESLWVLAIGAGIAYLFDLVMRQ----LRSYLIDVAGKKVDIIVSS 248
Cdd:cd18554 4 TIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLtldEKVYKLFTIIGIMFFIFLILRPpveyYRQYFAQWIANKILYDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 249 RLFYKAIGIPL----ENRSASVGgmARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVaslIIIG 324
Cdd:cd18554 84 DLFDHLQKLSLryyaNNRSGEII--SRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLV---IFPF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 325 YTLIVQ---PRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGH-------TANWQLRSKKLSNS 394
Cdd:cd18554 159 YILAVKyffGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHfltralkHTRWNAKTFSAVNT 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1310934957 395 VANVANFVVQLtvvsvviLGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASAL 459
Cdd:cd18554 239 ITDLAPLLVIG-------FAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASM 296
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
612-708 |
8.88e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 612 SEGLDQQVGegghSLSRGQRQTVALARAILNDPPVLLMDEPTASLD--ARAE-KQFMRSMhnVSRDRTLLIITHKM-HLL 687
Cdd:NF040905 395 TPSVFQKVG----NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDvgAKYEiYTIINEL--AAEGKGVIVISSELpELL 468
|
90 100
....*....|....*....|.
gi 1310934957 688 NLVDRIIVMDRGHIIADGPKD 708
Cdd:NF040905 469 GMCDRIYVMNEGRITGELPRE 489
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
493-657 |
9.01e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.17 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 493 LSFSypgSEKPVLHPFALRIRPGERIAIIGRNGSGKSTLAKLLVGLFKPSNGSLRYDGIDSAQIHP---SDLRRNFGyLP 569
Cdd:PRK13541 7 LQFN---IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpycTYIGHNLG-LK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 570 QDVTLFhgsvrDNILFGTRQVTEHQLIRAvqlsGVNLF--TDLesegLDQQVgeggHSLSRGQRQTVALARAILNDPPVL 647
Cdd:PRK13541 83 LEMTVF-----ENLKFWSEIYNSAETLYA----AIHYFklHDL----LDEKC----YSLSSGMQKIVAIARLIACQSDLW 145
|
170
....*....|
gi 1310934957 648 LMDEPTASLD 657
Cdd:PRK13541 146 LLDEVETNLS 155
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-460 |
1.16e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 47.95 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVV---------------PNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGK 240
Cdd:cd18565 4 GLLASILNRLFDLAPPLLIGVAIDAVFngeasflplvpaslgPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 241 KVDIIVSSRLFYKAIGIPL---ENRSasVGGM-------ARQLGEF--DSIREILTSATITTLVdlpFALLFVLiiylvA 308
Cdd:cd18565 84 RVQHDLRTDTYDHVQRLDMaffEDRQ--TGDLmsvlnndVNQLERFldDGANSIIRVVVTVLGI---GAILFYL-----N 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 309 GDLALIPLVASLIIIGYTLIVQPRLK---TAIEESnkfASLKHGHLIESLASLESIKSYGAEGL----VQKAWQQMigHT 381
Cdd:cd18565 154 WQLALVALLPVPLIIAGTYWFQRRIEpryRAVREA---VGDLNARLENNLSGIAVIKAFTAEDFererVADASEEY--RD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 382 ANWqlRSKKLSNSVANVANFVVQLTVVSVVILGVYRVADNDISMGGIIAA------VMLASRAVAPMAQLANLM---TRA 452
Cdd:cd18565 229 ANW--RAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVgtlvtfLFYTQRLLWPLTRLGDLIdqyQRA 306
|
....*...
gi 1310934957 453 nqTASALR 460
Cdd:cd18565 307 --MASAKR 312
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
624-721 |
2.76e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 46.85 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 624 HSLSRGQRQTVALArAILNDP---PVLLMDEPTASLDARAEKQFMRSMHNVSRDRTLLIITHKMHLLNLV--DRIIVMDR 698
Cdd:COG4637 257 RELSDGTLRFLALL-AALLSPrppPLLCIEEPENGLHPDLLPALAELLREASERTQVIVTTHSPALLDALepEEVLVLER 335
|
90 100
....*....|....*....|....*.
gi 1310934957 699 ---GHIIADGPKDKVLEKLNQGLMAG 721
Cdd:COG4637 336 eddGETRIRRLSDLELPEWLEGYSLG 361
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
624-700 |
7.46e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 7.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 624 HSLSRGQRQTVALARAI----LNDPPVLLMDEPTASLDARAEKQFMRS-MHNVSRDRTLLIITHKMHLLNLVDRIIVMDR 698
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAiLEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
..
gi 1310934957 699 GH 700
Cdd:cd03227 156 VI 157
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
177-367 |
1.84e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 44.03 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 177 LIASILVNLFAlvsPLFIMNVYDKVvpNLAFESLWVLAIGA----GIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFY 252
Cdd:cd18582 5 LVLAKLLNVAV---PFLLKYAVDAL--SAPASALLAVPLLLllayGLARILSSLFNELRDALFARVSQRAVRRLALRVFR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 253 KAIGIPLE---NRSasVGGMARqlgEFD----SIREILTSATIT---TLVDlpFALLFVLIIYLVAGDLALIPLVASLII 322
Cdd:cd18582 80 HLHSLSLRfhlSRK--TGALSR---AIErgtrGIEFLLRFLLFNilpTILE--LLLVCGILWYLYGWSYALITLVTVALY 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1310934957 323 IGYTLIVQPRLKTAIEESNKFASLKHGHLIESLASLESIKSYGAE 367
Cdd:cd18582 153 VAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNE 197
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
519-694 |
4.99e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.82 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 519 AIIGRNGSGKSTLAK-LLVGLFkpsnGSLRydgidsaqihpsdLRRNFGYLPQDVTlFHGSVRDNI--LFGTRQVTEHQL 595
Cdd:cd03240 26 LIVGQNGAGKTTIIEaLKYALT----GELP-------------PNSKGGAHDPKLI-REGEVRAQVklAFENANGKKYTI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 596 IRAVqlsgvNLFTD---LESEGLDQQVGEGGHSLSRGQRQTV------ALARAILNDPPVLLMDEPTASLDA-RAEKQFM 665
Cdd:cd03240 88 TRSL-----AILENvifCHQGESNWPLLDMRGRCSGGEKVLAsliirlALAETFGSNCGILALDEPTTNLDEeNIEESLA 162
|
170 180 190
....*....|....*....|....*....|.
gi 1310934957 666 R--SMHNVSRDRTLLIITHKMHLLNLVDRII 694
Cdd:cd03240 163 EiiEERKSQKNFQLIVITHDEELVDAADHIY 193
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
625-690 |
5.12e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 5.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1310934957 625 SLSRGQRQTVALARAILNDPPVLLMDEPTASLDARAekQFMRSMHNVSRDRTLLIITHKMHLLNLV 690
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA--VLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
177-449 |
5.63e-04 |
|
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: 42.43 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 177 LIASILVNLFALVSPLFIMNVYDKVVPNLAFESLWVLAIGAGIAYLFDLVMRQLRSYLIDVAGKKVDIIVSSRLFYKAIG 256
Cdd:cd18571 8 LLGLLLGSLLQLIFPFLTQSIVDKGINNKDLNFIYLILIAQLVLFLGSTSIEFIRSWILLHISSRINISIISDFLIKLMR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 257 IPL---ENRSasVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVASLIIIGYTLIVQPRL 333
Cdd:cd18571 88 LPIsffDTKM--TGDILQRINDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYILWILLFLKKR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 334 KtaIEESNKFA--SLKHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNSVANVANFVVQLTVVSVV 411
Cdd:cd18571 166 K--KLDYKRFDlsSENQSKLIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKNILIT 243
|
250 260 270
....*....|....*....|....*....|....*...
gi 1310934957 412 ILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLM 449
Cdd:cd18571 244 FLAAKLVIDGEITLGMMLAIQYIIGQLNSPIEQLIGFI 281
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
176-459 |
7.87e-04 |
|
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: 42.01 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLA------FESLWVLAIGAGIAYLFDLVMRQLRSYLIdvagkkvdIIVSSR 249
Cdd:cd18547 4 VIILAIISTLLSVLGPYLLGKAIDLIIEGLGggggvdFSGLLRILLLLLGLYLLSALFSYLQNRLM--------ARVSQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 250 --------LFYKAIGIPL---ENRSAsvgG--MAR------QLGEF--DSIREILTSatITTLVdlpFALLFVLIIYLVa 308
Cdd:cd18547 76 tvydlrkdLFEKLQRLPLsyfDTHSH---GdiMSRvtndvdNISQAlsQSLTQLISS--ILTIV---GTLIMMLYISPL- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 309 gdLALIPLVASLIIIGYTLIVQPR-LKTAIEESNKFASLkHGHLIESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLR 387
Cdd:cd18547 147 --LTLIVLVTVPLSLLVTKFIAKRsQKYFRKQQKALGEL-NGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1310934957 388 SKKLSNSVANVANFVVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMtraNQTASAL 459
Cdd:cd18547 224 AQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQI---NSLQSAL 292
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
466-550 |
1.70e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 466 MTQEDEFENkghlVSKQRLMGKIEADDLSFSYPGSEKPVLHpFAL-----RIRPGERIAIIGRNGSGKSTLAKLLVGLFK 540
Cdd:PRK13545 1 MNYKVKFEH----VTKKYKMYNKPFDKLKDLFFRSKDGEYH-YALnnisfEVPEGEIVGIIGLNGSGKSTLSNLIAGVTM 75
|
90
....*....|
gi 1310934957 541 PSNGSLRYDG 550
Cdd:PRK13545 76 PNKGTVDIKG 85
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
176-460 |
2.75e-03 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 40.57 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 176 ALIASILVNLFALVSPLFIMNVYDKVVPNLAFESLW-----------VLAIGAGIAYLFDLVMRQLRSYLIDV----AGK 240
Cdd:cd18564 4 ALLALLLETALRLLEPWPLKVVIDDVLGDKPLPGLLglapllgpdplALLLLAAAALVGIALLRGLASYAGTYltalVGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 241 KVDIIVSSRLFYKAIGIPLE--NRSASVGGMARQLGEFDSIREILTSATITTLVDLPFALLFVLIIYLVAGDLALIPLVA 318
Cdd:cd18564 84 RVVLDLRRDLFAHLQRLSLSfhDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 319 SLIIIGYTLIVQPRLKTAIEEsnkfASLKHGHLI----ESLASLESIKSYGAEGLVQKAWQQMIGHTANWQLRSKKLSNS 394
Cdd:cd18564 164 APLLLLAARRFSRRIKEASRE----QRRREGALAsvaqESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQAL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1310934957 395 VANVANFVVQLTVVSVVILGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQ-TASALR 460
Cdd:cd18564 240 LSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKaSASAER 306
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
624-688 |
3.84e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 3.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1310934957 624 HSLSRGQRQTVALARAILNDPP---VLLMDEPTASLDARAEKQFMRSMHNVSRDRT-LLIITHKMHLLN 688
Cdd:pfam13304 235 FELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTHSPLLLD 303
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
413-459 |
4.22e-03 |
|
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: 39.77 E-value: 4.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1310934957 413 LGVYRVADNDISMGGIIAAVMLASRAVAPMAQLANLMTRANQTASAL 459
Cdd:cd18543 242 LGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAA 288
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
610-694 |
8.67e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1310934957 610 LESEGLDQ-QVGEGGHSLSRGQRQTVALARAILN---DPPVLLMDEPTASLDARAEKQFMRSMHNVS-RDRTLLIITHKM 684
Cdd:PRK00635 793 LCSLGLDYlPLGRPLSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNM 872
|
90
....*....|
gi 1310934957 685 HLLNLVDRII 694
Cdd:PRK00635 873 HVVKVADYVL 882
|
|
| |
